ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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D2NT93 | MEHRIFGIESEFGLSYVPHGLGRLSIEESAAALFKPVLDQWRSTNVFLPNGGRLYLDVGSHPEYASAECGSIDELLAQERAGELLFADLARTARKRLLAGSEGRPLDGELYLFKNNVDSAGNSYGSHENYLISRKLQFNDLIAQLVPFLVTRQILVGAGKTHPNGGPVPGSTDPASSTGVPSYSFSQRADHIWEAASTSTSRARPLINTRDEPHADASKFRRMHVINGDSNMAEPTTLLKIASTDLVLRMLEDRFPVTSLDIVSVPAALRAISHDLTGTATFETTDGKHYTALSVQRHYLDAARQYVQQYGAHHHHVEYALDLWQRTLDAIESGDYSSIDSEIDWAIKKKLLDAYIARARAAGQPADYASARIRQLDLAYHDIDPERSVFHALVRRGAVKRILPEGAAEAAKTQPPNTRALQRSRFINAAVAAGEQFTVDWVHLKLNAYPQHTLVCKDPFATDSEGLEEVLTLLEGKARQHQEAAFPPPC | Function: Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine.
Catalytic Activity: ATP + [prokaryotic ubiquitin-like protein]-L-glutamate + [protein]-L-lysine = ADP + phosphate + N(6)-([prokaryotic ubiquitin-like protein]-gamma-L-glutamyl)-[protein]-L-lysine.
Sequence Mass (Da): 54082
Sequence Length: 490
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
EC: 6.3.1.19
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Q9HL57 | MSIEIRKLSIEDLETLIEVARESWKWTYAGIYSEEYIESWIREKYSKEKLLNEIVRSQSNLDILFLGAFADSTLIGFIELKIIANKAELLRLYLKPEYTHKKIGKTLLLEAEKIMKKKGILECRLYVHRQNSVGFSFYYKNGFKVEDTDGSDFIMEKKYES | Function: Involved in the protection against polyamine toxicity by regulating their concentration. Could also be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. It can use a variety of substrates including spermidine, L-tryptophan, L-leucine, L-lysine, dopamine and tyramine.
Catalytic Activity: acetyl-CoA + an alkane-alpha,omega-diamine = an N-acetylalkane-alpha,omega-diamine + CoA + H(+)
Sequence Mass (Da): 18997
Sequence Length: 161
EC: 2.3.1.57
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Q9W0Y6 | MDFNNCGFIDPQAQLAGALAKQDIRQFVAALDSGALADLQDDRHTSIYEKALSTPGCRDFIEACIDHGSQVNYINKKLDKAAISYAADSRDPGNLAALLKYRPGNKVQVDRKYGQLTPLNSLAKNLTDENAPDVYSCMQLLLDYGASPNIVDQGEFTPLHHVLRKSKVKAGKKELIQLFLDHPELDIDSYRNGEVRRLLQAQFPELKLPEERHTGPEIDIQTLQRTLRDGDETLFEQQFAEYLQNLKGGADNQLNAHQEEYFGLLQESIKRGRQRAFDVILSTGMDINSRPGRANEANLVETAVIYGNWQALERLLKEPNLRLTPDSKLLNAVIGRLDEPPYDGSSHQRCFELLINSDRVDINEADSGRLVPLFFAVKYRNTSAMQKLLKNGAYIGSKSAFGTLPIKDMPPEVLEEHFDSCITTNGERPGDQNFEIIIDYKNLMRQERDSGLNQLQDEMAPIAFIAESKEMRHLLQHPLISSFLFLKWHRLSVIFYLNFLIYSLFTASIITYTLLKFHESDQRALTAFFGLLSWLGISYLILRECIQWIMSPVRYFWSITNIMEVALITLSIFTCMESSFDKETQRVLAVFTILLVSMEFCLLVGSLPVLSISTHMLMLREVSNSFLKSFTLYSIFVLTFSLCFYILFGKSVEEDQSKSATPCPPLGKKEGKDEEQGFNTFTKPIEAVIKTIVMLTGEFDAGSIQFTSIYTYLIFLLFVIFMTIVLFNLLNGLAVSDTQVIKAQAELNGAICRTNVLSRYEQVLTGHGRAGFLLGNHLFRSICQRLMNIYPNYLSLRQISVLPNDGNKVLIPMSDPFEMRTLKKASFQQLPLSAAVPQKKLLDPPLRLLPCCCSLLTGKCSQMSGRVVKRALEVIDQKNAAEQRRKQEQINDSRLKLIEYKLEQLIQLVQDRK | Function: Receptor-activated non-selective cation channel involved in detection of pain sensation due to high temperature. Involved in heat nociception by being activated by noxious temperature of 38 degrees Celsius.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 103507
Sequence Length: 913
Subcellular Location: Membrane
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Q9H074 | MSDGFDRAPGAGRGRSRGLGRGGGGPEGGGFPNGAGPAERARHQPPQPKAPGFLQPPPLRQPRTTPPPGAQCEVPASPQRPSRPGALPEQTRPLRAPPSSQDKIPQQNSESAMAKPQVVVAPVLMSKLSVNAPEFYPSGYSSSYTESYEDGCEDYPTLSEYVQDFLNHLTEQPGSFETEIEQFAETLNGCVTTDDALQELVELIYQQATSIPNFSYMGARLCNYLSHHLTISPQSGNFRQLLLQRCRTEYEVKDQAAKGDEVTRKRFHAFVLFLGELYLNLEIKGTNGQVTRADILQVGLRELLNALFSNPMDDNLICAVKLLKLTGSVLEDAWKEKGKMDMEEIIQRIENVVLDANCSRDVKQMLLKLVELRSSNWGRVHATSTYREATPENDPNYFMNEPTFYTSDGVPFTAADPDYQEKYQELLEREDFFPDYEENGTDLSGAGDPYLDDIDDEMDPEIEEAYEKFCLESERKRKQ | Function: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain.
