Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P00727
|
AMPL_BOVIN
|
MFLLPLPAAARVAVRHLSVKRLWAPGPAAADMTKGLVLGIYSKEKEEDEPQFTSAGENFNKLVSGKLREILNISGPPLKAGKTRTFYGLHEDFPSVVVVGLGKKTAGIDEQENWHEGKENIRAAVAAGCRQIQDLEIPSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKRKVVVSAKLHGSEDQEAWQRGVLFASGQNLARRLMETPANEMTPTKFAEIVEENLKSASIKTDVFIRPKSWIEEQEMGSFLSVAKGSEEPPVFLEIHYKGSPNASEPPLVFVGKGITFDSGGISIKAAANMDLMRADMGGAATICSAIVSAAKLDLPINIVGLAPLCENMPSGKANKPGDVVRARNGKTIQVDNTDAEGRLILADALCYAHTFNPKVIINAATLTGAMDIALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLFEHYTRQVIDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGVMTNKDEVPYLRKGMAGRPTRTLIEFLFRFSQDSA
|
3.4.11.1; 3.4.11.5; 3.4.13.23
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16519517}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16519517}; Note=Binds two metal ions per subunit. Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals: site 1 is occupied by Zn(2+), Mn(2+), Mg(2+) or Co(2+), while the tight binding site 2 can be occupied by only Zn(2+) or Co(2+) (PubMed:16519517). One Zn(2+) ion is tightly bound to site 2 and essential for enzyme activity in vivo, while site 1 can be occupied by different metals to give different enzymatic activities (PubMed:16519517). Mn(2+) is required for Cys-Gly hydrolysis activity (PubMed:16519517). A third metal binding site may serve a structural role, possibly stabilizing part of the interface between the N-terminal and the catalytic domain (PubMed:7619821). {ECO:0000269|PubMed:16519517, ECO:0000269|PubMed:7619821, ECO:0000303|PubMed:16519517};
|
proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]
|
carboxypeptidase activity [GO:0004180]; dipeptidase activity [GO:0016805]; disordered domain specific binding [GO:0097718]; manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; peptidase activity [GO:0008233]
|
PF00883;PF02789;
|
3.40.220.10;3.40.630.10;
|
Peptidase M17 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q68FS4}.
|
CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000269|PubMed:14583094}; CATALYTIC ACTIVITY: Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103; EC=3.4.13.23; Evidence={ECO:0000269|PubMed:14583094}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445; Evidence={ECO:0000305|PubMed:14583094}; CATALYTIC ACTIVITY: Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine; Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235, ChEBI:CHEBI:57305, ChEBI:CHEBI:61694; Evidence={ECO:0000269|PubMed:14583094}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784; Evidence={ECO:0000305|PubMed:14583094}; CATALYTIC ACTIVITY: Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:145802, ChEBI:CHEBI:145803; Evidence={ECO:0000250|UniProtKB:Q68FS4}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569; Evidence={ECO:0000250|UniProtKB:Q68FS4}; CATALYTIC ACTIVITY: Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5; Evidence={ECO:0000250|UniProtKB:P28839};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.42 mM for Cys-Gly (at pH 6.9 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=2.3 mM for Leu-Gly (at pH 6.9 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=2.8 mM for Met-Gly (at pH 6.9 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=0.57 mM for Cys-Gly (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=2.5 mM for Leu-Gly (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=1.5 mM for Met-Gly (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=5.2 mM for Ser-Gly (at pH 7.4 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=0.59 mM for Cys-Gly (at pH 8.3 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=1.5 mM for Leu-Gly (at pH 8.3 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=1.3 mM for Met-Gly (at pH 8.3 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; KM=5 mM for Ser-Gly (at pH 8.3 and 25 degrees Celsius) {ECO:0000269|PubMed:14583094}; Note=kcat is 3400 min(-1) for Cys-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 11500 min(-1) for Leu-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius). kcat is 8150 min(-1) for Met-Gly hydrolysis activity (at pH 6.9 and 25 degrees Celsius) (PubMed:14583094). kcat is 6000 min(-1) for Cys-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius). kcat is 24000 min(-1) for Leu-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius). kcat is 28100 min(-1) for Met-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius). kcat is 1000 min(-1) for Ser-Gly hydrolysis activity (at pH 7.4 and 25 degrees Celsius) (PubMed:14583094). kcat is 7100 min(-1) for Cys-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius). kcat is 40500 min(-1) for Leu-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius). kcat is 59300 min(-1) for Met-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius). kcat is 2500 min(-1) for Ser-Gly hydrolysis activity (at pH 8.3 and 25 degrees Celsius) (PubMed:14583094). {ECO:0000269|PubMed:14583094};
| null | null | null |
FUNCTION: Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides (PubMed:14583094, PubMed:16519517). The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme (PubMed:16519517). For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates (PubMed:16519517). Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status (PubMed:14583094). {ECO:0000269|PubMed:14583094, ECO:0000269|PubMed:16519517}.
|
Bos taurus (Bovine)
|
P00729
|
CBPY_YEAST
|
MKAFTSLLCGLGLSTTLAKAISLQRPLGLDKDVLLQAAEKFGLDLDLDHLLKELDSNVLDAWAQIEHLYPNQVMSLETSTKPKFPEAIKTKKDWDFVVKNDAIENYQLRVNKIKDPKILGIDPNVTQYTGYLDVEDEDKHFFFWTFESRNDPAKDPVILWLNGGPGCSSLTGLFFELGPSSIGPDLKPIGNPYSWNSNATVIFLDQPVNVGFSYSGSSGVSNTVAAGKDVYNFLELFFDQFPEYVNKGQDFHIAGESYAGHYIPVFASEILSHKDRNFNLTSVLIGNGLTDPLTQYNYYEPMACGEGGEPSVLPSEECSAMEDSLERCLGLIESCYDSQSVWSCVPATIYCNNAQLAPYQRTGRNVYDIRKDCEGGNLCYPTLQDIDDYLNQDYVKEAVGAEVDHYESCNFDINRNFLFAGDWMKPYHTAVTDLLNQDLPILVYAGDKDFICNWLGNKAWTDVLPWKYDEEFASQKVRNWTASITDEVAGEVKSYKHFTYLRVFNGGHMVPFDVPENALSMVNEWIHGGFSL
|
3.4.16.5
| null |
macroautophagy [GO:0016236]; phytochelatin biosynthetic process [GO:0046938]; zymogen activation [GO:0031638]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; fungal-type vacuole [GO:0000324]; fungal-type vacuole lumen [GO:0000328]
|
serine-type carboxypeptidase activity [GO:0004185]
|
PF05388;PF00450;
|
1.10.287.410;3.40.50.1820;
|
Peptidase S10 family
|
PTM: Enters the endoplasmic reticulum as an inactive zymogen and is modified by four N-linked core oligosaccharides, giving rise to a precursor known as P1 (67 kDa). As P1 transits through the Golgi, extension of its core oligosaccharides leads to the Golgi-modified P2 precursor (69 kDa). P2 is sorted away from secretory proteins at or beyond a late Golgi compartment and is subsequently delivered to the vacuole via a prevacuolar endosome-like compartment. Upon arrival in the vacuole, the N-terminal prosegment of P2 is cleaved by vacuolar proteases to yield the enzymatically active mature vacuolar form of CPY (61 kDa). {ECO:0000269|PubMed:348476}.; PTM: The four high mannose core N-glycans found in mature CPY are Man(11-15)GlcNAc(2) at Asn-124, Man(8-12)GlcNAc(2) at Asn-198, Man(9-14)GlcNAc(2) at Asn-279 and phosphorylated Man(12-17)GlcNAc(2) as well as Man(11-16)GlcNAc(2) at Asn-479. {ECO:0000269|PubMed:28189789}.
|
SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:23708375, ECO:0000269|PubMed:29514932}. Note=The vacuolar sorting receptor VPS10 is required for the delivery of ATG42 to the vacuole lumen. {ECO:0000269|PubMed:29514932}.
|
CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid with broad specificity.; EC=3.4.16.5; Evidence={ECO:0000269|PubMed:8679540};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.021 mM for furylacryloyl-Phe-Leu-OH {ECO:0000269|PubMed:8679540}; Note=kcat is 4900 min(-1) with furylacryloyl-Phe-Leu-OH as substrate. {ECO:0000269|PubMed:8679540};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. Active from pH 4.5 to pH 8.5. {ECO:0000269|PubMed:8679540};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:25214228};
|
FUNCTION: Vacuolar serine-type carboxypeptidase involved in degradation of small peptides (PubMed:8679540). Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate (PubMed:8679540). Also plays a role in breakdown of the autophagic body and the autophagosome-dependent protein synthesis (PubMed:29514932). Plays a key role in phytochelatin (PC) synthesis from glutathione (GSH) by cleaving the Gly from GSH and form the PC-peptides of the structure (gamma-Glu-Cys)2-Gly (PubMed:17408619). Also involved in resistance to xenobiotics via the degradation of glutathione-S-conjugates (PubMed:19897216). {ECO:0000269|PubMed:17408619, ECO:0000269|PubMed:19897216, ECO:0000269|PubMed:29514932, ECO:0000269|PubMed:8679540}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00730
|
CBPA1_BOVIN
|
MQGLLILSVLLGAALGKEDFVGHQVLRITAADEAEVQTVKELEDLEHLQLDFWRGPGQPGSPIDVRVPFPSLQAVKVFLEAHGIRYRIMIEDVQSLLDEEQEQMFASQSRARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGVWFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSPCSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKYGSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTLNNLY
|
3.4.17.1
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P15085}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15085};
|
leukotriene metabolic process [GO:0006691]; proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270]
|
PF00246;PF02244;
|
3.30.70.340;3.40.630.10;
|
Peptidase M14 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9UI42}.
|
CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.; EC=3.4.17.1; Evidence={ECO:0000250|UniProtKB:P15085}; CATALYTIC ACTIVITY: Reaction=H2O + leukotriene C4 = glycine + leukotriene F4; Xref=Rhea:RHEA:50740, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305, ChEBI:CHEBI:57973, ChEBI:CHEBI:133618; Evidence={ECO:0000269|PubMed:12729612}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50741; Evidence={ECO:0000269|PubMed:12729612};
| null | null | null | null |
FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (By similarity). Catalyzes the conversion of leukotriene C4 to leukotriene F4 via the hydrolysis of an amide bond (PubMed:12729612). {ECO:0000250|UniProtKB:P15085, ECO:0000269|PubMed:12729612}.
|
Bos taurus (Bovine)
|
P00733
|
CBPM_STRAL
|
MRPRPIRLLLTALVGAGLAFAPVSAVAAPTATASASADVGALDGCYTWSGTLSEGSSGEAVRQLQIRVAGYPGTGAQLAIDGQFGPATKAAVQRFQSAYGLAADGIAGPATFNKIYQLQDDDCTPVNFTYAELNRCNSDWSGGKVSAATARANALVTMWKLQAMRHAMGDKPITVNGGFRSVTCNSNVGGASNSRHMYGHAADLGAGSQGFCALAQAARNHGFTEILGPGYPGHNDHTHVAGGDGRFWSAPSCGI
|
3.4.17.14
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
cell wall organization [GO:0071555]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]
|
metal ion binding [GO:0046872]; zinc D-Ala-D-Ala carboxypeptidase activity [GO:0009046]
|
PF08291;PF01471;
|
3.30.1380.10;1.10.101.10;
|
Peptidase M15 family
|
PTM: The N-terminus is partially blocked as a result of the cyclization of the first two amino acids into anhydroaspartylglycine imide.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of the bond: (Ac)2-L-lysyl-D-alanyl-|-D-alanine.; EC=3.4.17.14;
| null | null | null | null |
FUNCTION: This enzyme catalyzes carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism. It effectively catalyzes the transfer of the N-alpha, N-epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N-alpha,N-epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolyzing penicillin into penicilloate at a very low rate.
|
Streptomyces albus G
|
P00734
|
THRB_HUMAN
|
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE
|
3.4.21.5
| null |
acute-phase response [GO:0006953]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; blood coagulation [GO:0007596]; cell surface receptor signaling pathway [GO:0007166]; cytolysis by host of symbiont cells [GO:0051838]; fibrinolysis [GO:0042730]; G protein-coupled receptor signaling pathway [GO:0007186]; ligand-gated ion channel signaling pathway [GO:1990806]; negative regulation of astrocyte differentiation [GO:0048712]; negative regulation of cytokine production involved in inflammatory response [GO:1900016]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of platelet activation [GO:0010544]; negative regulation of proteolysis [GO:0045861]; neutrophil-mediated killing of gram-negative bacterium [GO:0070945]; platelet activation [GO:0030168]; positive regulation of blood coagulation [GO:0030194]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of insulin secretion [GO:0032024]; positive regulation of lipid kinase activity [GO:0090218]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway [GO:1900738]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; proteolysis [GO:0006508]; regulation of blood coagulation [GO:0030193]; regulation of cell shape [GO:0008360]; regulation of cytosolic calcium ion concentration [GO:0051480]; response to wounding [GO:0009611]
|
blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; lipopolysaccharide binding [GO:0001530]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102]; thrombospondin receptor activity [GO:0070053]
|
PF00594;PF00051;PF09396;PF00089;
|
2.40.20.10;4.10.140.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin. {ECO:0000269|PubMed:3759958, ECO:0000269|PubMed:6305407}.; PTM: N-glycosylated. N-glycan heterogeneity at Asn-121: Hex3HexNAc3 (minor), Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). At Asn-143: Hex4HexNAc3 (minor) and Hex5HexNAc4 (major). {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:873923}.; PTM: In the penultimate step of the coagulation cascade, prothrombin is converted to thrombin by the prothrombinase complex composed of factor Xa (F10), cofactor Va (F5), and phospholipids. This activation requires factor Xa-catalyzed sequential cleavage at 2 sites, Arg-314 and Arg-363, along 2 possible pathways. In the first pathway, the first cleavage occurs at Arg-314, leading to the formation of the inactive intermediate prethrombin-2. This pathway preferentially occurs on platelets and in the absence of cofactor Va. In the second pathway, the first cleavage occurs at Arg-363, which separates protease domain into 2 chains that remain connected through a disulfide bond and generates the active intermediate meizothrombin. The presence of cofactor Va directs activation along the meizothrombin pathway and greatly accelerates the rate of cleavage at Arg-363, but has a smaller effect on the cleavage of meizothrombin at Arg-314. Meizothrombin accumulates as an intermediate when prothrombinase is assembled on the membrane of red blood cells. {ECO:0000305|PubMed:34265300}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
| null | null | null | null |
FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. {ECO:0000269|PubMed:2856554}.
|
Homo sapiens (Human)
|
P00735
|
THRB_BOVIN
|
MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS
|
3.4.21.5
| null |
acute-phase response [GO:0006953]; platelet activation [GO:0030168]; positive regulation of blood coagulation [GO:0030194]; protein polymerization [GO:0051258]; proteolysis [GO:0006508]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; fibrinogen binding [GO:0070051]; serine-type endopeptidase activity [GO:0004252]
|
PF00594;PF00051;PF09396;PF00089;
|
2.40.20.10;4.10.140.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential for the conversion of prothrombin to thrombin. {ECO:0000269|Ref.4}.; PTM: In the penultimate step of the coagulation cascade, prothrombin is converted to thrombin by the prothrombinase complex composed of factor Xa (F10), cofactor Va (F5), and phospholipids. This activation requires factor Xa-catalyzed sequential cleavage at 2 sites, Arg-317 and Arg-366, along 2 possible pathways. In the first pathway, the first cleavage occurs at Arg-317, leading to the formation of the inactive intermediate prethrombin-2. This pathway preferentially occurs on platelets and in the absence of cofactor Va. In the second pathway, the first cleavage occurs at Arg-366, which separates protease domain into 2 chains that remain connected through a disulfide bond and generates the active intermediate meizothrombin. The presence of cofactor Va directs activation along the meizothrombin pathway and greatly accelerates the rate of cleavage at Arg-366, but has a smaller effect on the cleavage of meizothrombin at Arg-317. Meizothrombin accumulates as an intermediate when prothrombinase is assembled on the membrane of red blood cells. {ECO:0000250|UniProtKB:P00734}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.; EC=3.4.21.5;
| null | null | null | null |
FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
P00736
|
C1R_HUMAN
|
MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED
|
3.4.21.41
| null |
complement activation, classical pathway [GO:0006958]; immune response [GO:0006955]; innate immune response [GO:0045087]; zymogen activation [GO:0031638]
|
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; molecular sequestering activity [GO:0140313]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00431;PF14670;PF00084;PF00089;
|
2.10.70.10;2.10.25.10;2.60.120.290;2.40.10.10;
|
Peptidase S1 family
|
PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:2820791}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27745832}.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).; EC=3.4.21.41;
| null | null | null | null |
FUNCTION: C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.
|
Homo sapiens (Human)
|
P00738
|
HPT_HUMAN
|
MSALGAVIALLLWGQLFAVDSGNDVTDIADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNDKKQWINKAVGDKLPECEADDGCPKPPEIAHGYVEHSVRYQCKNYYKLRTEGDGVYTLNNEKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYSQVDIGLIKLKQKVSVNERVMPICLPSKDYAEVGRVGYVSGWGRNANFKFTDHLKYVMLPVADQDQCIRHYEGSTVPEKKTPKSPVGVQPILNEHTFCAGMSKYQEDTCYGDAGSAFAVHDLEEDTWYATGILSFDKSCAVAEYGVYVKVTSIQDWVQKTIAEN
| null | null |
acute-phase response [GO:0006953]; defense response [GO:0006952]; defense response to bacterium [GO:0042742]; immune system process [GO:0002376]; negative regulation of hydrogen peroxide catabolic process [GO:2000296]; negative regulation of oxidoreductase activity [GO:0051354]; response to hydrogen peroxide [GO:0042542]
|
blood microparticle [GO:0072562]; endocytic vesicle lumen [GO:0071682]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; haptoglobin-hemoglobin complex [GO:0031838]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724]
|
antioxidant activity [GO:0016209]; hemoglobin binding [GO:0030492]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.10.70.10;2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity, and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway. {ECO:0000269|PubMed:21248165}.; FUNCTION: The uncleaved form of allele alpha-2 (2-2), known as zonulin, plays a role in intestinal permeability, allowing intercellular tight junction disassembly, and controlling the equilibrium between tolerance and immunity to non-self antigens. {ECO:0000269|PubMed:21248165}.
|
Homo sapiens (Human)
|
P00739
|
HPTR_HUMAN
|
MSDLGAVISLLLWGRQLFALYSGNDVTDISDDRFPKPPEIANGYVEHLFRYQCKNYYRLRTEGDGVYTLNDKKQWINKAVGDKLPECEAVCGKPKNPANPVQRILGGHLDAKGSFPWQAKMVSHHNLTTGATLINEQWLLTTAKNLFLNHSENATAKDIAPTLTLYVGKKQLVEIEKVVLHPNYHQVDIGLIKLKQKVLVNERVMPICLPSKNYAEVGRVGYVSGWGQSDNFKLTDHLKYVMLPVADQYDCITHYEGSTCPKWKAPKSPVGVQPILNEHTFCVGMSKYQEDTCYGDAGSAFAVHDLEEDTWYAAGILSFDKSCAVAEYGVYVKVTSIQHWVQKTIAEN
| null | null | null |
blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; spherical high-density lipoprotein particle [GO:0034366]
|
hemoglobin binding [GO:0030492]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.10.70.10;2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16778136}. Note=Secreted into blood plasma and associated with subtypes of high density lipoproteins (HDL). {ECO:0000269|PubMed:16778136}.
| null | null | null | null | null |
FUNCTION: Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF-1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribute to the clearance of cell-free hemoglobin to allow hepatic recycling of heme iron. {ECO:0000269|PubMed:16778136}.
|
Homo sapiens (Human)
|
P00740
|
FA9_HUMAN
|
MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRIIPHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
|
3.4.21.22
| null |
blood coagulation [GO:0007596]; proteolysis [GO:0006508]; zymogen activation [GO:0031638]
|
collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF14670;PF00594;PF00089;
|
4.10.740.10;2.10.25.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: Activated by factor XIa, which excises the activation peptide (PubMed:1730085, PubMed:9169594). The propeptide can also be removed by snake venom protease (PubMed:20004170, PubMed:20080729). {ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6688526}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:3857619, ECO:0000269|PubMed:8295821, ECO:0000269|PubMed:9169594}.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence={ECO:0000269|PubMed:12444082, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373};
| null | null | null | null |
FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000269|PubMed:1730085, ECO:0000269|PubMed:19846852, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0000269|PubMed:2592373, ECO:0000269|PubMed:8295821}.
|
Homo sapiens (Human)
|
P00741
|
FA9_BOVIN
|
MWCLNMIMAESPGLVTICLLGYLLSAECTVFLDRENATKILHRPKRYNSGKLEEFVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGMCKDDINSYECWCQAGFEGTNCELDATCSIKNGRCKQFCKRDTDNKVVCSCTDGYRLAEDQKSCEPAVPFPCGRVSVSHISKKLTRAETIFSNTNYENSSEAEIIWDNVTQSNQSFDEFSRVVGGEDAERGQFPWQVLLHGEIAAFCGGSIVNEKWVVTAAHCIKPGVKITVVAGEHNTEKPEPTEQKRNVIRAIPYHSYNASINKYSHDIALLELDEPLELNSYVTPICIADRDYTNIFLKFGYGYVSGWGKVFNRGRSASILQYLKVPLVDRATCLRSTKFSIYSHMFCAGYHEGGKDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
|
3.4.21.22
| null |
blood coagulation [GO:0007596]; proteolysis [GO:0006508]; zymogen activation [GO:0031638]
|
endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; magnesium ion binding [GO:0000287]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF14670;PF00594;PF00089;
|
4.10.740.10;2.10.25.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease. {ECO:0000250|UniProtKB:P00740}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6688526}.; PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro. {ECO:0000250|UniProtKB:P00740}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12695512}.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence={ECO:0000269|PubMed:6782101};
| null | null | null | null |
FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000269|PubMed:6782101}.
|
Bos taurus (Bovine)
|
P00742
|
FA10_HUMAN
|
MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRKRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEVITSSPLK
|
3.4.21.6
| null |
blood coagulation [GO:0007596]; positive regulation of cell migration [GO:0030335]; positive regulation of leukocyte chemotaxis [GO:0002690]; positive regulation of TOR signaling [GO:0032008]; proteolysis [GO:0006508]
|
endoplasmic reticulum lumen [GO:0005788]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; phospholipid binding [GO:0005543]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF14670;PF00594;PF00089;
|
4.10.740.10;2.10.25.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8243461}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (PubMed:8920993). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity). {ECO:0000250|UniProtKB:P00743, ECO:0000269|PubMed:8920993}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6871167}.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6;
| null | null | null | null |
FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
|
Homo sapiens (Human)
|
P00743
|
FA10_BOVIN
|
MAGLLHLVLLSTALGGLLRPAGSVFLPRDQAHRVLQRARRANSFLEEVKQGNLERECLEEACSLEEAREVFEDAEQTDEFWSKYKDGDQCEGHPCLNQGHCKDGIGDYTCTCAEGFEGKNCEFSTREICSLDNGGCDQFCREERSEVRCSCAHGYVLGDDSKSCVSTERFPCGKFTQGRSRRWAIHTSEDALDASELEHYDPADLSPTESSLDLLGLNRTEPSAGEDGSQVVRIVGGRDCAEGECPWQALLVNEENEGFCGGTILNEFYVLTAAHCLHQAKRFTVRVGDRNTEQEEGNEMAHEVEMTVKHSRFVKETYDFDIAVLRLKTPIRFRRNVAPACLPEKDWAEATLMTQKTGIVSGFGRTHEKGRLSSTLKMLEVPYVDRSTCKLSSSFTITPNMFCAGYDTQPEDACQGDSGGPHVTRFKDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIDKIMKARAGAAGSRGHSEAPATWTVPPPLPL
|
3.4.21.6
| null |
blood coagulation [GO:0007596]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF14670;PF00594;PF00089;
|
4.10.740.10;2.10.25.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1059093, ECO:0000269|PubMed:8243461}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (By similarity). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (PubMed:1059122). {ECO:0000250|UniProtKB:P00742, ECO:0000269|PubMed:1059122}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6688526}.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6;
| null | null | null | null |
FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
|
Bos taurus (Bovine)
|
P00745
|
PROC_BOVIN
|
XTSLLLFVTIWGISSTPAPPDSVFSSSQRAHQVLRIRKRANSFLEELRPGNVERECSEEVCEFEEAREIFQNTEDTMAFWSFYSDGDQCEDRPSGSPCDLPCCGRGKCIDGLGGFRCDCAEGWEGRFCLHEVRFSNCSAENGGCAHYCMEEEGRRHCSCAPGYRLEDDHQLCVSKVTFPCGRLGKRMEKKRKTLKRDTNQVDQKDQLDPRIVDGQEAGWGESPWQAVLLDSKKKLVCGAVLIHVSWVLTVAHCLDSRKKLIVRLGEYDMRRWESWEVDLDIKEVIIHPNYTKSTSDNDIALLRLAKPATLSQTIVPICLPDSGLSERKLTQVGQETVVTGWGYRDETKRNRTFVLSFIKVPVVPYNACVHAMENKISENMLCAGILGDPRDACEGDSGGPMVTFFRGTWFLVGLVSWGEGCGRLYNYGVYTKVSRYLDWIYGHIKAQEAPLESQVP
|
3.4.21.69
| null |
blood coagulation [GO:0007596]; negative regulation of apoptotic process [GO:0043066]; negative regulation of blood coagulation [GO:0030195]; negative regulation of coagulation [GO:0050819]; negative regulation of inflammatory response [GO:0050728]; positive regulation of establishment of endothelial barrier [GO:1903142]; proteolysis [GO:0006508]
|
endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]
|
calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF14670;PF00594;PF00089;
|
4.10.740.10;2.10.25.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:6896876}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04070}. Golgi apparatus {ECO:0000250|UniProtKB:P04070}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04070}.
|
CATALYTIC ACTIVITY: Reaction=Degradation of blood coagulation factors Va and VIIIa.; EC=3.4.21.69;
| null | null | null | null |
FUNCTION: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function. {ECO:0000250|UniProtKB:P04070}.
|
Bos taurus (Bovine)
|
P00746
|
CFAD_HUMAN
|
MHSWERLAVLVLLGAAACAAPPRGRILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSLSQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPGTLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCKGDSGGPLVCGGVLEGVVTSGSRVCGNRKKPGIYTRVASYAAWIDSVLA
|
3.4.21.46
| null |
complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; proteolysis [GO:0006508]; response to bacterium [GO:0009617]
|
extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; platelet alpha granule lumen [GO:0031093]; secretory granule lumen [GO:0034774]
|
serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.; EC=3.4.21.46;
| null | null | null | null |
FUNCTION: Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
|
Homo sapiens (Human)
|
P00747
|
PLMN_HUMAN
|
MEHKEVVLLLLLFLKSGQGEPLDDYVNTQGASLFSVTKKQLGAGSIEECAAKCEEDEEFTCRAFQYHSKEQQCVIMAENRKSSIIIRMRDVVLFEKKVYLSECKTGNGKNYRGTMSKTKNGITCQKWSSTSPHRPRFSPATHPSEGLEENYCRNPDNDPQGPWCYTTDPEKRYDYCDILECEEECMHCSGENYDGKISKTMSGLECQAWDSQSPHAHGYIPSKFPNKNLKKNYCRNPDRELRPWCFTTDPNKRWELCDIPRCTTPPPSSGPTYQCLKGTGENYRGNVAVTVSGHTCQHWSAQTPHTHNRTPENFPCKNLDENYCRNPDGKRAPWCHTTNSQVRWEYCKIPSCDSSPVSTEQLAPTAPPELTPVVQDCYHGDGQSYRGTSSTTTTGKKCQSWSSMTPHRHQKTPENYPNAGLTMNYCRNPDADKGPWCFTTDPSVRWEYCNLKKCSGTEASVVAPPPVVLLPDVETPSEEDCMFGNGKGYRGKRATTVTGTPCQDWAAQEPHRHSIFTPETNPRAGLEKNYCRNPDGDVGGPWCYTTNPRKLYDYCDVPQCAAPSFDCGKPQVEPKKCPGRVVGGCVAHPHSWPWQVSLRTRFGMHFCGGTLISPEWVLTAAHCLEKSPRPSSYKVILGAHQEVNLEPHVQEIEVSRLFLEPTRKDIALLKLSSPAVITDKVIPACLPSPNYVVADRTECFITGWGETQGTFGAGLLKEAQLPVIENKVCNRYEFLNGRVQSTELCAGHLAGGTDSCQGDSGGPLVCFEKDKYILQGVTSWGLGCARPNKPGVYVRVSRFVTWIEGVMRNN
|
3.4.21.7
| null |
biological process involved in interaction with symbiont [GO:0051702]; blood coagulation [GO:0007596]; extracellular matrix disassembly [GO:0022617]; fibrinolysis [GO:0042730]; labyrinthine layer blood vessel development [GO:0060716]; mononuclear cell migration [GO:0071674]; muscle cell cellular homeostasis [GO:0046716]; myoblast differentiation [GO:0045445]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-cell adhesion mediated by cadherin [GO:2000048]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of fibrinolysis [GO:0051918]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of fibrinolysis [GO:0051919]; proteolysis [GO:0006508]; tissue regeneration [GO:0042246]; tissue remodeling [GO:0048771]; trans-synaptic signaling by BDNF, modulating synaptic transmission [GO:0099183]; trophoblast giant cell differentiation [GO:0060707]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; Schaffer collateral - CA1 synapse [GO:0098685]
|
apolipoprotein binding [GO:0034185]; endopeptidase activity [GO:0004175]; enzyme binding [GO:0019899]; kinase binding [GO:0019900]; protease binding [GO:0002020]; protein antigen binding [GO:1990405]; protein domain specific binding [GO:0019904]; protein-folding chaperone binding [GO:0051087]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; signaling receptor binding [GO:0005102]
|
PF00051;PF00024;PF00089;
|
3.50.4.10;2.40.20.10;2.40.10.10;
|
Peptidase S1 family, Plasminogen subfamily
|
PTM: N-linked glycan contains N-acetyllactosamine and sialic acid. O-linked glycans consist of Gal-GalNAc disaccharide modified with up to 2 sialic acid residues (microheterogeneity). {ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:3356193, ECO:0000269|PubMed:9054441}.; PTM: In the presence of the inhibitor, the activation involves only cleavage after Arg-580, yielding two chains held together by two disulfide bonds. In the absence of the inhibitor, the activation involves additionally the removal of the activation peptide. {ECO:0000269|PubMed:14699093, ECO:0000269|PubMed:9548733}.; PTM: (Microbial infection) The Y.pestis Pla protein cleaves between Arg-580 and Val-581, generating plasmin which facilitates bacterial migration and infection (PubMed:22645135). {ECO:0000269|PubMed:22645135}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:14699093}. Note=Locates to the cell surface where it is proteolytically cleaved to produce the active plasmin. Interaction with HRG tethers it to the cell surface.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin. Converts fibrin into soluble products.; EC=3.4.21.7; Evidence={ECO:0000269|PubMed:2143188};
| null | null | null | null |
FUNCTION: Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1 and C5. Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells. {ECO:0000269|PubMed:14699093}.; FUNCTION: Angiostatin is an angiogenesis inhibitor that blocks neovascularization and growth of experimental primary and metastatic tumors in vivo. {ECO:0000269|PubMed:14699093}.; FUNCTION: (Microbial infection) ENO/enoloase from parasite P.falciparum (strain NF54) interacts with PLG present in the mosquito blood meal to promote the invasion of the mosquito midgut by the parasite ookinete (PubMed:21949403). The catalytic active form, plasmin, is essential for the invasion of the mosquito midgut (PubMed:21949403). {ECO:0000269|PubMed:21949403}.; FUNCTION: (Microbial infection) Binds to OspC on the surface of B.burgdorferi cells, possibly conferring an extracellular protease activity on the bacteria that allows it to traverse host tissue. {ECO:0000269|PubMed:22433849}.
|
Homo sapiens (Human)
|
P00748
|
FA12_HUMAN
|
MRALLLLGFLLVSLESTLSIPPWEAPKEHKYKAEEHTVVLTVTGEPCHFPFQYHRQLYHKCTHKGRPGPQPWCATTPNFDQDQRWGYCLEPKKVKDHCSKHSPCQKGGTCVNMPSGPHCLCPQHLTGNHCQKEKCFEPQLLRFFHKNEIWYRTEQAAVARCQCKGPDAHCQRLASQACRTNPCLHGGRCLEVEGHRLCHCPVGYTGAFCDVDTKASCYDGRGLSYRGLARTTLSGAPCQPWASEATYRNVTAEQARNWGLGGHAFCRNPDNDIRPWCFVLNRDRLSWEYCDLAQCQTPTQAAPPTPVSPRLHVPLMPAQPAPPKPQPTTRTPPQSQTPGALPAKREQPPSLTRNGPLSCGQRLRKSLSSMTRVVGGLVALRGAHPYIAALYWGHSFCAGSLIAPCWVLTAAHCLQDRPAPEDLTVVLGQERRNHSCEPCQTLAVRSYRLHEAFSPVSYQHDLALLRLQEDADGSCALLSPYVQPVCLPSGAARPSETTLCQVAGWGHQFEGAEEYASFLQEAQVPFLSLERCSAPDVHGSSILPGMLCAGFLEGGTDACQGDSGGPLVCEDQAAERRLTLQGIISWGSGCGDRNKPGVYTDVAYYLAWIREHTVS
|
3.4.21.38
| null |
blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; Factor XII activation [GO:0002542]; fibrinolysis [GO:0042730]; innate immune response [GO:0045087]; plasma kallikrein-kinin cascade [GO:0002353]; positive regulation of blood coagulation [GO:0030194]; positive regulation of fibrinolysis [GO:0051919]; positive regulation of plasminogen activation [GO:0010756]; protein autoprocessing [GO:0016540]; protein processing [GO:0016485]; response to misfolded protein [GO:0051788]; zymogen activation [GO:0031638]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; rough endoplasmic reticulum [GO:0005791]
|
calcium ion binding [GO:0005509]; misfolded protein binding [GO:0051787]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF00039;PF00040;PF00051;PF00089;
|
2.10.10.10;2.10.25.10;2.40.20.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: Factor XII is activated by kallikrein in alpha-factor XIIa, which is further converted by trypsin into beta-factor XIIa. Alpha-factor XIIa is composed of an NH2-terminal heavy chain, called coagulation factor XIIa heavy chain, and a COOH-terminal light chain, called coagulation factor XIIa light chain, connected by a disulfide bond. Beta-factor XIIa is composed of 2 chains linked by a disulfide bond, an N-terminal nonapeptide, called beta-factor XIIa part 1, and coagulation factor XIIa light chain, also known in this context as beta-factor XIIa part 2.; PTM: O- and N-glycosylated. The O-linked polysaccharides were not identified, but are probably the mucin type linked to GalNAc. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:1544894, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:3886654}.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.; EC=3.4.21.38;
| null | null | null | null |
FUNCTION: Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa. {ECO:0000269|PubMed:21304106}.
|
Homo sapiens (Human)
|
P00749
|
UROK_HUMAN
|
MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRRRPWCYVQVGLKLLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIRSHTKEENGLAL
|
3.4.21.73
| null |
blood coagulation [GO:0007596]; chemotaxis [GO:0006935]; fibrinolysis [GO:0042730]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of plasminogen activation [GO:0010757]; plasminogen activation [GO:0031639]; positive regulation of cell migration [GO:0030335]; proteolysis [GO:0006508]; regulation of cell adhesion [GO:0030155]; regulation of cell adhesion mediated by integrin [GO:0033628]; regulation of cell population proliferation [GO:0042127]; regulation of fibrinolysis [GO:0051917]; regulation of plasminogen activation [GO:0010755]; regulation of signaling receptor activity [GO:0010469]; regulation of smooth muscle cell migration [GO:0014910]; regulation of smooth muscle cell-matrix adhesion [GO:2000097]; regulation of wound healing [GO:0061041]; response to hypoxia [GO:0001666]; signal transduction [GO:0007165]; smooth muscle cell migration [GO:0014909]; urokinase plasminogen activator signaling pathway [GO:0038195]
|
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; protein complex involved in cell-matrix adhesion [GO:0098637]; serine protease inhibitor complex [GO:0097180]; serine-type endopeptidase complex [GO:1905370]; specific granule membrane [GO:0035579]; tertiary granule membrane [GO:0070821]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00051;PF00089;
|
2.10.25.10;2.40.20.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: Phosphorylation of Ser-158 and Ser-323 abolishes proadhesive ability but does not interfere with receptor binding. {ECO:0000269|PubMed:9151681}.; PTM: Produced as an inactive single-chain protein (pro-uPA or sc-uPA), is processed into the active disulfide-linked two-chain form of PLAU/uPA by a proteolytic event mediated, at least, by TMPRSS4. {ECO:0000269|PubMed:24434139}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24434139}.
|
CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.73;
| null | null | null | null |
FUNCTION: Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.
|
Homo sapiens (Human)
|
P00750
|
TPA_HUMAN
|
MDAMKRGLCCVLLLCGAVFVSPSQEIHARFRRGARSYQVICRDEKTQMIYQQHQSWLRPVLRSNRVEYCWCNSGRAQCHSVPVKSCSEPRCFNGGTCQQALYFSDFVCQCPEGFAGKCCEIDTRATCYEDQGISYRGTWSTAESGAECTNWNSSALAQKPYSGRRPDAIRLGLGNHNYCRNPDRDSKPWCYVFKAGKYSSEFCSTPACSEGNSDCYFGNGSAYRGTHSLTESGASCLPWNSMILIGKVYTAQNPSAQALGLGKHNYCRNPDGDAKPWCHVLKNRRLTWEYCDVPSCSTCGLRQYSQPQFRIKGGLFADIASHPWQAAIFAKHRRSPGERFLCGGILISSCWILSAAHCFQERFPPHHLTVILGRTYRVVPGEEEQKFEVEKYIVHKEFDDDTYDNDIALLQLKSDSSRCAQESSVVRTVCLPPADLQLPDWTECELSGYGKHEALSPFYSERLKEAHVRLYPSSRCTSQHLLNRTVTDNMLCAGDTRSGGPQANLHDACQGDSGGPLVCLNDGRMTLVGIISWGLGCGQKDVPGVYTKVTNYLDWIRDNMRP
|
3.4.21.68
| null |
blood coagulation [GO:0007596]; fibrinolysis [GO:0042730]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of plasminogen activation [GO:0010757]; negative regulation of proteolysis [GO:0045861]; plasminogen activation [GO:0031639]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; prevention of polyspermy [GO:0060468]; protein modification process [GO:0036211]; proteolysis [GO:0006508]; response to hypoxia [GO:0001666]; smooth muscle cell migration [GO:0014909]; trans-synaptic signaling by BDNF, modulating synaptic transmission [GO:0099183]
|
apical part of cell [GO:0045177]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Schaffer collateral - CA1 synapse [GO:0098685]; secretory granule [GO:0030141]; serine protease inhibitor complex [GO:0097180]
|
phosphoprotein binding [GO:0051219]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102]
|
PF00008;PF00039;PF00051;PF00089;
|
2.10.70.10;2.10.25.10;2.40.20.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The single chain, almost fully active enzyme, can be further processed into a two-chain fully active form by a cleavage after Arg-310 catalyzed by plasmin, tissue kallikrein or factor Xa.; PTM: Differential cell-specific N-linked glycosylation gives rise to two glycoforms, type I (glycosylated at Asn-219) and type II (not glycosylated at Asn-219). The single chain type I glycoform is less readily converted into the two-chain form by plasmin, and the two-chain type I glycoform has a lower activity than the two-chain type II glycoform in the presence of fibrin. {ECO:0000269|PubMed:1900431}.; PTM: N-glycosylation of Asn-152; the bound oligomannosidic glycan is involved in the interaction with the mannose receptor. {ECO:0000269|PubMed:1900431}.; PTM: Characterization of O-linked glycan was studied in Bowes melanoma cell line. {ECO:0000269|PubMed:1900431}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin.; EC=3.4.21.68;
| null | null | null | null |
FUNCTION: Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy (By similarity). {ECO:0000250|UniProtKB:P19637}.
|
Homo sapiens (Human)
|
P00751
|
CFAB_HUMAN
|
MGSNLSPQLCLMPFILGLLSGGVTTTPWSLARPQGSCSLEGVEIKGGSFRLLQEGQALEYVCPSGFYPYPVQTRTCRSTGSWSTLKTQDQKTVRKAECRAIHCPRPHDFENGEYWPRSPYYNVSDEISFHCYDGYTLRGSANRTCQVNGRWSGQTAICDNGAGYCSNPGIPIGTRKVGSQYRLEDSVTYHCSRGLTLRGSQRRTCQEGGSWSGTEPSCQDSFMYDTPQEVAEAFLSSLTETIEGVDAEDGHGPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGASNFTGAKKCLVNLIEKVASYGVKPRYGLVTYATYPKIWVKVSEADSSNADWVTKQLNEINYEDHKLKSGTNTKKALQAVYSMMSWPDDVPPEGWNRTRHVIILMTDGLHNMGGDPITVIDEIRDLLYIGKDRKNPREDYLDVYVFGVGPLVNQVNINALASKKDNEQHVFKVKDMENLEDVFYQMIDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAHCFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVYIKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVHKRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL
|
3.4.21.47
| null |
complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; proteolysis [GO:0006508]; response to bacterium [GO:0009617]
|
blood microparticle [GO:0072562]; classical-complement-pathway C3/C5 convertase complex [GO:0005601]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
complement binding [GO:0001848]; serine-type endopeptidase activity [GO:0004252]
|
PF00084;PF00089;PF00092;
|
2.40.10.120;2.10.70.10;3.40.50.410;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b.; EC=3.4.21.47;
| null | null | null | null |
FUNCTION: Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes.