Sequence Mass (Da): 53525
Sequence Length: 479
Domain: Only the PABPC1-interacting motif-1 (PAM1) stimulates translation initiation.
Subcellular Location: Cytoplasm
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Q8VE62 | MSDSFDRAPEQTKPQRAPPSSQDKIPQQNSESAMAKPQVVVAPVLMSKLSANAPEFYPSGYSSNYTESYEDGCEDYPTLSEYVQDFLNHLTEQPGSFETEIEQFAETLNGWVTTDDALQELVELIYQQATSIPNFSYMGARLCNYLSHHLTISPQSGNFRQLLLQRCRTEYEAKDQAAKGDEVTRKRFHAFVLFLGELYLNLEIKGTNGQVTRADILQVGLRELLNALFSNPMDDNLICAVKLLKLTGSVLEDTWKEKGKTDMEEIIQRIENVVLDANCSRDVKQMLLKLVELRSSNWGRVHATSTYREATPENDPNYFMNEPTFYTSDGVPFTAADPDYQEKYQELLEREDFFPDYEENGTDLSGAGDPYLDDIDDEMDPEIEEAYEKFCLESERKRKQ | Function: Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain (By similarity).
Sequence Mass (Da): 45702
Sequence Length: 400
Domain: Only the PABPC1-interacting motif-1 (PAM1) stimulates translation initiation.
Subcellular Location: Cytoplasm
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Q3ZC67 | MKDPSRSSTSPSIINEDVIINGHSHEDDNPFAEYMWMENEEEFNRQIEEELWEEEFIERCFQEMLEEEEEHEWFIPARDLPQTMDQIQDQFNDLVISDGSSLEDLVVKSNLNPNAKEFVPGVKY | Function: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization (By similarity).
PTM: Ubiquitinated, leading to its degradation by the proteasome.
Sequence Mass (Da): 14700
Sequence Length: 124
Domain: Only the PABPC1-interacting motif-1 (PAM1) interferes with the binding of PABPC1 to poly(A) RNA and translation initiation.
Subcellular Location: Cytoplasm
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Q9BPZ3 | MKDPSRSSTSPSIINEDVIINGHSHEDDNPFAEYMWMENEEEFNRQIEEELWEEEFIERCFQEMLEEEEEHEWFIPARDLPQTMDQIQDQFNDLVISDGSSLEDLVVKSNLNPNAKEFVPGVKYGNI | Function: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization.
PTM: Ubiquitinated, leading to its degradation by the proteasome.
Sequence Mass (Da): 14984
Sequence Length: 127
Domain: Only the PABPC1-interacting motif-1 (PAM1) interferes with the binding of PABPC1 to poly(A) RNA and translation initiation.
Subcellular Location: Cytoplasm
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Q5R596 | MKDPSRSSTSPSIINEDVIINGHSHEDDNPFAEYMWMENEEEFNRQIEEELWEEEFIERCFQEMLEEEEEHEWFIPARDLPQTMDQIQDQFNELVISDSSSLEDLVVKSNLNPNAKEFVPGVKY | Function: Acts as a repressor in the regulation of translation initiation of poly(A)-containing mRNAs. Its inhibitory activity on translation is mediated via its action on PABPC1. Displaces the interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for binding to PABPC1. Its association with PABPC1 results in disruption of the cytoplasmic poly(A) RNP structure organization (By similarity).
PTM: Ubiquitinated, leading to its degradation by the proteasome.
Sequence Mass (Da): 14744
Sequence Length: 124
Domain: Only the PABPC1-interacting motif-1 (PAM1) interferes with the binding of PABPC1 to poly(A) RNA and translation initiation.
Subcellular Location: Cytoplasm
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Q13153 | MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH | Function: Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes . Can directly phosphorylate BAD and protects cells against apoptosis (By similarity). Activated by interaction with CDC42 and RAC1 . Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway . Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases (By similarity). Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes . Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton . Plays a role in the regulation of insulin secretion in response to elevated glucose levels . Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) (By similarity). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2 . Phosphorylates MYL9/MLC2 (By similarity). Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2 . Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus . In podocytes, promotes NR3C2 nuclear localization (By similarity). Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation . In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation (By similarity). Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion . In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling . In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization (By similarity). In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity). Along with GIT1, positively regulates microtubule nucleation during interphase . Phosphorylates FXR1, promoting its localization to stress granules and activity .