|
Homo sapiens (Human)
|
P00752
|
KLK_PIG
|
APPIQSRIIGGRECEKNSHPWQVAIYHYSSFQCGGVLVNPKWVLTAAHCKNDNYEVWLGRHNLFENENTAQFFGVTADFPHPGFNLSLLKXHTKADGKDYSHDLMLLRLQSPAKITDAVKVLELPTQEPELGSTCEASGWGSIEPGPDBFEFPDEIQCVQLTLLQNTFCABAHPBKVTESMLCAGYLPGGKDTCMGDSGGPLICNGMWQGITSWGHTPCGSANKPSIYTKLIFYLDWINDTITENP
|
3.4.21.35
| null |
regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638]
|
secretory granule [GO:0030141]
|
serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35;
| null | null | null | null |
FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
|
Sus scrofa (Pig)
|
P00755
|
K1KB1_MOUSE
|
MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYKEYICGGVLLDANWVLTAAHCYYEKNNVWLGKNNLYQDEPSAQHRLVSKSFLHPCYNMSLHRNRIQNPQDDYSYDLMLLRLSKPADITDVVKPIALPTEEPKLGSTCLASGWGSIIPVKFQYAKDLQCVNLKLLPNEDCDKAYVQKVTDVMLCAGVKGGGKDTCKGDSGGPLICDGVLQGLTSWGYNPCGEPKKPGVYTKLIKFTSWIKDTLAQNP
|
3.4.21.35
| null |
bradykinin biosynthetic process [GO:0002936]; cardiac muscle contraction [GO:0060048]; left ventricular cardiac muscle tissue morphogenesis [GO:0003220]; regulation of systemic arterial blood pressure [GO:0003073]; tissue kallikrein-kinin cascade [GO:0002255]; vasodilation [GO:0042311]; zymogen activation [GO:0031638]
|
acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141]
|
endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35;
| null | null | null | null |
FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
|
Mus musculus (Mouse)
|
P00756
|
K1KB3_MOUSE
|
MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYTQYLCGGVLLDPNWVLTAAHCYDDNYKVWLGKNNLFKDEPSAQHRFVSKAIPHPGFNMSLMRKHIRFLEYDYSNDLMLLRLSKPADITDTVKPITLPTEEPKLGSTCLASGWGSITPTKFQFTDDLYCVNLKLLPNEDCAKAHIEKVTDAMLCAGEMDGGKDTCKGDSGGPLICDGVLQGITSWGHTPCGEPDMPGVYTKLNKFTSWIKDTMAKNP
|
3.4.21.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per 7S complex. The Zn(2+) ions are bound at the alpha-gamma interfaces.;
|
regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638]
|
acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141]
|
endopeptidase activity [GO:0004175]; growth factor activity [GO:0008083]; metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35;
| null | null | null | null |
FUNCTION: 7S NGF alpha chain stabilizes the 7S complex. The beta dimer promotes neurite growth. The gamma chain is an arginine-specific protease; it may also have plasminogen activator activity, as well as mitogenic activity for chick embryo fibroblasts.
|
Mus musculus (Mouse)
|
P00757
|
K1KB4_MOUSE
|
MWFLILFLALSLGGIDAAPPVQSQVDCENSQPWHVAVYRFNKYQCGGVLLDRNWVLTAAHCYNDKYQVWLGKNNFLEDEPSDQHRLVSKAIPHPDFNMSLLNEHTPQPEDDYSNDLMLLRLSKPADITDVVKPITLPTEEPKLGSTCLASGWGSTTPIKFKYPDDLQCVNLKLLPNEDCDKAHEMKVTDAMLCAGEMDGGSYTCEHDSGGPLICDGILQGITSWGPEPCGEPTEPSVYTKLIKFSSWIRETMANNP
| null |
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per 7S complex. The Zn(2+) ions are bound at the alpha-gamma interfaces.;
|
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; regulation of systemic arterial blood pressure [GO:0003073]; small GTPase-mediated signal transduction [GO:0007264]; zymogen activation [GO:0031638]
|
acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141]
|
endopeptidase activity [GO:0004175]; growth factor activity [GO:0008083]; metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
|
PTM: The presence of Gln-24 prevents cleavage of the activation peptide, which remains attached at the amino end of the mature alpha chain.
| null | null | null | null | null | null | null |
Mus musculus (Mouse)
|
P00759
|
KLK2_RAT
|
MWLQILSLVLSVGRIDAAPPGQSRIVGGYKCEKNSQPWQVAVINEYLCGGVLIDPSWVITAAHCYSNNYQVLLGRNNLFKDEPFAQRRLVRQSFRHPDYIPLIVTNDTEQPVHDHSNDLMLLHLSEPADITGGVKVIDLPTKEPKVGSTCLASGWGSTNPSEMVVSHDLQCVNIHLLSNEKCIETYKDNVTDVMLCAGEMEGGKDTCAGDSGGPLICDGVLQGITSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP
|
3.4.21.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638]
|
secretory granule [GO:0030141]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Kallikrein subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35;
| null | null | null | null |
FUNCTION: This protein has both trypsin- and chymotrypsin-like activities, being able to release angiotensin II from angiotensin I or angiotensinogen.
|
Rattus norvegicus (Rat)
|
P00760
|
TRY1_BOVIN
|
MKTFIFLALLGAAVAFPVDDDDKIVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN
|
3.4.21.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
|
digestion [GO:0007586]; proteolysis [GO:0006508]
|
extracellular space [GO:0005615]; serine protease inhibitor complex [GO:0097180]
|
endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; serpin family protein binding [GO:0097655]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
|
PTM: Autocatalytic cleavage after Lys-23 leads to beta-trypsin by releasing a terminal hexapeptide. Subsequent cleavage after Lys-148 leads to alpha-trypsin. Further cleavage after Lys-193 yields pseudotrypsin. A cleavage may also occur after Arg-122.; PTM: Not sulfated on tyrosine residue(s).
|
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
| null | null | null | null | null |
Bos taurus (Bovine)
|
P00761
|
TRYP_PIG
|
FPTDDDDKIVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRLGEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRVATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKSSYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQKNKPGVYTKVCNYVNWIQQTIAAN
|
3.4.21.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
|
digestion [GO:0007586]; proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
| null | null | null | null | null |
Sus scrofa (Pig)
|
P00762
|
TRY1_RAT
|
MSALLILALVGAAVAFPLEDDDKIVGGYTCPEHSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGDEQFINAAKIIKHPNYSSWTLNNDIMLIKLSSPVKLNARVAPVALPSACAPAGTQCLISGWGNTLSNGVNNPDLLQCVDAPVLSQADCEAAYPGEITSSMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCALPDNPGVYTKVCNFVGWIQDTIAAN
|
3.4.21.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
|
digestion [GO:0007586]; proteolysis [GO:0006508]; response to caffeine [GO:0031000]; response to nicotine [GO:0035094]; response to nutrient [GO:0007584]; response to organic substance [GO:0010033]
|
extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
| null | null | null | null | null |
Rattus norvegicus (Rat)
|
P00763
|
TRY2_RAT
|
MRALLFLALVGAAVAFPVDDDDKIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
|
3.4.21.4
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.;
|
collagen catabolic process [GO:0030574]; digestion [GO:0007586]; proteolysis [GO:0006508]; response to nutrient [GO:0007584]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4;
| null | null | null | null | null |
Rattus norvegicus (Rat)
|
P00772
|
CELA1_PIG
|
MLRLLVVASLVLYGHSTQDFPETNARVVGGTEAQRNSWPSQISLQYRSGSSWAHTCGGTLIRQNWVMTAAHCVDRELTFRVVVGEHNLNQNDGTEQYVGVQKIVVHPYWNTDDVAAGYDIALLRLAQSVTLNSYVQLGVLPRAGTILANNSPCYITGWGLTRTNGQLAQTLQQAYLPTVDYAICSSSSYWGSTVKNSMVCAGGDGVRSGCQGDSGGPLHCLVNGQYAVHGVTSFVSRLGCNVTRKPTVFTRVSAYISWINNVIASN
|
3.4.21.36
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:7656008};
|
proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Elastase subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:4578945, ECO:0000269|PubMed:5415108}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.; EC=3.4.21.36; Evidence={ECO:0000269|PubMed:5415108};
| null | null | null | null |
FUNCTION: Serine proteases that hydrolyze many proteins in addition to elastin. {ECO:0000269|PubMed:5415108}.
|
Sus scrofa (Pig)
|
P00773
|
CELA1_RAT
|
MLRFLVFASLVLYGHSTQDFPETNARVVGGAEARRNSWPSQISLQYLSGGSWYHTCGGTLIRRNWVMTAAHCVSSQMTFRVVVGDHNLSQNDGTEQYVSVQKIMVHPTWNSNNVAAGYDIALLRLAQSVTLNNYVQLAVLPQEGTILANNNPCYITGWGRTRTNGQLSQTLQQAYLPSVDYSICSSSSYWGSTVKTTMVCAGGDGVRSGCQGDSGGPLHCLVNGQYSVHGVTSFVSSMGCNVSKKPTVFTRVSAYISWMNNVIAYT
|
3.4.21.36
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P00772}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P00772};
|
digestive system development [GO:0055123]; elastin catabolic process [GO:0060309]; exocrine pancreas development [GO:0031017]; inflammatory response [GO:0006954]; multicellular organism growth [GO:0035264]; negative regulation of transcription by RNA polymerase II [GO:0000122]; pancreas morphogenesis [GO:0061113]; positive regulation of angiogenesis [GO:0045766]; positive regulation of transcription by RNA polymerase II [GO:0045944]; post-embryonic development [GO:0009791]; proteolysis [GO:0006508]; regulation of cell differentiation [GO:0045595]; regulation of cell population proliferation [GO:0042127]; tissue remodeling [GO:0048771]; transcription by RNA polymerase II [GO:0006366]; Wnt signaling pathway [GO:0016055]
|
extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00089;
|
2.40.10.10;
|
Peptidase S1 family, Elastase subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00772}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.; EC=3.4.21.36; Evidence={ECO:0000250|UniProtKB:Q91X79};
| null | null | null | null |
FUNCTION: Serine proteases that hydrolyze many proteins in addition to elastin. {ECO:0000250|UniProtKB:Q91X79}.
|
Rattus norvegicus (Rat)
|
P00777
|
PRTB_STRGR
|
MRIKRTSNRSNAARRVRTTAVLAGLAAVAALAVPTANAETPRTFSANQLTAASDAVLGADIAGTAWNIDPQSKRLVVTVDSTVSKAEINQIKKSAGANADALRIERTPGKFTKLISGGDAIYSSTGRCSLGFNVRSGSTYYFLTAGHCTDGATTWWANSARTTVLGTTSGSSFPNNDYGIVRYTNTTIPKDGTVGGQDITSAANATVGMAVTRRGSTTGTHSGSVTALNATVNYGGGDVVYGMIRTNVCAEPGDSGGPLYSGTRAIGLTSGGSGNCSSGGTTFFQPVTEALSAYGVSVY
|
3.4.21.81
| null |
proteolysis [GO:0006508]
|
extracellular region [GO:0005576]
|
serine-type endopeptidase activity [GO:0004252]
|
PF02983;PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with trypsin-like specificity.; EC=3.4.21.81;
| null | null | null | null |
FUNCTION: Has a primary specificity for large aliphatic or aromatic amino acids.
|
Streptomyces griseus
|
P00780
|
SUBC_BACLI
|
MMRKKSFWLGMLTAFMLVFTMAFSDSASAAQPAKNVEKDYIVGFKSGVKTASVKKDIIKESGGKVDKQFRIINAAKAKLDKEALKEVKNDPDVAYVEEDHVAHALAQTVPYGIPLIKADKVQAQGFKGANVKVAVLDTGIQASHPDLNVVGGASFVAGEAYNTDGNGHGTHVAGTVAALDNTTGVLGVAPSVSLYAVKVLNSSGSGSYSGIVSGIEWATTNGMDVINMSLGGASGSTAMKQAVDNAYAKGVVVVAAAGNSGSSGNTNTIGYPAKYDSVIAVGAVDSNSNRASFSSVGAELEVMAPGAGVYSTYPTNTYATLNGTSMASPHVAGAAALILSKHPNLSASQVRNRLSSTATYLGSSFYYGKGLINVEAAAQ
|
3.4.21.62
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:8512925}; Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:8512925};
|
proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF05922;PF00082;
|
3.30.70.80;3.40.50.200;
|
Peptidase S8 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11109488}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for Suc-Ala(2)-Ala-pNA {ECO:0000269|Ref.4}; KM=0.79 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269|Ref.4}; KM=0.851 mM for Suc-Ala(2)-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.22 mM for MeO-Suc-Ala(2)-Phe-pNA {ECO:0000269|Ref.4}; KM=5.6 mM for Suc-Gly(2)-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.334 mM for Suc-Ala(2)-Pro-Phe-pNA {ECO:0000269|PubMed:11109488}; KM=0.062 mM for Suc-Ala(2)-Pro-Leu-pNA {ECO:0000269|PubMed:11109488}; KM=0.422 mM for Suc-Ala(2)-Pro-Arg-pNA {ECO:0000269|PubMed:11109488}; KM=0.245 mM for Suc-Ala(2)-Pro-Glu-pNA {ECO:0000269|PubMed:11109488}; KM=0.042 mM for Suc-Ala-Glu-Pro-Phe-pNA {ECO:0000269|PubMed:11109488}; Note=kcat is 1.6 sec(-1) with Suc-Ala(2)-Ala-pNA as substrate. kcat is 57 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 97 sec(-1) with MeO-Suc-Ala(2)-Phe-pNA as substrate (Ref.4). kcat is 0.990 sec(-1) with Suc-Gly(2)-Phe-pNA as substrate. kcat is 20.3 sec(-1) with Suc-Ala(2)-Phe-pNA as substrate. kcat is 646 sec(-1) with Suc-Ala(2)-Pro-Phe-pNA as substrate. kcat is 137 sec(-1) with Suc-Ala(2)-Pro-Leu-pNA as substrate. kcat is 5.31 sec(-1) with Suc-Ala(2)-Pro-Arg-pNA as substrate. kcat is 1.92 sec(-1) with Suc-Ala(2)-Pro-Glu-pNA as substrate. kcat is 375 sec(-1) with Suc-Ala-Glu-Pro-Phe-pNA as substrate (PubMed:11109488). {ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4};
| null | null | null |
FUNCTION: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (PubMed:11109488, Ref.4). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488). {ECO:0000269|PubMed:11109488, ECO:0000269|Ref.4}.
|
Bacillus licheniformis
|
P00782
|
SUBT_BACAM
|
MRGKKVWISLLFALALIFTMAFGSTSSAQAAGKSNGEKKYIVGFKQTMSTMSAAKKKDVISEKGGKVQKQFKYVDAASATLNEKAVKELKKDPSVAYVEEDHVAHAYAQSVPYGVSQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLKVAGGASMVPSETNPFQDNNSHGTHVAGTVAALNNSIGVLGVAPSASLYAVKVLGADGSGQYSWIINGIEWAIANNMDVINMSLGGPSGSAALKAAVDKAVASGVVVVAAAGNEGTSGSSSTVGYPGKYPSVIAVGAVDSSNQRASFSSVGPELDVMAPGVSIQSTLPGNKYGAYNGTSMASPHVAGAAALILSKHPNWTNTQVRSSLENTTTKLGDSFYYGKGLINVQAAAQ
|
3.4.21.62
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.;
|
fibrinolysis [GO:0042730]; proteolysis [GO:0006508]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
extracellular space [GO:0005615]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF05922;PF00082;
|
3.30.70.80;3.40.50.200;
|
Peptidase S8 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62;
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0. {ECO:0000269|PubMed:12524032};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 48 degrees Celsius. {ECO:0000269|PubMed:12524032};
|
FUNCTION: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin. {ECO:0000269|PubMed:12524032}.
|
Bacillus amyloliquefaciens (Bacillus velezensis)
|
P00784
|
PAPA1_CARPA
|
MAMIPSISKLLFVAICLFVYMGLSFGDFSIVGYSQNDLTSTERLIQLFESWMLKHNKIYKNIDEKIYRFEIFKDNLKYIDETNKKNNSYWLGLNVFADMSNDEFKEKYTGSIAGNYTTTELSYEEVLNDGDVNIPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGIHYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHAVAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
|
3.4.22.2
| null |
proteolysis involved in protein catabolic process [GO:0051603]
|
extracellular space [GO:0005615]; lysosome [GO:0005764]
|
cysteine-type endopeptidase activity [GO:0004197]; serpin family protein binding [GO:0097655]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.; EC=3.4.22.2; Evidence={ECO:0000269|PubMed:21416241, ECO:0000269|PubMed:23151624, ECO:0000269|PubMed:2404797};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.293 mM for L-pyroglutamyl-L-phenylalanyl-L-leucyl-p-nitroanilide {ECO:0000269|PubMed:23151624}; KM=2.95 mM for N-benzoyl-DL-arginine p-nitroanilide {ECO:0000269|PubMed:23151624}; KM=1.4 mM for Boc-Ala-Ala-Gly-NHPhNO(2) {ECO:0000269|PubMed:2404797}; KM=0.14 mM for Boc-Ala-Ala-Gly-NHMec {ECO:0000269|PubMed:2404797}; Note=kcat is 1.021 sec(-1) with L-pyroglutamyl-L-phenylalanyl-L-leucyl-p-nitroanilide as substrate (PubMed:23151624). kcat is 0.73 sec(-1) with N-benzoyl-DL-arginine p-nitroanilide as substrate (PubMed:23151624). kcat is 1.6 sec(-1) with Boc-Ala-Ala-Gly-NHPhNO(2) as substrate (PubMed:2404797). kcat is 2 sec(-1) with Boc-Ala-Ala-Gly-NHMec as substrate (PubMed:2404797). {ECO:0000269|PubMed:23151624, ECO:0000269|PubMed:2404797};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4. {ECO:0000269|PubMed:20304972};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius (PubMed:20304972). Unstable upon 65 degrees Celsius (PubMed:20304972). {ECO:0000269|PubMed:20304972};
|
FUNCTION: Cysteine proteinase with a high level of diversity in substrate specificity, an amino acid bearing a large hydrophobic side chain at the P2 position is preferred. {ECO:0000269|PubMed:21416241, ECO:0000269|PubMed:23151624, ECO:0000269|PubMed:2404797}.
|
Carica papaya (Papaya)
|
P00785
|
ACTN_ACTCC
|
MGLPKSFVSMSLLFFSTLLILSLAFNAKNLTQRTNDEVKAMYESWLIKYGKSYNSLGEWERRFEIFKETLRFIDEHNADTNRSYKVGLNQFADLTDEEFRSTYLGFTSGSNKTKVSNQYEPRVGQVLPSYVDWRSAGAVVDIKSQGECGGCWAFSAIATVEGINKIVTGVLISLSEQELIDCGRTQNTRGCNVGYITDGFQFIINNGGINTEENYPYTAQDGECNVDLQNEKYVTIDTYENVPYNNEWALQTAVTYQPVSVALDAAGDAFKHYSSGIFIGPCGTAIDHAVTIVGYGTEGGIDYWIVKNSWDTTWGEEGYMRILRNVGGAGTCGIATMPSYPVKYNNQNHPKSYSSLINPPAFSMSNDGPVGVDDGQRYSA
|
3.4.22.14
| null |
proteolysis involved in protein catabolic process [GO:0051603]
|
extracellular space [GO:0005615]; lysosome [GO:0005764]
|
cysteine-type endopeptidase activity [GO:0004197]
|
PF08246;PF00112;
|
1.10.287.2250;3.90.70.10;
|
Peptidase C1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain.; EC=3.4.22.14; Evidence={ECO:0000269|PubMed:18442249};
| null | null | null | null |
FUNCTION: Cysteine protease responsible for the cleavage of kiwellin into kissper and KiTH. {ECO:0000269|PubMed:18442249}.
|
Actinidia chinensis var. chinensis (Chinese soft-hair kiwi)
|
P00786
|
CATH_RAT
|
MWTALPLLCAGAWLLSAGATAELTVNAIEKFHFTSWMKQHQKTYSSREYSHRLQVFANNWRKIQAHNQRNHTFKMGLNQFSDMSFAEIKHKYLWSEPQNCSATKSNYLRGTGPYPSSMDWRKKGNVVSPVKNQGACGSCWTFSTTGALESAVAIASGKMMTLAEQQLVDCAQNFNNHGCQGGLPSQAFEYILYNKGIMGEDSYPYIGKNGQCKFNPEKAVAFVKNVVNITLNDEAAMVEAVALYNPVSFAFEVTEDFMMYKSGVYSSNSCHKTPDKVNHAVLAVGYGEQNGLLYWIVKNSWGSNWGNNGYFLIERGKNMCGLAACASYPIPQV
|
3.4.22.16
| null |
adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; bradykinin catabolic process [GO:0010815]; cellular response to thyroid hormone stimulus [GO:0097067]; dichotomous subdivision of terminal units involved in lung branching [GO:0060448]; ERK1 and ERK2 cascade [GO:0070371]; immune response [GO:0006955]; immune response-regulating signaling pathway [GO:0002764]; membrane protein proteolysis [GO:0033619]; metanephros development [GO:0001656]; negative regulation of apoptotic process [GO:0043066]; neuropeptide catabolic process [GO:0010813]; positive regulation of angiogenesis [GO:0045766]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidase activity [GO:0010952]; protein destabilization [GO:0031648]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to odorant [GO:1990834]; response to retinoic acid [GO:0032526]; spermatogenesis [GO:0007283]; surfactant homeostasis [GO:0043129]; T cell mediated cytotoxicity [GO:0001913]; zymogen activation [GO:0031638]
|
acrosomal vesicle [GO:0001669]; alveolar lamellar body [GO:0097208]; axoneme [GO:0005930]; cytosol [GO:0005829]; extracellular space [GO:0005615]; lysosome [GO:0005764]; outer dense fiber [GO:0001520]
|
aminopeptidase activity [GO:0004177]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; HLA-A specific activating MHC class I receptor activity [GO:0030108]; kininogen binding [GO:0030984]; peptidase activator activity involved in apoptotic process [GO:0016505]; peptidase activity [GO:0008233]; protein self-association [GO:0043621]; protein-containing complex binding [GO:0044877]; serine-type endopeptidase activity [GO:0004252]; thyroid hormone binding [GO:0070324]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null |
SUBCELLULAR LOCATION: Lysosome.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins, acting as an aminopeptidase (notably, cleaving Arg-|-Xaa bonds) as well as an endopeptidase.; EC=3.4.22.16;
| null | null | null | null |
FUNCTION: Important for the overall degradation of proteins in lysosomes.
|
Rattus norvegicus (Rat)
|
P00787
|
CATB_RAT
|
MWWSLIPLSCLLALTSAHDKPSSHPLSDDMINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGGPNLPERVGFSEDINLPESFDAREQWSNCPTIAQIRDQGSCGSCWAFGAVEAMSDRICIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWNFWTRKGLVSGGVYNSHIGCLPYTIPPCEHHVNGSRPPCTGEGDTPKCNKMCEAGYSTSYKEDKHYGYTSYSVSDSEKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDVMGGHAIRILGWGIENGVPYWLVANSWNVDWGDNGFFKILRGENHCGIESEIVAGIPRTQQYWGRF
|
3.4.22.1
| null |
autophagy [GO:0006914]; cellular response to mechanical stimulus [GO:0071260]; cellular response to thyroid hormone stimulus [GO:0097067]; collagen catabolic process [GO:0030574]; decidualization [GO:0046697]; epithelial cell differentiation [GO:0030855]; neuron apoptotic process [GO:0051402]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; response to amine [GO:0014075]; response to cytokine [GO:0034097]; response to dexamethasone [GO:0071548]; response to ethanol [GO:0045471]; response to glucose [GO:0009749]; response to interleukin-4 [GO:0070670]; response to mechanical stimulus [GO:0009612]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; skeletal muscle tissue development [GO:0007519]; spermatogenesis [GO:0007283]; symbiont entry into host cell [GO:0046718]; thyroid hormone generation [GO:0006590]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosome [GO:0005764]; melanosome [GO:0042470]; peptidase inhibitor complex [GO:1904090]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383]
|
collagen binding [GO:0005518]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopeptidase activity [GO:0004175]; kininogen binding [GO:0030984]; peptidase activity [GO:0008233]; peptide binding [GO:0042277]; protein self-association [GO:0043621]; protein-containing complex binding [GO:0044877]; proteoglycan binding [GO:0043394]
|
PF00112;PF08127;
|
3.90.70.10;
|
Peptidase C1 family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:8001549}. Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space {ECO:0000250|UniProtKB:A1E295}. Apical cell membrane {ECO:0000250|UniProtKB:P10605}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10605}; Extracellular side {ECO:0000250|UniProtKB:P10605}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000250|UniProtKB:P10605}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.; EC=3.4.22.1; Evidence={ECO:0000269|PubMed:1639824};
| null | null | null | null |
FUNCTION: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (PubMed:1639824). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis (By similarity). {ECO:0000250|UniProtKB:P07858, ECO:0000250|UniProtKB:P10605, ECO:0000269|PubMed:1639824}.
|
Rattus norvegicus (Rat)
|
P00789
|
CANX_CHICK
|
MMPFGGIAARLQRDRLRAEGVGEHNNAVKYLNQDYEALKQECIESGTLFRDPQFPAGPTALGFKELGPYSSKTRGVEWKRPSELVDDPQFIVGGATRTDICQGALGDCWLLAAIGSLTLNEELLHRVVPHGQSFQEDYAGIFHFQIWQFGEWVDVVVDDLLPTKDGELLFVHSAECTEFWSALLEKAYAKLNGCYESLSGGSTTEGFEDFTGGVAEMYDLKRAPRNMGHIIRKALERGSLLGCSIDITSAFDMEAVTFKKLVKGHAYSVTAFKDVNYRGQQEQLIRIRNPWGQVEWTGAWSDGSSEWDNIDPSDREELQLKMEDGEFWMSFRDFMREFSRLEICNLTPDALTKDELSRWHTQVFEGTWRRGSTAGGCRNNPATFWINPQFKIKLLEEDDDPGDDEVACSFLVALMQKHRRRERRVGGDMHTIGFAVYEVPEEAQGSQNVHLKKDFFLRNQSRARSETFINLREVSNQIRLPPGEYIVVPSTFEPHKEADFILRVFTEKQSDTAELDEEISADLADEEEITEDDIEDGFKNMFQQLAGEDMEISVFELKTILNRVIARHKDLKTDGFSLDSCRNMVNLMDKDGSARLGLVEFQILWNKIRSWLTIFRQYDLDKSGTMSSYEMRMALESAGFKLNNKLHQVVVARYADAETGVDFDNFVCCLVKLETMFRFFHSMDRDGTGTAVMNLAEWLLLTMCG
|
3.4.22.52
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 3 Ca(2+) ions.;
|
proteolysis [GO:0006508]
|
acrosomal vesicle [GO:0001669]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]
|
PF01067;PF00648;
|
2.60.120.380;3.90.70.10;1.10.238.10;
|
Peptidase C2 family
|
PTM: The N-terminus is blocked.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.52;
| null | null | null | null |
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction.
|
Gallus gallus (Chicken)
|
P00791
|
PEPA_PIG
|
MKWLLLLSLVVLSECLVKVPLVRKKSLRQNLIKNGKLKDFLKTHKHNPASKYFPEAAALIGDEPLENYLDTEYFGTIGIGTPAQDFTVIFDTGSSNLWVPSVYCSSLACSDHNQFNPDDSSTFEATSQELSITYGTGSMTGILGYDTVQVGGISDTNQIFGLSETEPGSFLYYAPFDGILGLAYPSISASGATPVFDNLWDQGLVSQDLFSVYLSSNDDSGSVVLLGGIDSSYYTGSLNWVPVSVEGYWQITLDSITMDGETIACSGGCQAIVDTGTSLLTGPTSAIANIQSDIGASENSDGEMVISCSSIDSLPDIVFTINGVQYPLSPSAYILQDDDSCTSGFEGMDVPTSSGELWILGDVFIRQYYTVFDRANNKVGLAPVA
|
3.4.23.1
| null |
digestion [GO:0007586]; proteolysis [GO:0006508]
|
extracellular exosome [GO:0070062]
|
aspartic-type endopeptidase activity [GO:0004190]
|
PF07966;PF00026;
|
6.10.140.60;2.40.70.10;
|
Peptidase A1 family
|
PTM: Minor amounts of the active enzyme occur with 'Ala-58' at the amino end.
|
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.; EC=3.4.23.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10094};
| null | null | null | null |
FUNCTION: Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
|
Sus scrofa (Pig)
|
P00794
|
CHYM_BOVIN
|
MRCLVVLLAVFALSQGAEITRIPLYKGKSLRKALKEHGLLEDFLQKQQYGISSKYSGFGEVASVPLTNYLDSQYFGKIYLGTPPQEFTVLFDTGSSDFWVPSIYCKSNACKNHQRFDPRKSSTFQNLGKPLSIHYGTGSMQGILGYDTVTVSNIVDIQQTVGLSTQEPGDVFTYAEFDGILGMAYPSLASEYSIPVFDNMMNRHLVAQDLFSVYMDRNGQESMLTLGAIDPSYYTGSLHWVPVTVQQYWQFTVDSVTISGVVVACEGGCQAILDTGTSKLVGPSSDILNIQQAIGATQNQYGEFDIDCDNLSYMPTVVFEINGKMYPLTPSAYTSQDQGFCTSGFQSENHSQKWILGDVFIREYYSVFDRANNLVGLAKAI
|
3.4.23.4
| null |
digestion [GO:0007586]; proteolysis [GO:0006508]
| null |
aspartic-type endopeptidase activity [GO:0004190]
|
PF07966;PF00026;
|
6.10.140.60;2.40.70.10;
|
Peptidase A1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 104-Ser-Phe-|-Met-Ala-107 bond in kappa-chain of casein.; EC=3.4.23.4;
| null | null | null | null |
FUNCTION: Chymosin is synthesized in the mucosa of the abomasum (fourth stomach) of young (unweaned) ruminants. The enzyme hydrolyzes casein to paracasein.
|
Bos taurus (Bovine)
|
P00795
|
CATD_PIG
|
GPIPEVLKNYMDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWIHHKYNSGKSSTYVKNGTTFAIHYGSGSLSGYLSSQDTVSVPCNSALSGVGGIKVERQTFGEATKQPGLTFIAAKFDGILGMAYPRISVNNVVPVFDNLMQQKLVDKDIFSFYLNRDPGAQPGGELMLGGIDSKYYKGSLDYHNVTRKAYWQIHMNQVAVGSSLTLCKGGCEAIVDTGTSLIVGQPEEVRELGKAIGAVPLIQGEYMIPCEKVPSLPDVTVTLGGKKYKLSSENYTLKVSQAGQTICLSGFMGMDIPPPGGPLWILGDVFIGRYYTVFDRDLNRVGLAEAA
|
3.4.23.5
| null |
proteolysis [GO:0006508]
|
extracellular space [GO:0005615]; lysosome [GO:0005764]; melanosome [GO:0042470]
|
aspartic-type endopeptidase activity [GO:0004190]
|
PF00026;
|
2.60.40.1960;2.40.70.10;
|
Peptidase A1 family
|
PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000250|UniProtKB:P07339}.
|
SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}. Secreted, extracellular space {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.; EC=3.4.23.5;
| null | null | null | null |
FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. {ECO:0000250|UniProtKB:P07339}.
|
Sus scrofa (Pig)
|
P00796
|
RENI2_MOUSE
|
MDRRRMPLWALLLLWSPCTFSLPTGTTFERIPLKKMPSVREILEERGVDMTRLSAEWDVFTKRSSLTDLISPVVLTNYLNSQYYGEIGIGTPPQTFKVIFDTGSANLWVPSTKCSRLYLACGIHSLYESSDSSSYMENGDDFTIHYGSGRVKGFLSQDSVTVGGITVTQTFGEVTELPLIPFMLAQFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEKVFSVYYNRGPHLLGGEVVLGGSDPEHYQGDFHYVSLSKTDSWQITMKGVSVGSSTLLCEEGCEVVVDTGSSFISAPTSSLKLIMQALGAKEKRLHEYVVSCSQVPTLPDISFNLGGRAYTLSSTDYVLQYPNRRDKLCTVALHAMDIPPPTGPVWVLGATFIRKFYTEFDRHNNRIGFALAR
|
3.4.23.15
| null |
angiotensin maturation [GO:0002003]; gene expression [GO:0010467]; positive regulation of blood pressure [GO:0045777]; regulation of blood pressure [GO:0008217]; response to cAMP [GO:0051591]; response to cGMP [GO:0070305]; response to xenobiotic stimulus [GO:0009410]
|
extracellular space [GO:0005615]
|
aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]; insulin-like growth factor receptor binding [GO:0005159]; signaling receptor binding [GO:0005102]
|
PF07966;PF00026;
|
2.40.70.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00797}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.; EC=3.4.23.15; Evidence={ECO:0000250|UniProtKB:P00797};
| null | null | null | null |
FUNCTION: Renin is a highly specific endopeptidase, related to pepsin, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. {ECO:0000250|UniProtKB:P00797}.
|
Mus musculus (Mouse)
|
P00797
|
RENI_HUMAN
|
MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCNEGPTLPDISFHLGGKEYTLTSADYVFQESYSSKKLCTLAIHAMDIPPPTGPTWALGATFIRKFYTEFDRRNNRIGFALAR
|
3.4.23.15
| null |
amyloid-beta metabolic process [GO:0050435]; angiotensin maturation [GO:0002003]; cell maturation [GO:0048469]; cellular response to xenobiotic stimulus [GO:0071466]; drinking behavior [GO:0042756]; hormone-mediated signaling pathway [GO:0009755]; juxtaglomerular apparatus development [GO:0072051]; kidney development [GO:0001822]; male gonad development [GO:0008584]; mesonephros development [GO:0001823]; proteolysis [GO:0006508]; regulation of blood pressure [GO:0008217]; regulation of MAPK cascade [GO:0043408]; renin-angiotensin regulation of aldosterone production [GO:0002018]; response to cAMP [GO:0051591]; response to cGMP [GO:0070305]; response to immobilization stress [GO:0035902]; response to lipopolysaccharide [GO:0032496]
|
apical part of cell [GO:0045177]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
aspartic-type endopeptidase activity [GO:0004190]; insulin-like growth factor receptor binding [GO:0005159]; peptidase activity [GO:0008233]; signaling receptor binding [GO:0005102]
|
PF07966;PF00026;
|
2.40.70.10;
|
Peptidase A1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12045255}. Membrane {ECO:0000269|PubMed:12045255}. Note=Associated to membranes via binding to ATP6AP2. {ECO:0000269|PubMed:12045255}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of Leu-|-Xaa bond in angiotensinogen to generate angiotensin I.; EC=3.4.23.15; Evidence={ECO:0000269|PubMed:12045255, ECO:0000269|PubMed:20927107};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for angiotensinogen (in absence of ATP6AP2) {ECO:0000269|PubMed:12045255}; KM=0.15 uM for angiotensinogen (in presence of membrane-bound ATP6AP2) {ECO:0000269|PubMed:12045255};
| null | null | null |
FUNCTION: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. {ECO:0000269|PubMed:12045255, ECO:0000269|PubMed:20927107}.
|
Homo sapiens (Human)
|
P00800
|
THER_BACTH
|
MKMKMKLASFGLAAGLAAQVFLPYNALASTEHVTWNQQFQTPQFISGDLLKVNGTSPEELVYQYVEKNENKFKFHENAKDTLQLKEKKNDNLGFTFMRFQQTYKGIPVFGAVVTSHVKDGTLTALSGTLIPNLDTKGSLKSGKKLSEKQARDIAEKDLVANVTKEVPEYEQGKDTEFVVYVNGDEASLAYVVNLNFLTPEPGNWLYIIDAVDGKILNKFNQLDAAKPGDVKSITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK
|
3.4.24.27
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 4 Ca(2+) ions per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
|
proteolysis [GO:0006508]
|
extracellular region [GO:0005576]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]
|
PF07504;PF03413;PF01447;PF02868;
|
3.10.170.10;3.10.450.40;3.10.450.490;1.10.390.10;
|
Peptidase M4 family
| null |
SUBCELLULAR LOCATION: Secreted.
|
CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.; EC=3.4.24.27;
| null | null | null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable.;
|
FUNCTION: Extracellular zinc metalloprotease.
|
Bacillus thermoproteolyticus
|
P00803
|
LEP_ECOLI
|
MANMFALILVIATLVTGILWCVDKFFFAPKRRERQAAAQAAAGDSLDKATLKKVAPKPGWLETGASVFPVLAIVLIVRSFIYEPFQIPSGSMMPTLLIGDFILVEKFAYGIKDPIYQKTLIETGHPKRGDIVVFKYPEDPKLDYIKRAVGLPGDKVTYDPVSKELTIQPGCSSGQACENALPVTYSNVEPSDFVQTFSRRNGGEATSGFFEVPKNETKENGIRLSERKETLGDVTHRILTVPIAQDQVGMYYQQPGQQLATWIVPPGQYFMMGDNRDNSADSRYWGFVPEANLVGRATAIWMSFDKQEGEWPTGLRLSRIGGIH
|
3.4.21.89
| null |
protein processing [GO:0016485]; proteolysis [GO:0006508]; signal peptide processing [GO:0006465]; thylakoid membrane organization [GO:0010027]
|
plasma membrane [GO:0005886]
|
endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]
|
PF10502;
|
2.170.230.10;2.10.109.10;
|
Peptidase S26 family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21778229}; Multi-pass membrane protein {ECO:0000269|PubMed:21778229}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89;
| null | null | null | null | null |
Escherichia coli (strain K12)
|
P00804
|
LSPA_ECOLI
|
MSQSICSTGLRWLWLVVVVLIIDLGSKYLILQNFALGDTVPLFPSLNLHYARNYGAAFSFLADSGGWQRWFFAGIAIGISVILAVMMYRSKATQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICVGAALIVLEGFLPSRAKKQ
|
3.4.23.36
| null |
lipoprotein biosynthetic process via signal peptide cleavage [GO:0097304]; proteolysis [GO:0006508]
|
plasma membrane [GO:0005886]
|
aspartic-type endopeptidase activity [GO:0004190]; endopeptidase activity [GO:0004175]
|
PF01252;
| null |
Peptidase A8 family
| null |
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1894646, ECO:0000269|PubMed:6368552}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:1894646, ECO:0000269|PubMed:6368552}.
|
CATALYTIC ACTIVITY: Reaction=Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.; EC=3.4.23.36; Evidence={ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:6368552};
| null |
PATHWAY: Protein modification; lipoprotein biosynthesis (signal peptide cleavage). {ECO:0000255|HAMAP-Rule:MF_00161}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.9. {ECO:0000269|PubMed:6368552};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37-45 degrees Celsius. {ECO:0000269|PubMed:6368552};
|
FUNCTION: This protein specifically catalyzes the removal of signal peptides from prolipoproteins. {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:6368552, ECO:0000269|PubMed:6374664, ECO:0000269|PubMed:6378662}.
|
Escherichia coli (strain K12)
|
P00805
|
ASPG2_ECOLI
|
MEFFKKTALAALVMGFSGAALALPNITILATGGTIAGGGDSATKSNYTVGKVGVENLVNAVPQLKDIANVKGEQVVNIGSQDMNDNVWLTLAKKINTDCDKTDGFVITHGTDTMEETAYFLDLTVKCDKPVVMVGAMRPSTSMSADGPFNLYNAVVTAADKASANRGVLVVMNDTVLDGRDVTKTNTTDVATFKSVNYGPLGYIHNGKIDYQRTPARKHTSDTPFDVSKLNELPKVGIVYNYANASDLPAKALVDAGYDGIVSAGVGNGNLYKSVFDTLATAAKTGTAVVRSSRVPTGATTQDAEVDDAKYGFVASGTLNPQKARVLLQLALTQTKDPQQIQQIFNQY
|
3.5.1.1
| null |
asparagine catabolic process [GO:0006530]; protein homotetramerization [GO:0051289]
|
cytosol [GO:0005829]; outer membrane-bounded periplasmic space [GO:0030288]; periplasmic space [GO:0042597]; protein-containing complex [GO:0032991]
|
asparaginase activity [GO:0004067]; identical protein binding [GO:0042802]
|
PF00710;PF17763;
|
3.40.50.40;3.40.50.1170;
|
Asparaginase 1 family
| null |
SUBCELLULAR LOCATION: Periplasm.
|
CATALYTIC ACTIVITY: Reaction=H2O + L-asparagine = L-aspartate + NH4(+); Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1; Evidence={ECO:0000269|PubMed:8706862};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.115 uM for L-asparagine;
| null | null | null | null |
Escherichia coli (strain K12)
|
P00806
|
ENLYS_BPT7
|
MARVQFKQRESTDAIFVHCSATKPSQNVGVREIRQWHKEQGWLDVGYHFIIKRDGTVEAGRDEMAVGSHAKGYNHNSIGVCLVGGIDDKGKFDANFTPAQMQSLRSLLVTLLAKYEGAVLRAHHEVAPKACPSFDLKRWWEKNELVTSDRG
|
3.5.1.28
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000269|PubMed:8171031}; Note=Zn(2+) is required for amidase activity. {ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000269|PubMed:8171031};
|
defense response to bacterium [GO:0042742]; negative regulation of viral transcription [GO:0032897]; peptidoglycan catabolic process [GO:0009253]; viral release from host cell by cytolysis [GO:0044659]
|
host cell cytoplasm [GO:0030430]
|
N-acetylmuramoyl-L-alanine amidase activity [GO:0008745]; zinc ion binding [GO:0008270]
|
PF01510;
|
3.40.80.10;
|
N-acetylmuramoyl-L-alanine amidase 2 family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04111}. Note=The endolysin is cytoplasmic, but can reach the periplasmic space with the help of the holins which disrupt the host cell membrane. {ECO:0000255|HAMAP-Rule:MF_04111}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28; Evidence={ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000269|PubMed:8171031};
| null | null | null | null |
FUNCTION: Plays an important role in the switch between viral transcription and genome replication. Once produced in sufficient amount, interacts with and inhibits the viral RNA polymerase that becomes unable to produce additional late transcripts. This lysozyme-polymerase complex in turn plays an active role in viral genome replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000269|PubMed:14764584, ECO:0000269|PubMed:15223315, ECO:0000269|PubMed:9192997}.; FUNCTION: Endolysin with amidase activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and breaking down the peptidoglycan layer. {ECO:0000255|HAMAP-Rule:MF_04111, ECO:0000305|PubMed:15223315}.
|
Escherichia phage T7 (Bacteriophage T7)
|
P00811
|
AMPC_ECOLI
|
MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWGYADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGITLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVKPSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVKSTIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSIINGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNYPNPARVDAAWQILNALQ
|
3.5.2.6
| null |
antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677]
|
outer membrane-bounded periplasmic space [GO:0030288]
|
beta-lactamase activity [GO:0008800]
|
PF00144;
|
3.40.710.10;
|
Class-C beta-lactamase family
| null |
SUBCELLULAR LOCATION: Periplasm {ECO:0000303|PubMed:6795623}.
|
CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:3264154, ECO:0000269|PubMed:3264155, ECO:0000269|PubMed:6998377};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.4 uM for benzylpenicillin (at pH 8.2) {ECO:0000269|PubMed:3264154}; KM=3.5 uM for ampicillin (at pH 8.2) {ECO:0000269|PubMed:3264154}; KM=500 uM for nitrocefin (at pH 8.2) {ECO:0000269|PubMed:3264155}; KM=170 uM for cephaloridine (at pH 8.2) {ECO:0000269|PubMed:3264155}; KM=400 uM for cefazolin (at pH 8.2) {ECO:0000269|PubMed:3264155}; KM=42 uM for cefalotin (at pH 8.2) {ECO:0000269|PubMed:3264155}; KM=4 uM for cephalexin (at pH 8.2) {ECO:0000269|PubMed:3264155}; Note=kcat is 45 sec(-1) with benzylpenicillin as substrate (at pH 8.2) (PubMed:3264154). kcat is 4.2 sec(-1) with ampicillin as substrate (at pH 8.2) (PubMed:3264154). kcat is 490 sec(-1) with nitrocefin as substrate (at pH 8.2) (PubMed:3264155). kcat is 130 sec(-1) with cephaloridine as substrate (at pH 8.2) (PubMed:3264155). kcat is 150 sec(-1) with cefazolin as substrate (at pH 8.2) (PubMed:3264155). kcat is 300 sec(-1) with cefalotin as substrate (at pH 8.2) (PubMed:3264155). kcat is 38 sec(-1) with cephalexin as substrate (at pH 8.2) (PubMed:3264155). {ECO:0000269|PubMed:3264154, ECO:0000269|PubMed:3264155};
| null | null | null |
FUNCTION: Beta-lactamase which confers resistance to penicillins and cephalosporins (PubMed:33199391, PubMed:6998377). Has benzylpenicillin- and cephaloridine-hydrolyzing activity (PubMed:3264154, PubMed:3264155, PubMed:6998377). Has weak cefuroxime, cefotaxime, cefoxitin and oxacillin-hydrolyzing activities (PubMed:3264154, PubMed:3264155). {ECO:0000269|PubMed:3264154, ECO:0000269|PubMed:3264155, ECO:0000269|PubMed:33199391, ECO:0000269|PubMed:6998377}.