PTM: Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one . Activated by autophosphorylation at Thr-423 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1 . Activated by phosphorylation at Thr-423 by BRSK2 and by PDPK1 . Phosphorylated by JAK2 in response to PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites . Upon DNA damage, phosphorylated at Thr-212 and translocates to the nucleoplasm . Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 60647
Sequence Length: 545
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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P35465 | MSNNGLDVQDKPPAPPMRNTSTMIGAGSKDPGTLNHGSKPLPPNPEEKKKKDRFYRSILAGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNTLNVKTVSETPAVPPVSEDEDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH | Function: Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes . Can directly phosphorylate BAD and protects cells against apoptosis (By similarity). Activated by interaction with CDC42 and RAC1 . Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway . Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases . Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes . Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton (By similarity). Plays a role in the regulation of insulin secretion in response to elevated glucose levels (By similarity). Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ) (By similarity). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2 (By similarity). Phosphorylates MYL9/MLC2 (By similarity). Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2 (By similarity). Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus (By similarity). In podocytes, promotes NR3C2 nuclear localization . Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (By similarity). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation . Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion (By similarity). In response to DNA damage, phosphorylates MORC2 which activates its ATPase activity and facilitates chromatin remodeling (By similarity). In neurons, plays a crucial role in regulating GABA(A) receptor synaptic stability and hence GABAergic inhibitory synaptic transmission through its role in F-actin stabilization . In hippocampal neurons, necessary for the formation of dendritic spines and excitatory synapses; this function is dependent on kinase activity and may be exerted by the regulation of actomyosin contractility through the phosphorylation of myosin II regulatory light chain (MLC) (By similarity). Along with GIT1, positively regulates microtubule nucleation during interphase (By similarity). Phosphorylates FXR1, promoting its localization to stress granules and activity (By similarity).
PTM: Autophosphorylated in trans, meaning that in a dimer, one kinase molecule phosphorylates the other one. Activated by autophosphorylation at Thr-422 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation at Thr-422 by PDPK1. Phosphorylated by JAK2 in response to PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites (By similarity). Activated by phosphorylation at Thr-422 by BRSK2. Upon DNA damage, phosphorylated at Thr-211 and translocates to the nucleoplasm (By similarity). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 60578
Sequence Length: 544
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q6C462 | MEGWQEPPRIPLTQICRVSHTAPVATEIGQLTDTLPLTFDLAEDLVWAGDTNGIVSSYYGETLQPYSRFRAGRGRVTSLVSHDRGLVALTTDALHYSTRGGLTRKHVTDPSLGNNLCMTFTHGPTEFVVGGNPGKLVVVNSERGDVTRVVDSPGMATHMAGSSSCVVWGTENGKLVVGDNNLKELHTFQAHQGPFSDVSVQDNVVMTCGFSAASTGHRIDPLIKVWDLRMMRAMAPISYPLAAFVCQTPDSRTLITSPSGQLEFLDHATQQIKLYQAEVALVNGVKLSPRGHHFVVSDTSGQLQLWSDEPQSSFAEFSAPTAFPTPEQSYPPVSIRDTRYPLGAVGMPYYSDTLLSAMPSSIINVGMPPEEVDEDLEVRQIDFVGHAPNYKQQKRNLAQKYSNQRRTSIAAPKFLSEKEKERARRMEDIEDESFFGDEDTCTEASMSSKKVPRLYRKLEIKYSKFGISDFDFSYYNNHTGLSGLETNPFNPLLQLFRFCSPVFNFALRSVARGTPNRLLNEVGLLFDMMHKARGHVCRASNLMHCYDGIAQTRSLAPEDATNIVLFCRFLLEQIGFEQRQTPALFDSFRQLLGATVITVNTFSCGKMAQAESVWYTLELALGSTFYECLERTLDKELHTRAWCDKCRKYQSLHVSKHVESLPQVLTLSVADGNVDVAKSFLVLDGKVSPAAETDNDAYKLVGFICQIQGNGQVAFIRVGDEWYLFNDFLVTKVSEKEAFMKTPWKRTVMMVYAVGADERFDYDSWKNDMDVSALFEERLVNGNNVSRETTDYGYELIKEVPPPKTLCAIDAEFVVLKNEETEIRSDGTKVVLAPRNLCLARVTLLNEDGHPFINDYIAINEHIVDYLTAFSGIEPGDLDPSISRKPLVSLPTSYRRLWLLLNLGCVFVGHGLANDFRTINMQVPPEQVIDTVDLYYIPSERRKLSLRFLAWCVLGKKVQSGNHDSTEDSHTALLLYKKYQDCAPEEFQVLLLDVYRQGRMCNFKVPEA | Cofactor: Binds 2 metal cations per subunit in the catalytic exonuclease domain.
Function: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
Sequence Mass (Da): 112973
Sequence Length: 1008
Domain: Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.