|
Escherichia coli (strain K12)
|
P00812
|
ARGI_YEAST
|
METGPHYNYYKNRELSIVLAPFSGGQGKLGVEKGPKYMLKHGLQTSIEDLGWSTELEPSMDEAQFVGKLKMEKDSTTGGSSVMIDGVKAKRADLVGEATKLVYNSVSKVVQANRFPLTLGGDHSIAIGTVSAVLDKYPDAGLLWIDAHADINTIESTPSGNLHGCPVSFLMGLNKDVPHCPESLKWVPGNLSPKKIAYIGLRDVDAGEKKILKDLGIAAFSMYHVDKYGINAVIEMAMKAVHPETNGEGPIMCSYDVDGVDPLYIPATGTPVRGGLTLREGLFLVERLAESGNLIALDVVECNPDLAIHDIHVSNTISAGCAIARCALGETLL
|
3.5.3.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00742};
|
arginine catabolic process to ornithine [GO:0019547]; regulation of ornithine metabolic process [GO:0090368]; urea cycle [GO:0000050]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mating projection tip [GO:0043332]; nucleus [GO:0005634]; ornithine carbamoyltransferase inhibitor complex [GO:1903269]
|
arginase activity [GO:0004053]; manganese ion binding [GO:0030145]; ornithine carbamoyltransferase inhibitor activity [GO:0090369]; zinc ion binding [GO:0008270]
|
PF00491;
|
3.40.800.10;
|
Arginase family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + L-arginine = L-ornithine + urea; Xref=Rhea:RHEA:20569, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911; EC=3.5.3.1; Evidence={ECO:0000250|UniProtKB:P05089};
| null |
PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:P05089}.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00813
|
ADA_HUMAN
|
MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL
|
3.5.4.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|Ref.24}; Note=Binds 1 zinc ion per subunit. {ECO:0000305|Ref.24};
|
adenosine catabolic process [GO:0006154]; adenosine metabolic process [GO:0046085]; allantoin metabolic process [GO:0000255]; alpha-beta T cell differentiation [GO:0046632]; amide catabolic process [GO:0043605]; AMP catabolic process [GO:0006196]; AMP salvage [GO:0044209]; B cell proliferation [GO:0042100]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; dAMP catabolic process [GO:0046059]; dATP catabolic process [GO:0046061]; deoxyadenosine catabolic process [GO:0006157]; embryonic digestive tract development [GO:0048566]; germinal center B cell differentiation [GO:0002314]; germinal center formation [GO:0002467]; GMP salvage [GO:0032263]; hypoxanthine salvage [GO:0043103]; inosine biosynthetic process [GO:0046103]; leukocyte migration [GO:0050900]; liver development [GO:0001889]; lung alveolus development [GO:0048286]; mature B cell apoptotic process [GO:0002901]; mucus secretion [GO:0070254]; negative regulation of adenosine receptor signaling pathway [GO:0060169]; negative regulation of inflammatory response [GO:0050728]; negative regulation of leukocyte migration [GO:0002686]; negative regulation of mature B cell apoptotic process [GO:0002906]; negative regulation of mucus secretion [GO:0070256]; negative regulation of penile erection [GO:0060407]; negative regulation of thymocyte apoptotic process [GO:0070244]; penile erection [GO:0043084]; Peyer's patch development [GO:0048541]; placenta development [GO:0001890]; positive regulation of alpha-beta T cell differentiation [GO:0046638]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of calcium-mediated signaling [GO:0050850]; positive regulation of germinal center formation [GO:0002636]; positive regulation of heart rate [GO:0010460]; positive regulation of smooth muscle contraction [GO:0045987]; positive regulation of T cell differentiation in thymus [GO:0033089]; positive regulation of T cell receptor signaling pathway [GO:0050862]; purine nucleotide salvage [GO:0032261]; purine-containing compound salvage [GO:0043101]; regulation of cell-cell adhesion mediated by integrin [GO:0033632]; response to hypoxia [GO:0001666]; response to inorganic substance [GO:0010035]; response to purine-containing compound [GO:0014074]; smooth muscle contraction [GO:0006939]; T cell activation [GO:0042110]; T cell differentiation in thymus [GO:0033077]; T cell receptor signaling pathway [GO:0050852]; thymocyte apoptotic process [GO:0070242]; trophectodermal cell differentiation [GO:0001829]; xanthine biosynthetic process [GO:0046111]; xenobiotic metabolic process [GO:0006805]
|
anchoring junction [GO:0070161]; cell surface [GO:0009986]; cytoplasmic vesicle lumen [GO:0060205]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
2'-deoxyadenosine deaminase activity [GO:0046936]; adenosine deaminase activity [GO:0004000]; deaminase activity [GO:0019239]; zinc ion binding [GO:0008270]
|
PF00962;
|
3.20.20.140;
|
Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:8101391}; Peripheral membrane protein; Extracellular side. Cell junction {ECO:0000269|PubMed:11772392}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P03958}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000269|PubMed:8452534}. Note=Colocalized with DPP4 at the cell surface. {ECO:0000269|PubMed:11772392}.
|
CATALYTIC ACTIVITY: Reaction=adenosine + H(+) + H2O = inosine + NH4(+); Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:16670267, ECO:0000269|PubMed:23193172, ECO:0000269|PubMed:26166670, ECO:0000269|PubMed:8452534, ECO:0000269|PubMed:9361033}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24409; Evidence={ECO:0000305|PubMed:9361033}; CATALYTIC ACTIVITY: Reaction=2'-deoxyadenosine + H(+) + H2O = 2'-deoxyinosine + NH4(+); Xref=Rhea:RHEA:28190, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256, ChEBI:CHEBI:28938, ChEBI:CHEBI:28997; EC=3.5.4.4; Evidence={ECO:0000269|PubMed:9361033}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28191; Evidence={ECO:0000305|PubMed:9361033};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=37 uM for adenosine (at 25 degrees Celsius and pH 5.5) {ECO:0000269|PubMed:8452534}; Vmax=41 umol/min/mg enzyme {ECO:0000269|PubMed:23193172};
| null | null | null |
FUNCTION: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (PubMed:16670267, PubMed:23193172, PubMed:26166670, PubMed:8452534, PubMed:9361033). Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4 (PubMed:20959412). Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation (PubMed:20959412). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (PubMed:23193172). Stimulates plasminogen activation (PubMed:15016824). Plays a role in male fertility (PubMed:21919946, PubMed:26166670). Plays a protective role in early postimplantation embryonic development (By similarity). {ECO:0000250|UniProtKB:P03958, ECO:0000250|UniProtKB:P56658, ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:15016824, ECO:0000269|PubMed:16670267, ECO:0000269|PubMed:20959412, ECO:0000269|PubMed:21919946, ECO:0000269|PubMed:23193172, ECO:0000269|PubMed:26166670, ECO:0000269|PubMed:8452534, ECO:0000269|PubMed:9361033}.
|
Homo sapiens (Human)
|
P00815
|
HIS2_YEAST
|
MVLPILPLIDDLASWNSKKEYVSLVGQVLLDGSSLSNEEILQFSKEEEVPLVALSLPSGKFSDDEIIAFLNNGVSSLFIASQDAKTAEHLVEQLNVPKERVVVEENGVFSNQFMVKQKFSQDKIVSIKKLSKDMLTKEVLGEVRTDRPDGLYTTLVVDQYERCLGLVYSSKKSIAKAIDLGRGVYYSRSRNEIWIKGETSGNGQKLLQISTDCDSDALKFIVEQENVGFCHLETMSCFGEFKHGLVGLESLLKQRLQDAPEESYTRRLFNDSALLDAKIKEEAEELTEAKGKKELSWEAADLFYFALAKLVANDVSLKDVENNLNMKHLKVTRRKGDAKPKFVGQPKAEEEKLTGPIHLDVVKASDKVGVQKALSRPIQKTSEIMHLVNPIIENVRDKGNSALLEYTEKFDGVKLSNPVLNAPFPEEYFEGLTEEMKEALDLSIENVRKFHAAQLPTETLEVETQPGVLCSRFPRPIEKVGLYIPGGTAILPSTALMLGVPAQVAQCKEIVFASPPRKSDGKVSPEVVYVAEKVGASKIVLAGGAQAVAAMAYGTETIPKVDKILGPGNQFVTAAKMYVQNDTQALCSIDMPAGPSEVLVIADEDADVDFVASDLLSQAEHGIDSQVILVGVNLSEKKIQEIQDAVHNQALQLPRVDIVRKCIAHSTIVLCDGYEEALEMSNQYAPEHLILQIANANDYVKLVDNAGSVFVGAYTPESCGDYSSGTNHTLPTYGYARQYSGANTATFQKFITAQNITPEGLENIGRAVMCVAKKEGLDGHRNAVKIRMSKLGLIPKDFQ
|
1.1.1.23; 3.5.4.19; 3.6.1.31
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P9WNW9}; Note=Binds 1 zinc ion. {ECO:0000250|UniProtKB:P9WNW9};
|
histidine biosynthetic process [GO:0000105]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; histidinol dehydrogenase activity [GO:0004399]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; phosphoribosyl-AMP cyclohydrolase activity [GO:0004635]; phosphoribosyl-ATP diphosphatase activity [GO:0004636]
|
PF00815;PF01502;PF01503;
|
1.20.5.1300;1.10.287.1080;3.40.50.1980;3.10.20.810;
|
Histidinol dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide; Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435, ChEBI:CHEBI:59457; EC=3.5.4.19; Evidence={ECO:0000250|UniProtKB:Q50837}; CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31; Evidence={ECO:0000250|UniProtKB:O82768}; CATALYTIC ACTIVITY: Reaction=H2O + L-histidinol + 2 NAD(+) = 3 H(+) + L-histidine + 2 NADH; Xref=Rhea:RHEA:20641, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57595, ChEBI:CHEBI:57699, ChEBI:CHEBI:57945; EC=1.1.1.23; Evidence={ECO:0000250|UniProtKB:P9WNW9};
| null |
PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.; PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.; PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00817
|
IPYR_YEAST
|
MTYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKENNIFNMVVEIPRWTNAKLEITKEETLNPIIQDTKKGKLRFVRNCFPHHGYIHNYGAFPQTWEDPNVSHPETKAVGDNDPIDVLEIGETIAYTGQVKQVKALGIMALLDEGETDWKVIAIDINDPLAPKLNDIEDVEKYFPGLLRATNEWFRIYKIPDGKPENQFAFSGEAKNKKYALDIIKETHDSWKQLIAGKSSDSKGIDLTNVTLPDTPTYSKAASDAIPPASPKADAPIDKSIDKWFFISGSV
|
3.6.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
phosphate-containing compound metabolic process [GO:0006796]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
inorganic diphosphate phosphatase activity [GO:0004427]; magnesium ion binding [GO:0000287]
|
PF00719;
|
3.90.80.10;
|
PPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=diphosphate + H2O = H(+) + 2 phosphate; Xref=Rhea:RHEA:24576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474; EC=3.6.1.1;
| null | null | null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00829
|
ATPB_BOVIN
|
MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS
|
7.1.2.2
| null |
proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
mitochondrial proton-transporting ATP synthase complex [GO:0005753]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
|
PF00006;PF02874;
|
2.40.10.170;3.40.50.300;
|
ATPase alpha/beta chains family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Peripheral membrane protein {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Matrix side {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:95168}.
|
CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; Evidence={ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:9687365}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:57722; Evidence={ECO:0000305|PubMed:23407638, ECO:0000305|PubMed:9687365};
| null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. {ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:9687365}.
|
Bos taurus (Bovine)
|
P00830
|
ATPB_YEAST
|
MVLPRLYTATSRAAFKAAKQSAPLLSTSWKRCMASAAQSTPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKLVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVPVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAEQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGVINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQEHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVERARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLEGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN
|
7.1.2.2
| null |
proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase, catalytic core [GO:0005754]; mitochondrion [GO:0005739]; proton-transporting ATP synthase complex, catalytic core F(1) [GO:0045261]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]; proton-transporting ATPase activity, rotational mechanism [GO:0046961]
|
PF00006;PF02874;
|
2.40.10.170;3.40.50.300;
|
ATPase alpha/beta chains family
| null |
SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
| null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00845
|
ATPL_BACP3
|
MSLGVLAAAIAVGLGALGAGIGNGLIVSRTIEGIARQPELRPVLQTTMFIGVALVEALPIIGVVFSFIYLGR
| null | null | null |
plasma membrane [GO:0005886]; proton-transporting ATP synthase complex, coupling factor F(o) [GO:0045263]
|
lipid binding [GO:0008289]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]
|
PF00137;
|
1.20.20.10;
|
ATPase C chain family
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.; FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
|
Bacillus sp. (strain PS3)
|
P00846
|
ATP6_HUMAN
|
MNENLFASFIAPTILGLPAAVLIILFPPLLIPTSKYLINNRLITTQQWLIKLTSKQMMTMHNTKGRTWSLMLVSLIIFIATTNLLGLLPHSFTPTTQLSMNLAMAIPLWAGTVIMGFRSKIKNALAHFLPQGTPTPLIPMLVIIETISLLIQPMALAVRLTANITAGHLLMHLIGSATLAMSTINLPSTLIIFTILILLTILEIAVALIQAYVFTLLVSLYLHDNT
| null | null |
proton motive force-driven ATP synthesis [GO:0015986]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]; response to hyperoxia [GO:0055093]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; proton-transporting ATP synthase complex, coupling factor F(o) [GO:0045263]
|
proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]
|
PF00119;
|
1.20.120.220;
|
ATPase A chain family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
|
Homo sapiens (Human)
|
P00854
|
ATP6_YEAST
|
MFNLLNTYITSPLDQFEIRTLFGLQSSFIDLSCLNLTTFSLYTIIVLLVITSLYTLTNNNNKIIGSRWLISQEAIYDTIMNMTKGQIGGKNWGLYFPMIFTLFMFIFIANLISMIPYSFALSAHLVFIISLSIVIWLGNTILGLYKHGWVFFSLFVPAGTPLPLVPLLVIIETLSYFARAISLGLRLGSNILAGHLLMVILAGLTFNFMLINLFTLVFGFVPLAMILAIMMLEFAIGIIQGYVWAILTASYLKDAVYLH
| null | null |
proton motive force-driven ATP synthesis [GO:0015986]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrion [GO:0005739]
|
proton-transporting ATP synthase activity, rotational mechanism [GO:0046933]
|
PF00119;
|
1.20.120.220;
|
ATPase A chain family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00860
|
DCOR_MOUSE
|
MSSFTKDEFDCHILDEGFTAKDILDQKINEVSSSDDKDAFYVADLGDILKKHLRWLKALPRVTPFYAVKCNDSRAIVSTLAAIGTGFDCASKTEIQLVQGLGVPAERVIYANPCKQVSQIKYAASNGVQMMTFDSEIELMKVARAHPKAKLVLRIATDDSKAVCRLSVKFGATLKTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQAVSDARCVFDMATEVGFSMHLLDIGGGFPGSEDTKLKFEEITSVINPALDKYFPSDSGVRIIAEPGRYYVASAFTLAVNIIAKKTVWKEQPGSDDEDESNEQTFMYYVNDGVYGSFNCILYDHAHVKALLQKRPKPDEKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPNIYYVMSRPMWQLMKQIQSHGFPPEVEEQDDGTLPMSCAQESGMDRHPAACASARINV
|
4.1.1.17
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10378276, ECO:0000269|PubMed:1730582};
|
cell population proliferation [GO:0008283]; kidney development [GO:0001822]; polyamine metabolic process [GO:0006595]; positive regulation of cell population proliferation [GO:0008284]; putrescine biosynthetic process [GO:0009446]; putrescine biosynthetic process from ornithine [GO:0033387]; regulation of protein catabolic process [GO:0042176]; response to virus [GO:0009615]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]
|
ornithine decarboxylase activity [GO:0004586]; protein homodimerization activity [GO:0042803]
|
PF02784;PF00278;
|
3.20.20.10;
|
Orn/Lys/Arg decarboxylase class-II family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + L-ornithine = CO2 + putrescine; Xref=Rhea:RHEA:22964, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:46911, ChEBI:CHEBI:326268; EC=4.1.1.17; Evidence={ECO:0000250|UniProtKB:P11926};
| null |
PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
| null | null |
FUNCTION: Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. {ECO:0000269|PubMed:18973822, ECO:0000269|PubMed:24967154}.
|
Mus musculus (Mouse)
|
P00861
|
DCDA_ECOLI
|
MPHSLFSTDTDLTAENLLRLPAEFGCPVWVYDAQIIRRQIAALKQFDVVRFAQKACSNIHILRLMREQGVKVDSVSLGEIERALAAGYNPQTHPDDIVFTADVIDQATLERVSELQIPVNAGSVDMLDQLGQVSPGHRVWLRVNPGFGHGHSQKTNTGGENSKHGIWYTDLPAALDVIQRHHLQLVGIHMHIGSGVDYAHLEQVCGAMVRQVIEFGQDLQAISAGGGLSVPYQQGEEAVDTEHYYGLWNAAREQIARHLGHPVKLEIEPGRFLVAQSGVLITQVRSVKQMGSRHFVLVDAGFNDLMRPAMYGSYHHISALAADGRSLEHAPTVETVVAGPLCESGDVFTQQEGGNVETRALPEVKAGDYLVLHDTGAYGASMSSNYNSRPLLPEVLFDNGQARLIRRRQTIEELLALELL
|
4.1.1.20
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:11856852, ECO:0000269|PubMed:14343156};
|
lysine biosynthetic process via diaminopimelate [GO:0009089]
| null |
diaminopimelate decarboxylase activity [GO:0008836]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170]
|
PF02784;PF00278;
|
3.20.20.10;
|
Orn/Lys/Arg decarboxylase class-II family, LysA subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine; Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20; Evidence={ECO:0000269|PubMed:11856852, ECO:0000269|PubMed:14343156, ECO:0000269|PubMed:18508763};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 mM for meso-2,6-diaminoheptanedioate (at pH 6.8 and 37 degrees Celsius) {ECO:0000269|PubMed:14343156}; KM=1.07 mM for meso-2,6-diaminoheptanedioate (at pH 8) {ECO:0000269|PubMed:18508763};
|
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. {ECO:0000269|PubMed:14343156}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.7-6.8. {ECO:0000269|PubMed:14343156};
| null |
FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate. {ECO:0000269|PubMed:11856852, ECO:0000269|PubMed:14343156, ECO:0000269|PubMed:18508763}.
|
Escherichia coli (strain K12)
|
P00862
|
DCHS_LACS3
|
MSELDAKLNKLGVDRIAISPYKQWTRGYMEPGNIGNGYVTGLKVDAGVRDKSDDDVLDGIVSYDRAETKNAYIGQINMTTASSFTGVQGRVIGYDILRSPEVDKAKPLFTETQWDGSELPIYDAKPLQDALVEYFGTEQDRRHYPAPGSFIVCANKGVTAERPKNDADMKPGQGYGVWSAIAISFAKDPTKDSSMFVEDAGVWETPNEDELLEYLEGRRKAMAKSIAECGQDAHASFESSWIGFAYTMMEPGQIGNAITVAPYVSLPIDSIPGGSILTPDKDMEIMENLTMPEWLEKMGYKSLSANNALKY
|
4.1.1.22
|
COFACTOR: Name=pyruvate; Xref=ChEBI:CHEBI:15361; Note=Binds 1 pyruvoyl group covalently per subunit.;
|
amino acid metabolic process [GO:0006520]; histidine metabolic process [GO:0006547]
| null |
histidine decarboxylase activity [GO:0004398]
|
PF02329;
|
4.10.510.10;3.50.20.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + L-histidine = CO2 + histamine; Xref=Rhea:RHEA:20840, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57595, ChEBI:CHEBI:58432; EC=4.1.1.22;
| null | null | null | null | null |
Lactobacillus sp. (strain 30a)
|
P00864
|
CAPP_ECOLI
|
MNEQYSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANRQELLTTLQNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEVIARTLRKLKNQPELSEDTIKKAVESLSLELVLTAHPTEITRRTLIHKMVEVNACLKQLDNKDIADYEHNQLMRRLRQLIAQSWHTDEIRKLRPSPVDEAKWGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEFVPVRFTSWMGGDRDGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELLALVGEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELWEPLYACYQSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHTEALGELTRYLGIGDYESWSEADKQAFLIRELNSKRPLLPRNWQPSAETREVLDTCQVIAEAPQGSIAAYVISMAKTPSDVLAVHLLLKEAGIGFAMPVAPLFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIGYSDSAKDAGVMAASWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQPPGSLKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESWRRIMDELSVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPAKRRPTGGVESLRAIPWIFAWTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPFFSTRLGMLEMVFAKADLWLAEYYDQRLVDKALWPLGKELRNLQEEDIKVVLAIANDSHLMADLPWIAESIQLRNIYTDPLNVLQAELLHRSRQAEKEGQEPDPRVEQALMVTIAGIAAGMRNTG
|
4.1.1.31
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
carbon fixation [GO:0015977]; gluconeogenesis [GO:0006094]; oxaloacetate metabolic process [GO:0006107]; protein homotetramerization [GO:0051289]; tricarboxylic acid cycle [GO:0006099]
|
cytosol [GO:0005829]
|
identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphoenolpyruvate carboxylase activity [GO:0008964]
|
PF00311;
|
1.20.1440.90;
|
PEPCase type 1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
| null | null | null | null |
FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
|
Escherichia coli (strain K12)
|
P00875
|
RBL_SPIOL
|
MSPQTETKASVEFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:2118958, ECO:0000269|PubMed:8648644, ECO:0000269|PubMed:9092835}; Note=Binds 1 Mg(2+) ion per subunit (PubMed:2118958, PubMed:8648644, PubMed:9092835). Ca(2+) can substitute but is not catalytically competent (PubMed:14596800, PubMed:9034362). {ECO:0000269|PubMed:14596800, ECO:0000269|PubMed:2118958, ECO:0000269|PubMed:8648644, ECO:0000269|PubMed:9034362, ECO:0000269|PubMed:9092835};
|
photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]
|
chloroplast [GO:0009507]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
|
PTM: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization. {ECO:0000250|UniProtKB:P11383, ECO:0000305}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-Rule:MF_01338}.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:26197050, ECO:0000305|PubMed:14596800, ECO:0000305|PubMed:17740342, ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:8648644, ECO:0000305|PubMed:8955130, ECO:0000305|PubMed:9034362, ECO:0000305|PubMed:9092835}; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000305|PubMed:14596800, ECO:0000305|PubMed:17740342, ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:26197050, ECO:0000305|PubMed:8648644, ECO:0000305|PubMed:8955130, ECO:0000305|PubMed:9034362, ECO:0000305|PubMed:9092835};
| null | null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process (Probable) (PubMed:2928307). Both reactions occur simultaneously and in competition at the same active site (Probable). Binds to abscisic acid (ABA) which has weakly inhibits carboxylation and more strongly inhibits enzyme activation (PubMed:26197050). {ECO:0000269|PubMed:26197050, ECO:0000269|PubMed:2928307, ECO:0000305|PubMed:14596800, ECO:0000305|PubMed:17740342, ECO:0000305|PubMed:2118958, ECO:0000305|PubMed:8648644, ECO:0000305|PubMed:8955130, ECO:0000305|PubMed:9034362, ECO:0000305|PubMed:9092835}.