Subcellular Location: Cytoplasm
EC: 3.1.13.4
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A1BH02 | MNTSNQHKAGHVTTRKLLDMKQQGEKISVLTAYDYTMARILDRAGIDVILVGDSASNVFSGHATTLPITIEEMIYHAKAVVRGVHDESGRAMVVVDMPFMSYQISGDEALRNAGKIMKEHGCDALKLEGGKIIADTVKRITDVGIPVMGHLGLMPQSIYKYGSYKVRAQEEQEAEQLLQDARLLEEAGAFAVVLEKIPSALAAEVTLMLTIPTIGIGAGSHCDGQVLVVNDILGLNREFHPRFVRQYANLNNVIDRAVQQYVDDVKQGGFPADDESY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 30328
Sequence Length: 277
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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Q8KCS2 | MNQPSGNKLPHVTTRRMLDMKERGEKIAMLTAYDYTMARILDRSGVDAILVGDSASNVFAGHSTTLPMTVDEMIYHAKAVVRGVQAETRRAMVIVDMPFMSYQLSPEDAVRNAGKIMKEHECDAVKMEGGKVIAEAVKRITDIGIPVMGHLGLMPQSIYKYGSYKVRAMEEEEARQLIEDAKIIEEAGAFAIVLEKIPSKLAGEVSRLLTIPTIGIGAGPECDGQVLVINDMLGLSTDFRPRFVRRYADLSSVIEQAVKSYVEDVRSNSFPSEDESY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 30608
Sequence Length: 277
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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A0M360 | MSVAKKEYKRITVKSLVDMKSNGEKISMLTAYDFTMAQIVDGAGIDVILVGDSASNVMAGHETTLPITLDQMIYHATSVVRAITRSLVVVDLPFGSYQSDPKEALRSAIRIMKESGGHAVKLEGGKEVKESIKRIIHAGIPVMGHLGLTPQSIYKFGTYTVRAKEEQEAEKLKSDAKLLEKMGCFAIVLEKVPAELAKEVAESITIPVIGIGAGNGVDGQVLVVHDMLGMTHEFNPRFLRRYADLHGEMTKAFQNYRDDVKSRKFPSDDEQY | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29961
Sequence Length: 272
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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B5E846 | MQKQRTILDFQRMKAEGEKIAVLTSYDFPMTGIMDACGIDMILVGDSVGVVVAGYDNTLPVTMEDMIYHTRAVMRARPKAFVVADLPFLSYQTDLKSARLNAGLLVKDGGAAAVKIEGGVNVEETITAITDMDIPVVGHIGLTPQSLHRMGGFKVQGKGEEQAEKLMADALAVERAGAFAVVLEGIPMSLAARITAELSIPTIGIGAGPHCDGQVLVIHDILGLCSKYSPKFVKRYAELAPLIGEACSNYIAEVKGGIFPEERHGFK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28592
Sequence Length: 267
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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Q97F39 | MKNTTETFKNSKFKKEKLVMLTAYDYSTAKIIDSCDINGILVGDSLGMVCLGYENTLSVTMEDMIHHTKAVVRGAKSTLIVADLPFMSYQTSVYDAVFNAGRLVKEAGATAIKLEGGALVCDRIKAIVDAQIPVMGHIGLTPQSVNAFGGFKIQGKNISKAKELIEDAKKIEAAGAFAITLEGIPEKLAKIITESITIPTIGIGAGKHCDGQILVYQDMLGMFSDLAPKFVKRYGNIGDDMKEAFNSYAKEVREGTFPDEAHSFKIDQSIIDEITK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 29959
Sequence Length: 276
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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A4WMD4 | MPDKKRRVTDFVKGGGPYVWVTAYDYPTAKLVDEAGVDGILVGDSLGMVVLGLPNTLGVTLADMVRHTQAVARAAPKALVVADMPFMTYETGPRDALRNAARLIRAGAEAVKLEGGSEYAHVVEKLVKAGIPVMGHIGLNPQRVLALGGFKMVGKTEEQKKKLVEDAKALRDVGVFAIVVEFVPASVAKEVTQSVDVPTICIGAGPHCDGQILVLHDVVGLSERTPSFAKRYANVAEQILSAVRQYVQEVRTKAFPAKEHYRDV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + 3-methyl-2-oxobutanoate + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-dehydropantoate
Sequence Mass (Da): 28399
Sequence Length: 264
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.1.2.11
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Q9AMR9 | MKVITKVAELRRALADVRNAEKRIGFVPTMGYLHDGHLALISASREHCDVTVVSIFVNPTQFGPNEDLSRYPRDFARDEALCGSAGVSIIFAPSAEEIYPAQFESFVEPGELAKPLCGAFRPGHFRGVATVVCKLFNMVQPDVAYFGQKDFQQCAVIRRMTVDLNLPIEIVTVPTVREPDGLAMSSRNRYLCPEERDRSLAISRGLFAAAHEFASGERDAATLIALARRHLERVDRLQYLELVDPGTLRIADSPLRYPAVLCVAAYVGSTRLIDNVVLSWSPS | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31322
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q0RK33 | MITTEKHAEVRELLDAERAAGRRVAMVGTSGGTHAGHISLVEQAKKECDVVAVFWNGALKLEWASGGVQAYNRDLAHDQALFEAAGVDIFYIPMRDDLYQRPSNTFMAMPGMLRHLTGMPEGEHMELLVTMVATLLNIAGPCLTFFGEKDWQQLVMFQRMAEDLHLPSRVIGCPTRREPDGVAISSRNTKLSPEQRAAAPALYAALTAAADAIAAGERDARAAAEVALARLRPVADPDYIVAVEAATLRPLDTLDPAAEGGPSDGEVRLLASVRFGTTPLVDNIGVTVPTA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31255
Sequence Length: 291
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q89JV7 | MSRSPLIARTVPALRRAADNLRKRKATIALVPTMGALHDGHVSLVRLAKRRASRVVVSIFVNPTQFAPTEDFGAYPRTWKADIAKLAAEDVDIVWHPGVEAMYPEGFATRIVPEGPALAGLEDRFRPHFFGGVATVVGKLFTQCRPDFAIFGEKDFQQLRVVTQMARDLDLGVKVIGSRTVRERDGLAMSSRNVYLSPQERQTATTLYRAMKDSAGRIRAGEAIASAMARGAATIKAAGFVLDYFEARHAETLAQVTSRKDGPLRILVAAKLGTTRLIDNIAV | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30969
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q0REL2 | MSGNGGGIGTGLGSLAGSGRTVTTIAEVRAAADAVRAAGGRVGFFGTSGALHEGHLTVIRRMAAECDLSIMPLFLAPVPGVTSDAVPAYDRDFDADAALAFDAGVNLVFRPAVAEMYPALPVRTAVVPADELAAPWEGAEDPSFLRMAATALAKYYNIVGPCRAYTGEKDWVPLTVLRRMVVDLSIRAEIVACPVVRLADGLCASSRNSRLSAADRAAAPTLYAALTAAVAAVEAGERDAEAIRSLLRRRISAVAPVDYAEVVDATTLARVDPLAGELRLLVSADFTGTHLFDNVGLTVRDADADADARVTVPAVGTTAAAPATDRRTSG | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 34091
Sequence Length: 330
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
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Q0RC35 | MLRVLHTIEDVREQTREWRAAGSSIGCVMTMGALHEGHLSLVDAARRECDKVVLTLFVNPIQFGPSEDFDRYPRTEEADFRALRDRECDAVFAPATETIFPLGERRIDQVRTKVVVRGLTDVLCGPRRPGHFDGVTTEVLKMLHIVDCDRTYWGEKDYQQYAVIRAMVEDQGLPVKVVPCPTMRDVDGLALSSRNTYLDSGQRAIAPRLYAALRRGARRIAEQGIDVIGETTKQIAETLLAHGFDLVEYVEVYTGSLGPAVAGTPVEELRVFGAVRLGGARLLDNAAVADEVGG | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 32511
Sequence Length: 294
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
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Q0RB94 | MLVRDRAELRAALVALDRAASSHPPAAAQDAGPARAASRHDRPVRAVVMTMGALHEGHASLLRAARARADQVVATIFVNPLQFGAGEDLDRYPRTLAADLAVCAREGVDVVFAPAVIHDPPPLVRFGAGPLGAVLEGASRPGHFDGMLTLVGTMLHLVQPDLAFFGRKDAQQLVCIRRMVADLAFDVTVIGVETAREPDGLARSSRNVYLTAEQRTEALALSRALAAGAAASADGAPAVLAAARAVLDAADGVDVDYLELAGPEDLGPVRGGPALLLVAARVGTTRLIDNVSLILPTDTQGA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31350
Sequence Length: 302
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
B0C6S1 | MDNVPIIRTVSGLRHFLRCFPGNLNTGASPSSTVIGQIGLVPTMGALHAGHLSLIQRARQENQCVIVSIFVNPLQFAAHEDLTEYPQTLNQDQALCQEQGVNTIFAPSTDTLLADAPLTQVIPPASLTEYLCGPHRPDHFTGVATIVLKLLNIVQPTRAYFGQKDAQQLAIIQRLVQDFNLDVTIVPCKLIRDATGLALSSRNQYLNAQEAQQATILHHSLQAARHTFQGGSCDRNSVLATVAQTLAKGPQVEVEYIDLVDPVTLQPLEQITTQGLVAIAARVGSARLIDNMLLDARLPILAIDGPAGAGKSTVTRRCAQAIGLQYLDTGAMYRAVAWLALDQQVEVSDPFAIADLVEDCQIELKPHADPQQQPQVWVNHQEVTQAIRTPDVTALVSAVAAQPPVREALVKQQQRLGRQGGLIAEGRDIGTNVFPDAGLKIFLTASIEERARRRQQDLKNQNLPPQTQSELEDLIASRDQQDSQREFAPLRKAYDAVEINTDGMTIEQVITRITTLYQERFPDRA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 57533
Sequence Length: 525
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
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A3PF80 | MKKVIIRKTEEIENWRRNINSEINFIPTMGNLHDGHIKLISTAKNDNSNVNLVSIFINPLQFDNKLDLENYPQTIDNDIKISFSNGADAIFIPSYEDIYPPNNKNIKFLKAPKELSSALCGLNRIGHFDGVCTVVYRLLNLIKPKNLYLGEKDWQQLLILKNLVLRKNLNVAIRSIPTQRDFDGIPLSSRNVHLSKNERKLISFFSSELLEAKKIFQQDKKINLNQIIKKLSAKKISVEYLEHLHPHTLQKARPEDNISLLAGAIRCGETRLIDHVFLMKRRPIIAIDGPAGSGKSTVTKLIAKKLNLLYLDTGAMYRALSWLIIKESVDYKIEKKLQNILKDISIFFKSNTNSHQDVYVNNYCVTKEIRSQKISSIVSKISSIKEVRKFLVAEQRKIGESGGLVAEGRDIGTTVFPHAELKIFLTASIDERAKRRKYDKNSKDSQEIDLYTLKELIKKRDFEDSNREISPLIKANDAIEIITDGYTIDEVVDKIIDLYNDRIPKETEIK | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 58445
Sequence Length: 510
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
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A9KEG8 | MTKVIEALSDWQSIRKTINDLSVGFVPTMGNLHAGHLSLLERSKCENTITVLSLFINPTQFNNKNDFKNYPRTLAQDIAMAEENGIDYVLAPTDDALYPDQYAYKITNSTINNQEAEFRPRHFDGVLTVVMKLLLLVKPTRAYFGEKDYQQLQLVKGLAEAFFLDTEIIGCKIVRNEFGLPLSSRNRRLTEDQYQLAQRFSEIFHSDLSCDEIKNALIQEGIIVDYIEDYNERRFAAVHVGDIRLIDNIPFAKDKKC | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 29478
Sequence Length: 257