|
Spinacia oleracea (Spinach)
|
P00876
|
RBL_TOBAC
|
MSPQTETKASVGFKAGVKEYKLTYYTPEYQTKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIERVVGEKDQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDFVEQDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVKARNEGRDLAQEGNEIIREACKWSPELAAACEVWKEIVFNFAAVDVLDK
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.;
|
photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]
|
chloroplast [GO:0009507]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
|
PTM: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 3RUB and 4RUB may be the result of oxidation during crystallization (PubMed:1512238). {ECO:0000250|UniProtKB:P11383, ECO:0000269|PubMed:1512238}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000269|PubMed:3681999}; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
| null | null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process (PubMed:2928307, PubMed:3681999). Both reactions occur simultaneously and in competition at the same active site. {ECO:0000269|PubMed:2928307, ECO:0000269|PubMed:3681999, ECO:0000305}.
|
Nicotiana tabacum (Common tobacco)
|
P00877
|
RBL_CHLRE
|
MVPQTETKAGAGFKAGVKDYRLTYYTPDYVVRDTDILAAFRMTPQLGVPPEECGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYDIEPVPGEDNQYIAYVAYPIDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYVKTFVGPPHGIQVERDKLNKYGRGLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFVAEAIYKAQAETGEVKGHYLNATAGTCEEMMKRAVCAKELGVPIIMHDYLTGGFTANTSLAIYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRMSGGDHLHSGTVVGKLEGEREVTLGFVDLMRDDYVEKDRSRGIYFTQDWCSMPGVMPVASGGIHVWHMPALVEIFGDDACLQFGGGTLGHPWGNAPGAAANRVALEACTQARNEGRDLAREGGDVIRSACKWSPELAAACEVWKEIKFEFDTIDKL
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:11641402, ECO:0000269|PubMed:11866526};
|
photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]
|
chloroplast [GO:0009507]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
|
PTM: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bond reported in 1IR2 may be the result of oxidation during crystallization. {ECO:0000250|UniProtKB:P11383, ECO:0000305}.; PTM: The electron density found in the position of Thr-471 suggests it is either O-methylthreonine, or Ile, which may be produced by RNA editing (PubMed:11866526). {ECO:0000305|PubMed:11866526}.
|
SUBCELLULAR LOCATION: Plastid, chloroplast.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272;
| null | null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. {ECO:0000269|PubMed:11866526}.
|
Chlamydomonas reinhardtii (Chlamydomonas smithii)
|
P00879
|
RBL_NOSS1
|
MSYAQTKTQTKSGYKAGVQDYRLTYYTPDYTPKDTDILAAFRVTPQPGVPFEEAAAAVAAESSTGTWTTVWTDLLTDLDRYKGRCYDIEPVPGEDNQFIAYIAYPLDLFEEGSITNVLTSIVGNVFGFKALRALRLEDIRFPVAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSAPFQRWRDRFLFVADAITKAQAETGEIKGHYLNVTAPTCEEMLKRAEYAKELKQPIIMHDYLTAGFTANTTLARWCRDNGVLLHIHRAMHAVIDRQKNHGIHFRVLAKALRLSGGDHIHTGTVVGKLEGERGITMGFVDLLRENYVEQDKSRGIYFTQDWASLPGVMAVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRNLAREGNDVIREAAKWSPELAVACELWKEIKFEFEAMDTV
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01338}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01338};
|
photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]
|
carboxysome [GO:0031470]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
|
PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000255|HAMAP-Rule:MF_01338}.
|
SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:24907906}. Note=This cyanobacterium makes beta-type carboxysomes (PubMed:24907906). In the carboxysome RuBisCO is organized into a paracrystalline array (By similarity). {ECO:0000250|UniProtKB:Q31NB3, ECO:0000269|PubMed:24907906}.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000255|HAMAP-Rule:MF_01338, ECO:0000269|PubMed:32451445}; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272; Evidence={ECO:0000255|HAMAP-Rule:MF_01338};
| null | null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. {ECO:0000255|HAMAP-Rule:MF_01338}.
|
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
|
P00880
|
RBL_SYNP6
|
MPKTQSAAGYKAGVKDYKLTYYTPDYTPKDTDLLAAFRFSPQPGVPADEAGAAIAAESSTGTWTTVWTDLLTDMDRYKGKCYHIEPVQGEENSYFAFIAYPLDLFEEGSVTNILTSIVGNVFGFKAIRSLRLEDIRFPVALVKTFQGPPHGIQVERDLLNKYGRPMLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENINSQPFQRWRDRFLFVADAIHKSQAETGEIKGHYLNVTAPTCEEMMKRAEFAKELGMPIIMHDFLTAGFTANTTLAKWCRDNGVLLHIHRAMHAVIDRQRNHGIHFRVLAKCLRLSGGDHLHSGTVVGKLEGDKASTLGFVDLMREDHIEADRSRGVFFTQDWASMPGVLPVASGGIHVWHMPALVEIFGDDSVLQFGGGTLGHPWGNAPGATANRVALEACVQARNEGRDLYREGGDILREAGKWSPELAAALDLWKEIKFEFETMDKL
|
4.1.1.39
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8245022}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8245022};
|
photorespiration [GO:0009853]; reductive pentose-phosphate cycle [GO:0019253]
|
carboxysome [GO:0031470]
|
magnesium ion binding [GO:0000287]; monooxygenase activity [GO:0004497]; ribulose-bisphosphate carboxylase activity [GO:0016984]
|
PF00016;PF02788;
|
3.20.20.110;3.30.70.150;
|
RuBisCO large chain family, Type I subfamily
|
PTM: The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover. {ECO:0000305|PubMed:8245022}.
|
SUBCELLULAR LOCATION: Carboxysome {ECO:0000255|HAMAP-Rule:MF_01338}. Note=In the carboxysome RuBisCO is organized into a paracrystalline array (By similarity). This cyanobacterium makes beta-type carboxysomes (Probable). {ECO:0000250|UniProtKB:Q31NB3, ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, ChEBI:CHEBI:58272; EC=4.1.1.39; Evidence={ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445}; CATALYTIC ACTIVITY: Reaction=D-ribulose 1,5-bisphosphate + O2 = (2R)-3-phosphoglycerate + 2-phosphoglycolate + 2 H(+); Xref=Rhea:RHEA:36631, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57870, ChEBI:CHEBI:58033, ChEBI:CHEBI:58272; Evidence={ECO:0000269|PubMed:9882445};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 uM for ribulose 1,5-bisphosphate {ECO:0000269|PubMed:9882445}; KM=173 uM for CO(2) {ECO:0000269|PubMed:9882445}; Vmax=2.5 umol/min/mg enzyme with CO(2) as substrate {ECO:0000269|PubMed:9882445}; Note=The CO(2)/O(2) specificity factor (tau) is 39.;
| null | null | null |
FUNCTION: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site. {ECO:0000269|PubMed:7922027, ECO:0000269|PubMed:9882445}.
|
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans)
|
P00883
|
ALDOA_RABIT
|
MPHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTPSGQAGAAASESLFISNHAY
|
4.1.2.13
| null |
fructose 1,6-bisphosphate metabolic process [GO:0030388]; glycolytic process [GO:0006096]; negative regulation of Arp2/3 complex-mediated actin nucleation [GO:0034316]; positive regulation of cell migration [GO:0030335]; protein homotetramerization [GO:0051289]
|
cytosol [GO:0005829]; I band [GO:0031674]; M band [GO:0031430]
|
fructose-bisphosphate aldolase activity [GO:0004332]
|
PF00274;
|
3.20.20.70;
|
Class I fructose-bisphosphate aldolase family
|
PTM: Asn-361 in form alpha is deaminated to Asp in form beta.
|
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band {ECO:0000269|PubMed:15757649}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:15757649}. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+).
|
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:20129922, ECO:0000269|PubMed:2204832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; Evidence={ECO:0000305|PubMed:20129922};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14 mM for fructose-l-phosphate {ECO:0000269|PubMed:2204832}; KM=28 uM for fructose-l,6-bisphosphate {ECO:0000269|PubMed:2204832};
|
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
| null | null |
FUNCTION: Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein. {ECO:0000269|PubMed:17329259}.
|
Oryctolagus cuniculus (Rabbit)
|
P00884
|
ALDOB_RAT
|
MAHRFPALTSEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMLTAGHACTKKYTPEQVAMATVTALHRTVPAAVPSICFLSGGMSEEDATLNLNAIYRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVANCQAAQGQYVHTGSSGAASTQSLFTASYTY
|
4.1.2.13
| null |
cellular response to extracellular stimulus [GO:0031668]; cellular response to insulin stimulus [GO:0032869]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose catabolic process [GO:0006001]; fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate [GO:0061624]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; liver development [GO:0001889]; NADH oxidation [GO:0006116]; negative regulation of pentose-phosphate shunt [GO:1905856]; response to amino acid [GO:0043200]; response to cAMP [GO:0051591]; response to carbohydrate [GO:0009743]; response to copper ion [GO:0046688]; response to fructose [GO:0009750]; response to glucocorticoid [GO:0051384]; response to interleukin-6 [GO:0070741]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to starvation [GO:0042594]; response to xenobiotic stimulus [GO:0009410]; response to zinc ion [GO:0010043]; vacuolar proton-transporting V-type ATPase complex assembly [GO:0070072]
|
centriolar satellite [GO:0034451]; cytosol [GO:0005829]; microtubule organizing center [GO:0005815]; perinuclear region of cytoplasm [GO:0048471]; rough endoplasmic reticulum membrane [GO:0030867]; smooth endoplasmic reticulum membrane [GO:0030868]
|
ATPase binding [GO:0051117]; cytoskeletal protein binding [GO:0008092]; fructose binding [GO:0070061]; fructose-1-phosphate aldolase activity [GO:0061609]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; phosphatidylcholine binding [GO:0031210]
|
PF00274;
|
3.20.20.70;
|
Class I fructose-bisphosphate aldolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P05062}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:P05062}.
|
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000250|UniProtKB:P05062}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; Evidence={ECO:0000250|UniProtKB:P05062}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14731; Evidence={ECO:0000250|UniProtKB:P05062}; CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1-phosphate = D-glyceraldehyde + dihydroxyacetone phosphate; Xref=Rhea:RHEA:30851, ChEBI:CHEBI:17378, ChEBI:CHEBI:57642, ChEBI:CHEBI:138881; Evidence={ECO:0000250|UniProtKB:P05062}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30852; Evidence={ECO:0000250|UniProtKB:P05062}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30853; Evidence={ECO:0000250|UniProtKB:P05062};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. {ECO:0000250|UniProtKB:P05062}.; PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000250|UniProtKB:P05062}.; PATHWAY: Carbohydrate metabolism; fructose metabolism. {ECO:0000250|UniProtKB:P05062}.
| null | null |
FUNCTION: Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the phosphorylation of dietary fructose by fructokinase into dihydroxyacetone phosphate and D-glyceraldehyde (By similarity). Acts as an adapter independently of its enzymatic activity, exerts a tumor suppressor role by stabilizing the ternary complex with G6PD and TP53 to inhibit G6PD activity and keep oxidative pentose phosphate metabolism in check (By similarity). {ECO:0000250|UniProtKB:P05062}.
|
Rattus norvegicus (Rat)
|
P00889
|
CISY_PIG
|
MALLTAAARLFGAKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGNTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKMLPKAKGGEEPLPEGLFWLLVTGQIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAITALNSESNFARAYAEGIHRTKYWELIYEDCMDLIAKLPCVAAKIYRNLYREGSSIGAIDSKLDWSHNFTNMLGYTDAQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPLHGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQREFALKHLPHDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYYTVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTDGLIKLVDSK
|
2.3.3.1
| null |
carbohydrate metabolic process [GO:0005975]; citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099]
|
mitochondrial matrix [GO:0005759]
|
citrate (Si)-synthase activity [GO:0004108]; citrate synthase activity [GO:0036440]
|
PF00285;
|
1.10.580.10;1.10.230.10;
|
Citrate synthase family
|
PTM: Methylated (PubMed:7093227). Trimethylation at Lys-395 by CSKMT decreases citrate synthase activity (By similarity). {ECO:0000250|UniProtKB:O75390, ECO:0000269|PubMed:7093227}.
|
SUBCELLULAR LOCATION: Mitochondrion matrix.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10117};
| null |
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.
| null | null | null |
Sus scrofa (Pig)
|
P00890
|
CISY1_YEAST
|
MSAILSTTSKSFLSRGSTRQCQNMQKALFALLNARHYSSASEQTLKERFAEIIPAKAEEIKKFKKEHGKTVIGEVLLEQAYGGMRGIKGLVWEGSVLDPEEGIRFRGRTIPEIQRELPKAEGSTEPLPEALFWLLLTGEIPTDAQVKALSADLAARSEIPEHVIQLLDSLPKDLHPMAQFSIAVTALESESKFAKAYAQGVSKKEYWSYTFEDSLDLLGKLPVIASKIYRNVFKDGKITSTDPNADYGKNLAQLLGYENKDFIDLMRLYLTIHSDHEGGNVSAHTTHLVGSALSSPYLSLAAGLNGLAGPLHGRANQEVLEWLFKLREEVKGDYSKETIEKYLWDTLNAGRVVPGYGHAVLRKTDPRYTAQREFALKHFPDYELFKLVSTIYEVAPGVLTKHGKTKNPWPNVDSHSGVLLQYYGLTEASFYTVLFGVARAIGVLPQLIIDRAVGAPIERPKSFSTEKYKELVKKIESKN
|
2.3.3.1
| null |
acetyl-CoA catabolic process [GO:0046356]; carbohydrate metabolic process [GO:0005975]; citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099]
|
cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
citrate (Si)-synthase activity [GO:0004108]; citrate synthase activity [GO:0036440]
|
PF00285;
|
1.10.580.10;1.10.230.10;
|
Citrate synthase family
|
PTM: Phosphorylation at Ser-462. Dephosphorylated at Ser-462 by PTC7. {ECO:0000269|PubMed:28076776}.
|
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:11502169}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.1; Evidence={ECO:0000269|PubMed:17570335, ECO:0000269|PubMed:28076776};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=76 uM for acetyl-CoA {ECO:0000269|PubMed:17570335}; KM=9.86 uM for oxaloacetate {ECO:0000269|PubMed:28076776}; Vmax=1.92 uM/sec/ug enzyme {ECO:0000269|PubMed:28076776};
|
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. {ECO:0000305}.
| null | null |
FUNCTION: Specific citrate synthase with catalytic activity only with acetyl-CoA. {ECO:0000269|PubMed:17570335, ECO:0000269|PubMed:28076776}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00893
|
ILVI_ECOLI
|
MEMLSGAEMVVRSLIDQGVKQVFGYPGGAVLDIYDALHTVGGIDHVLVRHEQAAVHMADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSFLVKQTEDIPQVLKKAFWLAASGRPGPVVVDLPKDILNPANKLPYVWPESVSMRSYNPTTTGHKGQIKRALQTLVAAKKPVVYVGGGAITAGCHQQLKETVEALNLPVVCSLMGLGAFPATHRQALGMLGMHGTYEANMTMHNADVIFAVGVRFDDRTTNNLAKYCPNATVLHIDIDPTSISKTVTADIPIVGDARQVLEQMLELLSQESAHQPLDEIRDWWQQIEQWRARQCLKYDTHSEKIKPQAVIETLWRLTKGDAYVTSDVGQHQMFAALYYPFDKPRRWINSGGLGTMGFGLPAALGVKMALPEETVVCVTGDGSIQMNIQELSTALQYELPVLVVNLNNRYLGMVKQWQDMIYSGRHSQSYMQSLPDFVRLAEAYGHVGIQISHPHELESKLSEALEQVRNNRLVFVDVTVDGSEHVYPMQIRGGGMDEMWLSKTERT
|
2.2.1.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
|
amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]
|
acetolactate synthase complex [GO:0005948]; cytosol [GO:0005829]
|
acetolactate synthase activity [GO:0003984]; flavin adenine dinucleotide binding [GO:0050660]; magnesium ion binding [GO:0000287]; thiamine pyrophosphate binding [GO:0030976]
|
PF02775;PF00205;PF02776;
|
3.40.50.970;3.40.50.1220;
|
TPP enzyme family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
| null |
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.
| null | null | null |
Escherichia coli (strain K12)
|
P00894
|
ILVH_ECOLI
|
MRRILSVLLENESGALSRVIGLFSQRGYNIESLTVAPTDDPTLSRMTIQTVGDEKVLEQIEKQLHKLVDVLRVSELGQGAHVEREIMLVKIQASGYGRDEVKRNTEIFRGQIIDVTPSLYTVQLAGTSGKLDAFLASIRDVAKIVEVARSGVVGLSRGDKIMR
|
2.2.1.6
| null |
amino acid biosynthetic process [GO:0008652]; branched-chain amino acid biosynthetic process [GO:0009082]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099]
|
acetolactate synthase complex [GO:0005948]; cytosol [GO:0005829]
|
acetolactate synthase activity [GO:0003984]; acetolactate synthase regulator activity [GO:1990610]
|
PF01842;PF10369;
|
3.30.70.260;3.30.70.1150;
|
Acetolactate synthase small subunit family
| null | null |
CATALYTIC ACTIVITY: Reaction=H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2; Xref=Rhea:RHEA:25249, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58476; EC=2.2.1.6;
| null |
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.
| null | null | null |
Escherichia coli (strain K12)
|
P00898
|
TRPE_SALTY
|
MQTPKPTLELLTCDAAYRENPTALFHQVCGDRPATLLLESADIDSKDDLKSLLLVDSALRITALGDTVTIQALSDNGASLLPLLDTALPAGVENDVLPAGRVLRFPPVSPLLDEDARLCSLSVFDAFRLLQGVVNIPTQEREAMFFGGLFAYDLVAGFEALPHLEAGNNCPDYCFYLAETLMVIDHQKKSTRIQASLFTASDREKQRLNARLAYLSQQLTQPAPPLPVTPVPDMRCECNQSDDAFGAVVRQLQKAIRAGEIFQVVPSRRFSLPCPSPLAAYYVLKKSNPSPYMFFMQDNDFTLFGASPESSLKYDAASRQIEIYPIAGTRPRGRRADGTLDRDLDSRIELDMRTDHKELSEHLMLVDLARNDLARICTPGSRYVADLTKVDRYSYVMHLVSRVVGELRHDLDALHAYRACMNMGTLSGAPKVRAMQLIADAEGQRRGSYGGAVGYFTAHGDLDTCIVIRSALVENGIATVQAGAGIVLDSVPQSEADETRNKARAVLRAIATAHHAQETF
|
4.1.3.27
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10089433}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:10089433};
|
tryptophan biosynthetic process [GO:0000162]
| null |
anthranilate synthase activity [GO:0004049]; metal ion binding [GO:0046872]
|
PF04715;PF00425;
|
3.60.120.10;
|
Anthranilate synthase component I family
| null | null |
CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 uM for chorismate {ECO:0000269|PubMed:2022650}; KM=4 uM for anthranilate (with the dimeric form and for the phosphoribosyltransferase activity at pH 7.5) {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945}; KM=6 uM for anthranilate (with the monomeric form and for the phosphoribosyltransferase activity at pH 7.5) {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945}; KM=10 uM for phosphoribosylpyrophosphate (with the monomeric and dimeric forms and for the phosphoribosyltransferase activity at pH 7.5) {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945}; KM=30 uM for magnesium ion (with the monomeric and dimeric forms and for the phosphoribosyltransferase activity at pH 7.5) {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945}; Vmax=5800 nmol/min/mg enzyme (with the dimeric form and for the phosphoribosyltransferase activity at pH 7.5) {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945}; Vmax=4700 nmol/min/mg enzyme (for the monomeric form at pH 7.5) {ECO:0000269|PubMed:2022650, ECO:0000269|PubMed:4358945}; Note=kcat is 12 sec(-1) for chorismate. {ECO:0000269|PubMed:2022650};
|
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
| null | null |
FUNCTION: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. {ECO:0000269|PubMed:4358945}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
P00903
|
PABA_ECOLI
|
MILLIDNYDSFTWNLYQYFCELGADVLVKRNDALTLADIDALKPQKIVISPGPCTPDEAGISLDVIRHYAGRLPILGVCLGHQAMAQAFGGKVVRAAKVMHGKTSPITHNGEGVFRGLANPLTVTRYHSLVVEPDSLPACFDVTAWSETREIMGIRHRQWDLEGVQFHPESILSEQGHQLLANFLHR
|
2.6.1.85
| null |
folic acid biosynthetic process [GO:0046656]; glutamine metabolic process [GO:0006541]; para-aminobenzoic acid biosynthetic process [GO:0008153]; tetrahydrofolate biosynthetic process [GO:0046654]; tryptophan biosynthetic process [GO:0000162]
|
aminodeoxychorismate synthase complex [GO:0009356]; cytosol [GO:0005829]
|
4-amino-4-deoxychorismate synthase activity [GO:0046820]; anthranilate synthase activity [GO:0004049]; protein heterodimerization activity [GO:0046982]
|
PF00117;
|
3.40.50.880;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85; Evidence={ECO:0000269|PubMed:7592344, ECO:0000305|PubMed:4914080}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11673; Evidence={ECO:0000269|PubMed:7592344, ECO:0000305|PubMed:4914080};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.2 uM for chorismate (with the heterodimer PabA-PabB and glutamine as the amino donor at pH 7.5) {ECO:0000269|PubMed:7592344}; KM=18.6 uM for chorismate (with the heterodimer PabA-PabB and ammonia as the amino donor at pH 7.5) {ECO:0000269|PubMed:7592344};
|
PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
| null | null |
FUNCTION: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. {ECO:0000269|PubMed:4914080, ECO:0000269|PubMed:7592344}.
|
Escherichia coli (strain K12)
|
P00904
|
TRPGD_ECOLI
|
MADILLLDNIDSFTYNLADQLRSNGHNVVIYRNHIPAQTLIERLATMSNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLTNPLPVARYHSLVGSNIPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPANTLQPILEKLYQAQTLSQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPDYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGFRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQEQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGHEDLQANAQTVLEVLRSGSAYDRVTALAARG
|
2.4.2.18; 4.1.3.27
| null |
glutamine metabolic process [GO:0006541]; phenazine biosynthetic process [GO:0002047]; tryptophan biosynthetic process [GO:0000162]
|
anthranilate synthase complex [GO:0005950]; cytosol [GO:0005829]
|
anthranilate phosphoribosyltransferase activity [GO:0004048]; anthranilate synthase activity [GO:0004049]; magnesium ion binding [GO:0000287]
|
PF00117;PF02885;PF00591;
|
3.40.50.880;3.40.1030.10;
|
Anthranilate phosphoribosyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; Evidence={ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199}; CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18; Evidence={ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for chorismate (at pH 7.5) {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199}; KM=5 uM for chorismate (at 25 degrees Celsius and at pH 7.8) {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199}; KM=360 uM for glutamine (at pH 7.5) {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199}; Vmax=0.53 nmol/min/mg enzyme (at 25 degrees Celsius and at pH 7.8) {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199};
|
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5. {ECO:0000305|PubMed:2428387, ECO:0000305|PubMed:4567790, ECO:0000305|PubMed:5333199}.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5. {ECO:0000305|PubMed:2428387, ECO:0000305|PubMed:4567790, ECO:0000305|PubMed:5333199}.
| null | null |
FUNCTION: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate. {ECO:0000269|PubMed:2428387, ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:5333199}.
|
Escherichia coli (strain K12)
|
P00905
|
TRPGD_SALTY
|
MADILLLDNIDSFTWNLADQLRTNGHNVVIYRNHIPAQTLIDRLATMKNPVLMLSPGPGVPSEAGCMPELLTRLRGKLPIIGICLGHQAIVEAYGGYVGQAGEILHGKASSIEHDGQAMFAGLANPLPVARYHSLVGSNVPAGLTINAHFNGMVMAVRHDADRVCGFQFHPESILTTQGARLLEQTLAWAQQKLEPTNTLQPILEKLYQAQTLTQQESHQLFSAVVRGELKPEQLAAALVSMKIRGEHPNEIAGAATALLENAAPFPRPEYLFADIVGTGGDGSNSINISTASAFVAAACGLKVAKHGNRSVSSKSGSSDLLAAFGINLDMNADKSRQALDELGVCFLFAPKYHTGLRHAMPVRQQLKTRTLFNVLGPLINPAHPPLALIGVYSPELVLPIAETLRVLGYQRAAVVHSGGMDEVSLHAPTIVAELHDGEIKSYQLTAEDFGLTPYHQDQLAGGTPEENRDILTRLLQGKGDAAHEAAVAANVAMLMRLHGQEDLKANAQTVLDVLRNGTAYDRVTALAARG
|
2.4.2.18; 4.1.3.27
| null |
glutamine metabolic process [GO:0006541]; phenazine biosynthetic process [GO:0002047]; tryptophan biosynthetic process [GO:0000162]
|
cytosol [GO:0005829]
|
anthranilate phosphoribosyltransferase activity [GO:0004048]; anthranilate synthase activity [GO:0004049]; magnesium ion binding [GO:0000287]
|
PF00117;PF02885;PF00591;
|
3.40.50.880;3.40.1030.10;
|
Anthranilate phosphoribosyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; CATALYTIC ACTIVITY: Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-phospho-alpha-D-ribose 1-diphosphate + anthranilate; Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
| null |
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
| null | null |
FUNCTION: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. In addition to synthesizing anthranilate, it also catalyzes the second step of the pathway, the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate. {ECO:0000269|PubMed:4914739}.
|
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
|
P00908
|
TRPG_NEUCR
|
MSSSSVVDHSPHDSAPSPLVPTASNLILIDNYDSFTWNVYQYLVLEGAKVTVFRNDQITIDELIAKNPTQLVISPGPGHPGTDSGISRDAIRHFAGKIPIFGVCMGQQCIFDVYGGDVCFAGEILHGKTSPLRHDGKGAYAGLSQDLPVTRYHSLAGTHVTLPECLEVTSWIAKEDGSKGVIMGVRHKEYTIEGVQFHPESILSAEGRGMFRNFLHMQGGTWAENERLQKAAQAQAANTKSDAPTPKKSNILQKIYAHRKAAVDAQKQIPSLRPSDLQAAYNLSIAPPQISLVDRLRNSPFDVALCAEIKRASPSKGVFALDIDAPSQARKYALAGASVISVLTEPEWFKGSIDDLRAVRQVLNGMPNRPAVLRKEFIFDEYQILEARLAGADTVLLIVKMLEYELLERLYKYSLSLGMEPLVEVQNTEEMATAIKLGAKVIGVNNRNLESFEVDLGTTGRLRSMVPSDTFLCALSGINTHQDVLDCKRDGVNGILVGEAIMRAPDATQFIRELCAGLTGPVPKSAAEPLLVKICGTRSAEAAAEAIKAGADLVGMIMVPGTKRCVDHETALSISQAVHMSKKTGSTEVSSQASKSARDFFNINAEIIRKRGPLLVGVFMNQPLEEVLEKQHLYDLDIVQLHGDEPLEWANLIPVPVVRKFKPGQVGLATRGYHAVPLLDSGAGSGTLLDLESVKKELEKDEQVTVLLAGGLEPSNVVETVKSLGPLSERVIGVDVSSGVEEGGKQSLEKIREFVKAAKSVR
|
4.1.1.48; 4.1.3.27; 5.3.1.24
| null |
glutamine metabolic process [GO:0006541]; tetrahydrofolate biosynthetic process [GO:0046654]; tryptophan biosynthetic process [GO:0000162]
|
cytosol [GO:0005829]
|
4-amino-4-deoxychorismate synthase activity [GO:0046820]; anthranilate synthase activity [GO:0004049]; indole-3-glycerol-phosphate synthase activity [GO:0004425]; phosphoribosylanthranilate isomerase activity [GO:0004640]
|
PF00117;PF00218;PF00697;
|
3.40.50.880;3.20.20.70;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; CATALYTIC ACTIVITY: Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
| null |
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
| null | null |
FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
|
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
|
P00914
|
PHR_ECOLI
|
MTTHLVWFRQDLRLHDNLALAAACRNSSARVLALYIATPRQWATHNMSPRQAELINAQLNGLQIALAEKGIPLLFREVDDFVASVEIVKQVCAENSVTHLFYNYQYEVNERARDVEVERALRNVVCEGFDDSVILPPGAVMTGNHEMYKVFTPFKNAWLKRLREGMPECVAAPKVRSSGSIEPSPSITLNYPRQSFDTAHFPVEEKAAIAQLRQFCQNGAGEYEQQRDFPAVEGTSRLSASLATGGLSPRQCLHRLLAEQPQALDGGAGSVWLNELIWREFYRHLITYHPSLCKHRPFIAWTDRVQWQSNPAHLQAWQEGKTGYPIVDAAMRQLNSTGWMHNRLRMITASFLVKDLLIDWREGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIFNPTTQGEKFDHEGEFIRQWLPELRDVPGKVVHEPWKWAQKAGVTLDYPQPIVEHKEARVQTLAAYEAARKGK
|
4.1.99.3
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.; COFACTOR: Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate; Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000269|PubMed:7604260}; Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit. {ECO:0000269|PubMed:7604260};
|
circadian regulation of gene expression [GO:0032922]; entrainment of circadian clock by photoperiod [GO:0043153]; photoreactive repair [GO:0000719]; phototransduction, visible light [GO:0007603]; response to light stimulus [GO:0009416]
|
cytoplasm [GO:0005737]
|
damaged DNA binding [GO:0003684]; deoxyribodipyrimidine photo-lyase activity [GO:0003904]; DNA binding [GO:0003677]; FAD binding [GO:0071949]
|
PF00875;PF03441;
|
1.25.40.80;1.10.579.10;3.40.50.620;
|
DNA photolyase class-1 family
| null | null |
CATALYTIC ACTIVITY: Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.3;
| null | null | null | null |
FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
|
Escherichia coli (strain K12)
|
P00915
|
CAH1_HUMAN
|
MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362};
|
one-carbon metabolic process [GO:0006730]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
arylesterase activity [GO:0004064]; carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; hydro-lyase activity [GO:0016836]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000269|PubMed:10550681};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4 mM for CO(2) {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:18618712}; KM=15 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:18618712};
| null | null | null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide (PubMed:10550681, PubMed:16506782, PubMed:16686544, PubMed:16807956, PubMed:17127057, PubMed:17314045, PubMed:17407288, PubMed:18618712, PubMed:19186056, PubMed:19206230). Can hydrate cyanamide to urea (PubMed:10550681). {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230}.
|
Homo sapiens (Human)
|
P00917
|
CAH1_HORSE
|
MAHSDWGYDSPNGPZEWVKLYPIANGNNQSPIDIKTSETKHDTSLKPFSVSYDPATAKEIVNVGHSFQVKFEDSDNRSVLKDGPLPGSYRLVQFHFHWGSTDDYGSEHTVDGVKYSAELHLVHWNSSKYSSFDEASSQADGLAILGVLMKVGEANPKLQKVLDALNEVKTKGKKAPFKNFDPSSLLPSSPDYWTYSGSLTHPPLYESVTWIVCKENISISSQQLSQFRSLLSNVEGGKAVPIQHNNRPPQPLKGRTVRAFF
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00915};
|
one-carbon metabolic process [GO:0006730]
|
cytoplasm [GO:0005737]
|
carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; hydro-lyase activity [GO:0016836]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNN3}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P00915}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000250|UniProtKB:P00915};
| null | null | null | null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. {ECO:0000250|UniProtKB:P00915}.
|
Equus caballus (Horse)
|
P00918
|
CAH2_HUMAN
|
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:19583303}; Note=Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II). {ECO:0000269|PubMed:19583303};
|
angiotensin-activated signaling pathway [GO:0038166]; carbon dioxide transport [GO:0015670]; morphogenesis of an epithelium [GO:0002009]; neuron cellular homeostasis [GO:0070050]; one-carbon metabolic process [GO:0006730]; positive regulation of cellular pH reduction [GO:0032849]; positive regulation of dipeptide transmembrane transport [GO:2001150]; positive regulation of synaptic transmission, GABAergic [GO:0032230]; regulation of chloride transport [GO:2001225]; regulation of intracellular pH [GO:0051453]; regulation of monoatomic anion transport [GO:0044070]; secretion [GO:0046903]
|
apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]
|
arylesterase activity [GO:0004064]; carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15990874}. Cell membrane {ECO:0000269|PubMed:15990874}. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells. {ECO:0000269|PubMed:15990874}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:11802772, ECO:0000269|PubMed:11831900, ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236, ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:15453828, ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:15865431, ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:16290146, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17251017, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:17346964, ECO:0000269|PubMed:17540563, ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396, ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572, ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:18640037, ECO:0000269|PubMed:18942852, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:19170619, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230, ECO:0000269|PubMed:19520834, ECO:0000269|PubMed:19778001, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8485129, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:9265618, ECO:0000269|PubMed:9398308}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:11015219};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.3 mM for CO(2) {ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:7761440}; KM=11 mM for CO(2) {ECO:0000269|PubMed:1909891}; KM=8.2 mM for CO(2) {ECO:0000269|PubMed:9398308}; KM=82 mM for H(2)CO(3) {ECO:0000269|PubMed:8262987}; KM=2.9 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:10550681};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-8. {ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:18942852, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:9398308};
| null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide (PubMed:11327835, PubMed:11802772, PubMed:11831900, PubMed:12056894, PubMed:12171926, PubMed:1336460, PubMed:14736236, PubMed:15300855, PubMed:15453828, PubMed:15667203, PubMed:15865431, PubMed:16106378, PubMed:16214338, PubMed:16290146, PubMed:16686544, PubMed:16759856, PubMed:16807956, PubMed:17127057, PubMed:17251017, PubMed:17314045, PubMed:17330962, PubMed:17346964, PubMed:17540563, PubMed:17588751, PubMed:17705204, PubMed:18024029, PubMed:18162396, PubMed:18266323, PubMed:18374572, PubMed:18481843, PubMed:18618712, PubMed:18640037, PubMed:18942852, PubMed:1909891, PubMed:1910042, PubMed:19170619, PubMed:19186056, PubMed:19206230, PubMed:19520834, PubMed:19778001, PubMed:7761440, PubMed:7901850, PubMed:8218160, PubMed:8262987, PubMed:8399159, PubMed:8451242, PubMed:8485129, PubMed:8639494, PubMed:9265618, PubMed:9398308). Can also hydrate cyanamide to urea (PubMed:10550681, PubMed:11015219). Stimulates the chloride-bicarbonate exchange activity of SLC26A6 (PubMed:15990874). Essential for bone resorption and osteoclast differentiation (PubMed:15300855). Involved in the regulation of fluid secretion into the anterior chamber of the eye. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:11015219, ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:11802772, ECO:0000269|PubMed:11831900, ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236, ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:15453828, ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:15865431, ECO:0000269|PubMed:15990874, ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:16290146, ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856, ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17251017, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:17346964, ECO:0000269|PubMed:17540563, ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204, ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396, ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572, ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18618712, ECO:0000269|PubMed:18640037, ECO:0000269|PubMed:18942852, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:19170619, ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230, ECO:0000269|PubMed:19520834, ECO:0000269|PubMed:19778001, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8485129, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:9265618, ECO:0000269|PubMed:9398308}.
|
Homo sapiens (Human)
|
P00919
|
CAH2_RABIT
|
MSHHWGYGKHNGPEHWHKDFPIANGERQSPIDIDTNAAKHDPSLKPLRVCYEHPISRRIINNGHSFNVEFDDSHDKTVLKEGPLEGTYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVKHPDGLAVLGIFLKIGSATPGLQKVVDTLSSIKTKGKSVDFTDFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPITVSSEQMLKFRNLNFNKEAEPEEPMVDNWRPTQPLKGRQVKASFV
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00921};
|
angiotensin-activated signaling pathway [GO:0038166]; carbon dioxide transport [GO:0015670]; positive regulation of dipeptide transmembrane transport [GO:2001150]; regulation of intracellular pH [GO:0051453]; regulation of monoatomic anion transport [GO:0044070]
|
apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell membrane {ECO:0000250|UniProtKB:P00918}. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells (By similarity). {ECO:0000250|UniProtKB:P00918}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P00918}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000250|UniProtKB:P00918};
| null | null | null | null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can also hydrate cyanamide to urea (By similarity). Involved in the regulation of fluid secretion into the anterior chamber of the eye. Essential for bone resorption and osteoclast differentiation. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6. {ECO:0000250|UniProtKB:P00918}.
|
Oryctolagus cuniculus (Rabbit)
|
P00920
|
CAH2_MOUSE
|
MSHHWGYSKHNGPENWHKDFPIANGDRQSPVDIDTATAQHDPALQPLLISYDKAASKSIVNNGHSFNVEFDDSQDNAVLKGGPLSDSYRLIQFHFHWGSSDGQGSEHTVNKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKIGPASQGLQKVLEALHSIKTKGKRAAFANFDPCSLLPGNLDYWTYPGSLTTPPLLECVTWIVLREPITVSSEQMSHFRTLNFNEEGDAEEAMVDNWRPAQPLKNRKIKASFK
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00921};
|
angiotensin-activated signaling pathway [GO:0038166]; carbon dioxide transport [GO:0015670]; morphogenesis of an epithelium [GO:0002009]; neuron cellular homeostasis [GO:0070050]; one-carbon metabolic process [GO:0006730]; positive regulation of bone resorption [GO:0045780]; positive regulation of cellular pH reduction [GO:0032849]; positive regulation of dipeptide transmembrane transport [GO:2001150]; positive regulation of osteoclast differentiation [GO:0045672]; positive regulation of synaptic transmission, GABAergic [GO:0032230]; regulation of chloride transport [GO:2001225]; regulation of intracellular pH [GO:0051453]; regulation of monoatomic anion transport [GO:0044070]; regulation of pH [GO:0006885]; secretion [GO:0046903]
|
apical part of cell [GO:0045177]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; microvillus [GO:0005902]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]
|
arylesterase activity [GO:0004064]; carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell membrane {ECO:0000250|UniProtKB:P00918}. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells. {ECO:0000250|UniProtKB:P00918}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P00918}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000250|UniProtKB:P00918};
| null | null | null | null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide (By similarity). Can also hydrate cyanamide to urea (By similarity). Involved in the regulation of fluid secretion into the anterior chamber of the eye (By similarity). Essential for bone resorption and osteoclast differentiation (By similarity). Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption (By similarity). Stimulates the chloride-bicarbonate exchange activity of SLC26A6 (By similarity). {ECO:0000250|UniProtKB:P00918}.
|
Mus musculus (Mouse)
|
P00921
|
CAH2_BOVIN
|
MSHHWGYGKHNGPEHWHKDFPIANGERQSPVDIDTKAVVQDPALKPLALVYGEATSRRMVNNGHSFNVEYDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDALDSIKTKGKSTDFPNFDPGSLLPNVLDYWTYPGSLTTPPLLESVTWIVLKEPISVSSQQMLKFRTLNFNAEGEPELLMLANWRPAQPLKNRQVRGFPK
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15039588};
|
angiotensin-activated signaling pathway [GO:0038166]; carbon dioxide transport [GO:0015670]; one-carbon metabolic process [GO:0006730]; positive regulation of dipeptide transmembrane transport [GO:2001150]; regulation of intracellular pH [GO:0051453]; regulation of monoatomic anion transport [GO:0044070]
|
apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell membrane {ECO:0000250|UniProtKB:P00918}. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells. {ECO:0000250|UniProtKB:P00918}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P00918}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000250|UniProtKB:P00918};
| null | null | null | null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide (By similarity). Can also hydrate cyanamide to urea (By similarity). Involved in the regulation of fluid secretion into the anterior chamber of the eye (By similarity). Essential for bone resorption and osteoclast differentiation (By similarity). Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption (By similarity). Stimulates the chloride-bicarbonate exchange activity of SLC26A6 (By similarity). {ECO:0000250|UniProtKB:P00918}.
|
Bos taurus (Bovine)
|
P00922
|
CAH2_SHEEP
|
MSHHWGYGEHNGPEHWHKDFPIADGERQSPVDIDTKAVVPDPALKPLALLYEQAASRRMVNNGHSFNVEFDDSQDKAVLKDGPLTGTYRLVQFHFHWGSSDDQGSEHTVDRKKYAAELHLVHWNTKYGDFGTAAQQPDGLAVVGVFLKVGDANPALQKVLDVLDSIKTKGKSADFPNFDPSSLLKRALNYWTYPGSLTNPPLLESVTWVVLKEPTSVSSQQMLKFRSLNFNAEGEPELLMLANWRPAQPLKNRQVRVFPK
|
4.2.1.1; 4.2.1.69
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00921};
|
angiotensin-activated signaling pathway [GO:0038166]; carbon dioxide transport [GO:0015670]; positive regulation of dipeptide transmembrane transport [GO:2001150]; regulation of intracellular pH [GO:0051453]; regulation of monoatomic anion transport [GO:0044070]
|
apical part of cell [GO:0045177]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
carbonate dehydratase activity [GO:0004089]; cyanamide hydratase activity [GO:0018820]; zinc ion binding [GO:0008270]
|
PF00194;
|
3.10.200.10;
|
Alpha-carbonic anhydrase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00918}. Cell membrane {ECO:0000250|UniProtKB:P00918}. Note=Colocalized with SLC26A6 at the surface of the cell membrane in order to form a bicarbonate transport metabolon. Displaced from the cytosolic surface of the cell membrane by PKC in phorbol myristate acetate (PMA)-induced cells (By similarity). {ECO:0000250|UniProtKB:P00918}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P00918}; CATALYTIC ACTIVITY: Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69; Evidence={ECO:0000250|UniProtKB:P00918};
| null | null | null | null |
FUNCTION: Catalyzes the reversible hydration of carbon dioxide. Can also hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye. Essential for bone resorption and osteoclast differentiation. Contributes to intracellular pH regulation in the duodenal upper villous epithelium during proton-coupled peptide absorption. Stimulates the chloride-bicarbonate exchange activity of SLC26A6. {ECO:0000250|UniProtKB:P00918}.