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q11NE6 | MISITSIQQLRLHLAEEKRKNHSVGFVPTMGALHRGHISLIKQAKAENTVCVASIFVNPLQFNNPEDFNKYPIQRESDMKLMSEAGCDILFMPDVAEFYPTRPNMKIDIGLLDQILEGAHRPGHFSGVAIVVSKLFHIIEPGKAYFGQKDIQQVAVIRQLVSELNFPIEIIACPIIREESGLAMSSRNMRLSAQGKAVAANIYKALSVIEKQIKQDKVTVSDAQHAGKNYLNQFKEIEVEYLEIVAADTLEAITEYADQTKIAVCIAAYVEGVRLIDNLVIIL | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 31546
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q3Z8B3 | MQKLHREICGPVGLVPTMGYLHEGHLSLIRASKKQDLNTVASIFVNPTQFGPHEDFKKYPRDEKRDMAMLENAGVDYVFAPSVEEMYPPGFDSWVEPGVLQERLEGAVRPGHFRGVCTVVAKLFTIICPAKAYFGQKDYQQYLIIKKMASDLNLDVSVEMLPIVRESDGLALSSRNTYLSASERKAALVLYRSLLTAKSLFAAKEYNPEIIRRKMTEEIQRESLAEIDYVSLSDQDTLGEADKVSIKTIALVAARFGKTRLIDNMFLA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30142
Sequence Length: 268
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q1J0L2 | MNRTATRVLSSIEEVREALAGPGRVGLVPTMGYLHEGHAALIRRARAECDTVVLSVFVNPRQFGVNEDLSRYPRDLNRDLAVAEAAGADLLFHPDVATMYPAGYATTVAVGGVSEPLEGSSRPGHFDGVATVVLKLLNIVQPERAYFGEKDWQQLAVVRRMVRDLNVPVQIVGVPTVREPSGLALSSRNSYLTPEQQARAAILSRALQAVQAAAAAGERDTARLRQAGLAVLAEEPEIELDYLAVVDGDMREKAHVENDPLTRVLVAARLFGVRLIDNVPLSPAERRLSERESRNT | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 32200
Sequence Length: 296
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q9RV66 | MQTALASRGRVGLVPTMGFLHEGHATLIRRARAECDVVVVSIFVNPMQFGPTEDLATYPRDLDRDLALAGAAGADFVFHPEAAAMYPAGFSTRVEVSGVSEPLDGAARPGHFAGVATVVLKLLNIVQPERAYFGEKDWQQLAVVRRLVADLNLRSEIVGVPTVRADEEAAHAGLALSSRNSYLSPEQQRRATVLSRALRAVQAAYAGGERDTGRLRQAGLDVLASEPELALDYLVVVGPDLRDVPQLSDDPLNRVLIAGRLFGVRLIDNMPLSTAPVPAPA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30118
Sequence Length: 281
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q211R2 | MSRSPVIVRTLPALRRALDTLRARNASLALVPTMGALHDGHVSLVRLAKRRASKVAVSIFINPAQFAPNEDFAAYPRTWKADLARLTAEKVDLIWNPDAKTMYPAGFASKILTEGPALAGLEDRFRPQFFGGVTTVVGKLFAQVRPDLALFGEKDFQQLRVVARMARDLDLGVKVVGAQIVRERDGLAMSSRNRYLSPEHRESATALCRGLKEAAKRIRAGEAIEAALAGSAALITAAGFKIDYLEARHAETLAPVASRKDGPIRLLVAATIGTTRLIDNVAV | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30673
Sequence Length: 283
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q2RP31 | MRALPIARSVSELRAVVDGWKAEGLRVGLVPTMGALHAGHLSLVRLALSKVDRVVASVFVNPTQFGPNEDFAAYPRDEAADAAKLGGAGAHLLYAPDVAGMYPPGFSTTITVSGVSSGLCGDLRPGHFQGVATVVAKLFLRVRPDVAVFGEKDYQQLLVLKRLVNDLDLAIEVIGAPIVRETDGLALSSRNAYLSAEQRALAPGLYRTLRRVGADILGGGRVDDCLAWGIDELKALGFGPVDYLDLRDGATLERLDDAPEGPGRLLCAAYLGKTRLIDNIGV | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 29896
Sequence Length: 282
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
A7NG78 | MRVIATIGEFRAARAAMHGAVGLVPTMGYLHEGHLSLVRRARAENDHVIVTIFVNPTQFGPSEDLSRYPRDLPRDLALLEAEKIDVVFAPNVAEMYPPGFGTFVDVGPIAAPLEGAARPGHFRGVATVVCKLFNITTPHRAYFGQKDAQQTLVIRRMTLDLNLPVEIIVCPIVREPDGLAMSSRNVYLNPKERRAATVLFRALQAVQERFRAGERNGDALRAAMRAVIDAEPLAHPDYVSIADLDDLHELDRVTSRALASLAVRIGTTRLIDNCILEA | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30590
Sequence Length: 278
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q5LWR2 | MSAPILRKLADLRAATAGWKRAGESIGVVPTMGALHDGHLSLVAAAKAGCDRVVVTIFVNPKQFNNPEDLAKYPRTELADASKLAPYGVDAIYVPDPDQIYPEGFATTVSVSGLTDVMEGACRPGHFDGVATVVAKLFLQTGADQAYFGEKDYQQMMLVTRMAQDLDIPITVVGCPTVREASGLAMSSRNMRLSAEGLERAGRLHPVMRQVAERLAAGASFGDLAPGAREALGAAGFVDIEYFDLRAADSLRALDRPTEPARLLVAAWLDGVRLIDNIAVSQLND | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30411
Sequence Length: 285
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
A8M8F3 | MTELVHTRAELAAARDGLTGTVGVVMTMGALHSGHETLLRAARERADHVLVTIFVNPLQFGPDEDFNRYPRTLDVDLEICRRAGVAVVFAPVVTELYPEGKPRVWVAPGQLGEELEGQSRPGFFHGVLTVVLKLLHVTRPDLAFFGEKDYQQLTLVRRMVGDLDVPVEIVGVPTVREPDGLALSSRNRYLSPDERAAALSLSGALRAGAAAAAVGADAGAVLAAAHAAFESGPSGARLDYLVLTDSDLEPGPTAGPARMLVAAWVGTTRLIDNMSVQLAPYS | Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 30023
Sequence Length: 282
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.2.1
|
Q89ZR7 | MMIEVLKSKIHCARVTEANLNYMGSITIDEDLLDAANMIPGEKVYIADNNNGERFETYIIKGERGSGKICLNGAAARKVQPDDIVIIMSYALMDFEEAKSFKPTVIFPDPATNSVVK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 12930
Sequence Length: 117
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q6MHH9 | MNISLLRTKIHRATVTGADLNYEGSVSICPDLIKASGLLMNERVDIYNCNNGARFSTYVIKGKKGEICLNGAAARHVQKGDLVIICSYCGLSMDEAKKHEPTVVFVNAKNKVTEKRKEDRKNNK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13743
Sequence Length: 124
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q7VXF8 | MQRIMLRAKLHRVTVTEADLHYEGSCGIDEDLLDAAGMREFERIELYNVTNGERFDTYIIKAARGSGAISLNGAAARRAQVGDLLIICTYGPMSEEQSAAHKPQVVLVDDANRVKEIRKFPA | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13549
Sequence Length: 122
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q9AMS6 | MQITLMKGKIHRASVTEADLHYEGSISIDRTLLEAAGMVINERVEIYNVETGTRFATYVIEAPPMSGTMSLNGAAARLVMPGDKIIIVAYASFDEAEAKKFKPHVVRVDRDNRILAS | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 12895
Sequence Length: 117
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
Q7UQU4 | MVDTPYRKMLAAKIHRATVTGADVNYEGSLTVPPELLVAAKIHPYESLHVWNVTRGTRLETYAIEGLPNSNDVCANGAAAHLIRPGDHVILAAYAMVPEADAATHKPRLIFVDDNNQLSHVGPEIAGPNLRSDSDDTHLVRSTEMTPDGQPLAEGC | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 16828
Sequence Length: 156
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
B7JX32 | MKRTFLNSKIHRATVTGSELNYVGSMAIDAELMKAANILPFERIEIVNVNNGQRWATYVIEAEPGSGIMEVRGAAARLAEVGDIVIIFTYIEIEEPIPVPWHPRVVMVNEKNQISEIRHIAADKPSELLFSL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 14772
Sequence Length: 132
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
|
A1AXA6 | MKRTFLSAKLHKVITTAVELDYEGSCEIDGVLLDAADIGAFEQIQIYNINNGNRFTTYTIRGKDNSGVISVNGAAAHKVNVGDMLIIAAYGVYSEKELESYTPRLCYVNDQNILTKISS | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 13083
Sequence Length: 119
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
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A4F6T1 | MFRTMLKSKIHRATVTQADLHYVGSVTVDADLMDAADLLEGEQVAIVDVTNGARLETYVITGERGSGVIGINGAAAHLIEPGDLVILISYGVMDELEARSVRPKVIFVDADNRIVERGQDPGHAPAGSGLAGTAASVTSAITEAAAETDDAAKLDALLQQPEH | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
PTM: Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus.
Catalytic Activity: H(+) + L-aspartate = beta-alanine + CO2
Sequence Mass (Da): 17060
Sequence Length: 163
Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.1.1.11
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Q8TI88 | MRSHLVKPGSVYDGIEPGELGESTESVQDRVRQLESRNSFLEEQCSQIESEKRYLENQKIKYEREIRKLQSELDRMKTSPLIIGTVIDVIKNDRIIVRSSNGPQFLVNVSQYIDEKKLLPGAKVALNQHTLAIAEVIPSTEEPFVAAMEVIESIEVDYDQIGGLDEQIQELQEAVELPLIEPERFARIGIEPPKGVLLYGLPGTGKTLLAKAVAHRTNATFIRVVGSELVQKYIGDGSKLVREIFEMARKKAPSIIFIDELDSIAARRLNETTGADREVQRTLMQLLAEMDGFDKRKNIRIIAATNRPDVLDPAILRPGRFDRLVHVPMPGIEARGKILKIHCGKMTLAGDIDFKKLAKVTEGMSGADLKAIATEAGMFAVRKDKALVEMEDFLEAVEKVSMAADTQKMMPGNLPETTMFV | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates.
Sequence Mass (Da): 46965
Sequence Length: 421
Domain: Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type.
Subcellular Location: Cytoplasm
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Q58576 | MVFEEFISTELKKEKKAFTEEFKEEKEINDNSNLKNDLLKEELQEKARIAELESRILKLELEKKELERENLQLMKENEILRRELDRMRVPPLIVGTVVDKVGERKVVVKSSTGPSFLVNVSHFVNPDDLAPGKRVCLNQQTLTVVDVLPENKDYRAKAMEVDERPNVRYEDIGGLEKQMQEIREVVELPLKHPELFEKVGIEPPKGILLYGPPGTGKTLLAKAVATETNATFIRVVGSELVKKFIGEGASLVKDIFKLAKEKAPSIIFIDEIDAIAAKRTDALTGGDREVQRTLMQLLAEMDGFDARGDVKIIGATNRPDILDPAILRPGRFDRIIEVPAPDEKGRLEILKIHTRKMNLAEDVNLEEIAKMTEGCVGAELKAICTEAGMNAIRELRDYVTMDDFRKAVEKIMEKKKVKVKEPAHLDVLYR | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates. In addition to ATP, is able to cleave other nucleotide triphosphates such as CTP, GTP and UTP, but hydrolysis of these other nucleotides is less effective in promoting proteolysis than ATP. Moreover, PAN by itself can function as a chaperone in vitro.