|
Ovis aries (Sheep)
|
P00924
|
ENO1_YEAST
|
MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGKGVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASRAAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKIKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDNAVFAGENFHHGDKL
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:8605183}; Note=Mg(2+) is required for catalysis and for stabilizing the dimer. {ECO:0000269|PubMed:8605183};
|
glycolytic process [GO:0006096]; regulation of vacuole fusion, non-autophagic [GO:0032889]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; fungal-type vacuole [GO:0000324]; mitochondrion [GO:0005739]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]
|
magnesium ion binding [GO:0000287]; melatonin binding [GO:1904408]; phosphopyruvate hydratase activity [GO:0004634]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11502169}.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11;
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00925
|
ENO2_YEAST
|
MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDEDKSKWMGKGVMNAVNNVNNVIAAAFVKANLDVKDQKAVDDFLLSLDGTANKSKLGANAILGVSMAAARAAAAEKNVPLYQHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEAMRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASSEFFKDGKYDLDFKNPESDKSKWLTGVELADMYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPARIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAANWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDKAVYAGENFHHGDKL
|
4.2.1.11
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.;
|
glycolytic process [GO:0006096]; regulation of vacuole fusion, non-autophagic [GO:0032889]
|
cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; fungal-type vacuole [GO:0000324]; mitochondrion [GO:0005739]; phosphopyruvate hydratase complex [GO:0000015]; plasma membrane [GO:0005886]
|
magnesium ion binding [GO:0000287]; melatonin binding [GO:1904408]; phosphopyruvate hydratase activity [GO:0004634]
|
PF00113;PF03952;
|
3.20.20.120;3.30.390.10;
|
Enolase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11;
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00926
|
SDHD_ECOLI
|
MENAKMNSLIAQYPLVKDLVALKETTWFNPGTTSLAEGLPYVGLTEQDVQDAHARLSRFAPYLAKAFPETAATGGIIESELVAIPAMQKRLEKEYQQPISGQLLLKKDSHLPISGSIKARGGIYEVLAHAEKLALEAGLLTLDDDYSKLLSPEFKQFFSQYSIAVGSTGNLGLSIGIMSARIGFKVTVHMSADARAWKKAKLRSHGVTVVEYEQDYGVAVEEGRKAAQSDPNCFFIDDENSRTLFLGYSVAGQRLKAQFAQQGRIVDADNPLFVYLPCGVGGGPGGVAFGLKLAFGDHVHCFFAEPTHSPCMLLGVHTGLHDQISVQDIGIDNLTAADGLAVGRASGFVGRAMERLLDGFYTLSDQTMYDMLGWLAQEEGIRLEPSALAGMAGPQRVCASVSYQQMHGFSAEQLRNTTHLVWATGGGMVPEEEMNQYLAKGR
|
4.3.1.18
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:22197591};
|
D-serine catabolic process [GO:0036088]; D-serine metabolic process [GO:0070178]; detoxification of nitrogen compound [GO:0051410]; DNA damage response [GO:0006974]; isoleucine biosynthetic process [GO:0009097]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
D-serine ammonia-lyase activity [GO:0008721]; hydro-lyase activity [GO:0016836]; pyridoxal phosphate binding [GO:0030170]
|
PF00291;
|
3.40.50.1100;
|
Serine/threonine dehydratase family, DsdA subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
| null | null | null | null | null |
Escherichia coli (strain K12)
|
P00927
|
THDH_YEAST
|
MSATLLKQPLCTVVRQGKQSKVSGLNLLRLKAHLHRQHLSPSLIKLHSELKLDELQTDNTPDYVRLVLRSSVYDVINESPISQGVGLSSRLNTNVILKREDLLPVFSFKLRGAYNMIAKLDDSQRNQGVIACSAGNHAQGVAFAAKHLKIPATIVMPVCTPSIKYQNVSRLGSQVVLYGNDFDEAKAECAKLAEERGLTNIPPFDHPYVIAGQGTVAMEILRQVRTANKIGAVFVPVGGGGLIAGIGAYLKRVAPHIKIIGVETYDAATLHNSLQRNQRTPLPVVGTFADGTSVRMIGEETFRVAQQVVDEVVLVNTDEICAAVKDIFEDTRSIVEPSGALSVAGMKKYISTVHPEIDHTKNTYVPILSGANMNFDRLRFVSERAVLGEGKEVFMLVTLPDVPGAFKKMQKIIHPRSVTEFSYRYNEHRHESSSEVPKAYIYTSFSVVDREKEIKQVMQQLNALGFEAVDISDNELAKSHGRYLVGGASKVPNERIISFEFPERPGALTRFLGGLSDSWNLTLFHYRNHGADIGKVLAGISVPPRENLTFQKFLEDLGYTYHDETDNTVYQKFLKY
|
4.3.1.19
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
|
amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; L-serine catabolic process [GO:0006565]; threonine catabolic process [GO:0006567]
|
mitochondrion [GO:0005739]
|
L-serine ammonia-lyase activity [GO:0003941]; pyridoxal phosphate binding [GO:0030170]; threonine deaminase activity [GO:0004794]
|
PF00291;PF00585;
|
3.40.50.1100;
|
Serine/threonine dehydratase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
|
CATALYTIC ACTIVITY: Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19; Evidence={ECO:0000269|PubMed:3289762};
| null |
PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00935
|
METB_ECOLI
|
MTRKQATIAVRSGLNDDEQYGCVVPPIHLSSTYNFTGFNEPRAHDYSRRGNPTRDVVQRALAELEGGAGAVLTNTGMSAIHLVTTVFLKPGDLLVAPHDCYGGSYRLFDSLAKRGCYRVLFVDQGDEQALRAALAEKPKLVLVESPSNPLLRVVDIAKICHLAREVGAVSVVDNTFLSPALQNPLALGADLVLHSCTKYLNGHSDVVAGVVIAKDPDVVTELAWWANNIGVTGGAFDSYLLLRGLRTLVPRMELAQRNAQAIVKYLQTQPLVKKLYHPSLPENQGHEIAARQQKGFGAMLSFELDGDEQTLRRFLGGLSLFTLAESLGGVESLISHAATMTHAGMAPEARAAAGISETLLRISTGIEDGEDLIADLENGFRAANKG
|
2.5.1.48
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:2405903}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000269|PubMed:2405903};
|
cysteine biosynthetic process via cystathionine [GO:0019343]; methionine biosynthetic process [GO:0009086]; transsulfuration [GO:0019346]
|
cytoplasm [GO:0005737]
|
cystathionine gamma-lyase activity [GO:0004123]; cystathionine gamma-synthase activity [GO:0003962]; cystathionine gamma-synthase activity (acts on O-phosphohomoserine) [GO:0102028]; pyridoxal phosphate binding [GO:0030170]
|
PF01053;
|
3.90.1150.10;3.40.640.10;
|
Trans-sulfuration enzymes family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=L-cysteine + O-succinyl-L-homoserine = H(+) + L,L-cystathionine + succinate; Xref=Rhea:RHEA:20397, ChEBI:CHEBI:15378, ChEBI:CHEBI:30031, ChEBI:CHEBI:35235, ChEBI:CHEBI:57661, ChEBI:CHEBI:58161; EC=2.5.1.48; Evidence={ECO:0000269|PubMed:2405903};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.33 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-elimination reaction) {ECO:0000269|PubMed:2405903}; KM=1 mM for O-succinyl-L-homoserine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction) {ECO:0000269|PubMed:2405903}; KM=0.05 mM for L-cysteine (at pH 8.2 and 25 degrees Celsius, when assaying the gamma-replacement reaction) {ECO:0000269|PubMed:2405903}; Note=kcat are 700 min(-1) and 460 min(-1) for the gamma-replacement and gamma-elimination reaction, respectively.;
|
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-cystathionine from O-succinyl-L-homoserine: step 1/1.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 for the gamma-replacement reaction. {ECO:0000269|PubMed:2405903};
| null |
FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia. {ECO:0000269|PubMed:2405903}.
|
Escherichia coli (strain K12)
|
P00936
|
CYAA_ECOLI
|
MYLYIETLKQRLDAINQLRVDRALAAMGPAFQQVYSLLPTLLHYHHPLMPGYLDGNVPKGICLYTPDETQRHYLNELELYRGMSVQDPPKGELPITGVYTMGSTSSVGQSCSSDLDIWVCHQSWLDSEERQLLQRKCSLLENWAASLGVEVSFFLIDENRFRHNESGSLGGEDCGSTQHILLLDEFYRTAVRLAGKRILWNMVPCDEEEHYDDYVMTLYAQGVLTPNEWLDLGGLSSLSAEEYFGASLWQLYKSIDSPYKAVLKTLLLEAYSWEYPNPRLLAKDIKQRLHDGEIVSFGLDPYCMMLERVTEYLTAIEDFTRLDLVRRCFYLKVCEKLSRERACVGWRRAVLSQLVSEWGWDEARLAMLDNRANWKIDQVREAHNELLDAMMQSYRNLIRFARRNNLSVSASPQDIGVLTRKLYAAFEALPGKVTLVNPQISPDLSEPNLTFIYVPPGRANRSGWYLYNRAPNIESIISHQPLEYNRYLNKLVAWAWFNGLLTSRTRLYIKGNGIVDLPKLQEMVADVSHHFPLRLPAPTPKALYSPCEIRHLAIIVNLEYDPTAAFRNQVVHFDFRKLDVFSFGENQNCLVGSVDLLYRNSWNEVRTLHFNGEQSMIEALKTILGKMHQDAAPPDSVEVFCYSQHLRGLIRTRVQQLVSECIELRLSSTRQETGRFKALRVSGQTWGLFFERLNVSVQKLENAIEFYGAISHNKLHGLSVQVETNHVKLPAVVDGFASEGIIQFFFEETQDENGFNIYILDESNRVEVYHHCEGSKEELVRDVSRFYSSSHDRFTYGSSFINFNLPQFYQIVKVDGREQVIPFRTKSIGNMPPANQDHDTPLLQQYFS
|
4.6.1.1
| null |
cAMP biosynthetic process [GO:0006171]
|
cytoplasm [GO:0005737]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]
|
PF12633;PF01295;
| null |
Adenylyl cyclase class-1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
| null | null | null | null |
FUNCTION: Catalyzes the formation of the second messenger cAMP from ATP. Its transcript is probably degraded by endoribonuclease LS (rnlA), decreasing cAMP levels and the negative regulator Crp-cAMP, which then induces its own transcription again.
|
Escherichia coli (strain K12)
|
P00937
|
TRPG_YEAST
|
MSVHAATNPINKHVVLIDNYDSFTWNVYEYLCQEGAKVSVYRNDAITVPEIAALNPDTLLISPGPGHPKTDSGISRDCIRYFTGKIPVFGICMGQQCMFDVFGGEVAYAGEIVHGKTSPISHDNCGIFKNVPQGIAVTRYHSLAGTESSLPSCLKVTASTENGIIMGVRHKKYTVEGVQFHPESILTEEGHLMIRNILNVSGGTWEENKSSPSNSILDRIYARRKIDVNEQSKIPGFTFQDLQSNYDLGLAPPLQDFYTVLSSSHKRAVVLAEVKRASPSKGPICLKAVAAEQALKYAEAGASAISVLTEPHWFHGSLQDLVNVRKILDLKFPPKERPCVLRKEFIFSKYQILEARLAGADTVLLIVKMLSQPLLKELYSYSKDLNMEPLVEVNSKEELQRALEIGAKVVGVNNRDLHSFNVDLNTTSNLVESIPKDVLLIALSGITTRDDAEKYKKEGVHGFLVGEALMKSTDVKKFIHELCE
|
4.1.1.48; 4.1.3.27
| null |
glutamine metabolic process [GO:0006541]; tetrahydrofolate biosynthetic process [GO:0046654]; tryptophan biosynthetic process [GO:0000162]
|
anthranilate synthase complex [GO:0005950]; cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
4-amino-4-deoxychorismate synthase activity [GO:0046820]; anthranilate synthase activity [GO:0004049]; indole-3-glycerol-phosphate synthase activity [GO:0004425]
|
PF00117;PF00218;
|
3.40.50.880;3.20.20.70;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate + pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27; CATALYTIC ACTIVITY: Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O; Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
| null |
PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00939
|
TPIS_RABIT
|
MAPSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
|
4.2.3.3; 5.3.1.1
| null |
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; methylglyoxal biosynthetic process [GO:0019242]
|
cytosol [GO:0005829]
|
methylglyoxal synthase activity [GO:0008929]; protein homodimerization activity [GO:0042803]; triose-phosphate isomerase activity [GO:0004807]; ubiquitin protein ligase binding [GO:0031625]
|
PF00121;
|
3.20.20.70;
|
Triosephosphate isomerase family
|
PTM: Asn-16 and Asn-72 undergo deamidation which gives rise to four extra negative charges. These are expected to decrease subunit-subunit interactions and so expose the hydrophobic interface to the aqueous environment. {ECO:0000269|PubMed:7574709}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000269|PubMed:2021650}; CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000269|PubMed:2021650};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.62 mM for dihydroxyacetone phosphate (at pH 7.9) {ECO:0000269|PubMed:2021650}; Note=The kcat is 900 sec(-1) for the isomerization of dihydroxyacetone phosphate (PubMed:2021650). The kcat is 0.011 sec(-1) for the production of methylglyoxal via the elimination reaction (PubMed:2021650). Produces methylglyoxal with a calculated cellular velocity of 0.4 mM per day (PubMed:2021650). {ECO:0000269|PubMed:2021650};
|
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-ProRule:PRU10127}.; PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|PROSITE-ProRule:PRU10127}.
| null | null |
FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000305|PubMed:2021650}.; FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. {ECO:0000269|PubMed:2021650}.
|
Oryctolagus cuniculus (Rabbit)
|
P00940
|
TPIS_CHICK
|
MAPRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQKLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSHVSDAVAQSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH
|
4.2.3.3; 5.3.1.1
| null |
canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]; methylglyoxal biosynthetic process [GO:0019242]
|
cytosol [GO:0005829]
|
methylglyoxal synthase activity [GO:0008929]; protein homodimerization activity [GO:0042803]; triose-phosphate isomerase activity [GO:0004807]; ubiquitin protein ligase binding [GO:0031625]
|
PF00121;
|
3.20.20.70;
|
Triosephosphate isomerase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
|
CATALYTIC ACTIVITY: Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, ChEBI:CHEBI:57642; EC=4.2.3.3; Evidence={ECO:0000250|UniProtKB:P00939}; CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10127};
| null |
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE-ProRule:PRU10127}.; PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|PROSITE-ProRule:PRU10127}.
| null | null |
FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis. {ECO:0000250|UniProtKB:P00939}.; FUNCTION: It is also responsible for the non-negligible production of methylglyoxal a reactive cytotoxic side-product that modifies and can alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}.
|
Gallus gallus (Chicken)
|
P00942
|
TPIS_YEAST
|
MARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN
|
5.3.1.1
| null |
gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
triose-phosphate isomerase activity [GO:0004807]
|
PF00121;
|
3.20.20.70;
|
Triosephosphate isomerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1;
| null |
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1.
| null | null | null |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P00943
|
TPIS_GEOSE
|
MRKPIIAGNWKMHKTLAEAVQFVEDVKGHVPPADEVISVVCAPFLFLDRLVQAADGTDLKIGAQTMHFADQGAYTGEVSPVMLKDLGVTYVILGHSERRQMFAETDETVNKKVLAAFTRGLIPIICCGESLEEREAGQTNAVVASQVEKALAGLTPEQVKQAVIAYEPIWAIGTGKSSTPEDANSVCGHIRSVVSRLFGPEAAEAIRIQYGGSVKPDNIRDFLAQQQIDGPLVGGASLEPASFLQLVEAGRHE
|
5.3.1.1
| null |
gluconeogenesis [GO:0006094]; glyceraldehyde-3-phosphate biosynthetic process [GO:0046166]; glycerol catabolic process [GO:0019563]; glycolytic process [GO:0006096]
|
cytosol [GO:0005829]
|
triose-phosphate isomerase activity [GO:0004807]
|
PF00121;
|
3.20.20.70;
|
Triosephosphate isomerase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=5.3.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00147};
| null |
PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. {ECO:0000255|HAMAP-Rule:MF_00147}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00147}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius (PubMed:8421318). Thermostable (PubMed:10383424). {ECO:0000269|PubMed:10383424, ECO:0000269|PubMed:8421318};
|
FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:8421318}.
|
Geobacillus stearothermophilus (Bacillus stearothermophilus)
|
P00946
|
MANA_ECOLI
|
MQKLINSVQNYAWGSKTALTELYGMENPSSQPMAELWMGAHPKSSSRVQNAAGDIVSLRDVIESDKSTLLGEAVAKRFGELPFLFKVLCAAQPLSIQVHPNKHNSEIGFAKENAAGIPMDAAERNYKDPNHKPELVFALTPFLAMNAFREFSEIVSLLQPVAGAHPAIAHFLQQPDAERLSELFASLLNMQGEEKSRALAILKSALDSQQGEPWQTIRLISEFYPEDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANQLLTQPVKQGAELDFPIPVDDFAFSLHDLSDKETTISQQSAAILFCVEGDATLWKGSQQLQLKPGESAFIAANESPVTVKGHGRLARVYNKL
|
5.3.1.8
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
colanic acid biosynthetic process [GO:0009242]; GDP-mannose biosynthetic process [GO:0009298]; mannose catabolic process [GO:0019309]
|
cytosol [GO:0005829]
|
mannose-6-phosphate isomerase activity [GO:0004476]; zinc ion binding [GO:0008270]
|
PF21621;PF20511;PF20512;
|
2.60.120.10;1.10.441.10;
|
Mannose-6-phosphate isomerase type 1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=D-mannose 6-phosphate = D-fructose 6-phosphate; Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527; EC=5.3.1.8;
| null | null | null | null |
FUNCTION: Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide.
|
Escherichia coli (strain K12)
|
P00949
|
PGM1_RABIT
|
MVKIVTVKTKAYPDQKPGTSGLRKRVKVFQSSTNYAENFIQSIISTVEPAQRQEATLVVGGDGRFYMKEAIQLIVRIAAANGIGRLVIGQNGILSTPAVSCIIRKIKAIGGIILTASHNPGGPNGDFGIKFNISNGGPAPEAITDKIFQISKTIEEYAICPDLKVDLGVLGKQQFDLENKFKPFTVEIVDSVEAYATMLRNIFDFNALKELLSGPNRLKIRIDAMHGVVGPYVKKILCEELGAPANSAVNCVPLEDFGGHHPDPNLTYAADLVETMKSGEHDFGAAFDGDGDRNMILGKHGFFVNPSDSVAVIAANIFSIPYFQQTGVRGFARSMPTSGALDRVANATKIALYETPTGWKFFGNLMDASKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILATRKQSVEDILKDHWHKFGRNFFTRYDYEEVEAEGATKMMKDLEALMFDRSFVGKQFSANDKVYTVEKADNFEYHDPVDGSVSKNQGLRLIFADGSRIIFRLSGTGSAGATIRLYIDSYEKDNAKINQDPQVMLAPLISIALKVSQLQERTGRTAPTVIT
|
5.4.2.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15299905}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:15299905};
|
glucose metabolic process [GO:0006006]
|
cytosol [GO:0005829]; sarcoplasmic reticulum [GO:0016529]
|
magnesium ion binding [GO:0000287]; phosphoglucomutase activity [GO:0004614]
|
PF02878;PF02879;PF02880;
|
3.40.120.10;3.30.310.50;
|
Phosphohexose mutase family
|
PTM: Isoform 2 is the major calmodulin-dependent phosphoprotein in junctional skeletal sarcoplasmic reticulum vesicles. {ECO:0000269|PubMed:1328221}.; PTM: Phosphorylation at Thr-467 by PAK1 significantly enhances enzymatic activity. {ECO:0000250|UniProtKB:P36871}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 2]: Sarcoplasmic reticulum {ECO:0000269|PubMed:1328221}. Note=Localizes to the junctional skeletal sarcoplasmic reticulum, probably by association with phospholipids and/or other proteins. {ECO:0000269|PubMed:1328221}.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000269|PubMed:1328221}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]; Xref=Rhea:RHEA:68748, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58392, ChEBI:CHEBI:58601, ChEBI:CHEBI:83421; Evidence={ECO:0000305|PubMed:1328221}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = alpha-D-glucose 6-phosphate + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:68752, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58225, ChEBI:CHEBI:58392, ChEBI:CHEBI:83421; Evidence={ECO:0000305|PubMed:1328221};
| null | null | null | null |
FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (PubMed:1328221). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable). This enzyme participates in both the breakdown and synthesis of glucose (By similarity). {ECO:0000250|UniProtKB:P36871, ECO:0000269|PubMed:1328221, ECO:0000305|PubMed:1328221}.
|
Oryctolagus cuniculus (Rabbit)
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.