Sequence Mass (Da): 48690
Sequence Length: 430
Domain: Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type.
Subcellular Location: Cytoplasm
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O26824 | MENNSQNVLKKIEDLKKEVRMLKEENSKTKRNLMWKIRKLEKDKLLIENERTRLDREVKSLRGEIERFRTPPLVIATVTEVLDDHRVAVKSTTGPHFVINYSRFIDRKQLEPGARVALNQQTFSIVDVLPSEKDPVVTGMEVEEKPDVSYEQIGGLEEQVREVKETVELPLKKPELFEKIGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIKIVASEFVRKYIGEGARLVRGVFELAKEKSPSIIFIDEIDAVAAKRLKSSTSGDREVQRTLMQLLAELDGFESRGNVGIVAATNRPDILDPALLRPGRFDRFIEVPLPNEDGRREILKIHTSGMALAEEVDIELLARITDGASGADLKAICTEAGMFAIRDERDEVTMADFMDAVDKIMGVEKEEEYKQETGVMFG | Function: ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates.
Sequence Mass (Da): 46111
Sequence Length: 410
Domain: Consists of three main regions, an N-terminal coiled-coil domain that may assist in substrate recognition, an interdomain involved in PAN hexamerization, and a C-terminal ATPase domain of the AAA type.
Subcellular Location: Cytoplasm
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Q9NRJ5 | MMPFPVTTQGPPQPAPPPNRYGVSSPISLAVPKETDCLLTQRLIETLRPFGVFEEEEELQRRILVLEKLNNLVKEWIREISESKSLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPSHVDRSDFFTSFYAKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDNFRLTLRAIKLWAKCHNIYSNILGFLGGVSWAMLVARTCQLYPNAVASTLVRKFFLVFSEWEWPNPVLLKEPEERNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSISTRMVMIEEFKQGLAITHEILLSKAEWSKLFEAPSFFQKYKHYIVLLASASTEKQHLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKENPDMEEFRTMWVIGLGLKKPDNSEILSIDLTYDIQSFTDTVYRQAVNSKMFEMGMKITAMHLRRKELHQLLPHHVLQDKKAHSTEGRRLTDLNDSSFDLSAGCENSMSVPSSTSTMKTGPLISSSQGRNSPALAVMTASVANIQATEFSLQQVNTNESSGVALNESIPHAVSQPAISPSPKAMVARVVSSTCLISHPDLQETQQQTYLIL | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 71813
Sequence Length: 637
Subcellular Location: Nucleus
EC: 2.7.7.19
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Q9WVP6 | MMPFAVTTQGAQQPAPAPKQFGISSPISLAAPKDTDRELTQKLIETLQPFGVFEEEEELQRRILILQKLNNLVKEWIREISESRNLPQAVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRNDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLVPNIDSFRLTLRAIKLWAKCHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVRKFFLVFSEWEWPNPVLLKEPEERNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMIEEFKQGLAITHEILLNKAEWSKLFEAPSFFQKYKHYIVLLASAPTEKQHLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKETADKEEFRTMWVIGLVLKKPENSEILSIDLTYDIQSFTDTVYRQAINSKMFEMDMKIAAMHLRRKELHQLLPNHVLQKKETHLTESVRLTAVTDSSLLLSIDSENSMTAPSPTGTMKTGPLTGNPQGRNSPALAVMAASVTNIQFPDVSLQHVNPIESSGIALSESIPQIPSQPTISPPPKPTMTRVVSSTHLVNHPSRPSGNTATNIPNPILGV | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 72329
Sequence Length: 642
Subcellular Location: Cytoplasm
EC: 2.7.7.19
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Q6PCL9 | MKEMSANTMLDSQRQQKHYGITSPISLACPKEIDHIYTQKLIDAMKPFGVFEDEEELNHRLVVLGKLNNLVKEWISDISESKNLPPSVVATVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVERSDFFQSFFEKLKHQDGIRNLRAVEDAFVPVIKFEFDGIEIDLVFARLAIQTISDNLDLRDDSRLRSLDIRCIRSLNGCRVTDEILHLVPNKETFRLTLRAVKLWAKRRGIYSNMLGFLGGVSWAMLVARTCQLYPNAAASTLVHKFFLVFSKWEWPNPVLLKQPEESNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSTSTRTVMVEEFKQGLAVTDEILQGKSDWSKLLEPPNFFQKYRHYIVLTASASTEENHLEWVGLVESKIRVLVGNLERNEFITLAHVNPQSFPGNKEHHKANNYVSMWFLGIIFRRVENAESVNIDLTYDIQSFTDTVYRQANNINMLKDGMKIEATHVKKKQLHHYLPAEILQKKKKSLSDVSRSSGGLQSKRSSLDSTCLDSSRDTDSGTPFNSPVSANKPSNPDSPTGEIERSSAEPVAVVVEKLPSVPPAQGLSIPVIGAKVDPTAKAVSSPAVCTIPTVVGRNVIPRITTPHNPVQGQPHLNGISNITKNVTPKRSHSPPTDGTSKRLKDIEKFIRLESAFKESRAAEDRKRKPMDSIGGESMPIPTIDTARKKRLPSKELPDSSSPVPANNIRVIKNSIRLTLNR | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Responsible for the post-transcriptional adenylation of the 3'-terminal of mRNA precursors and several small RNAs including signal recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA, and ribosomal 5S RNA.
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 82957
Sequence Length: 739
Subcellular Location: Nucleus
EC: 2.7.7.19
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Q9LMT2 | MASVQQNGQRFGVSEPISMGGPTEFDVIKTRELEKHLQDVGLYESKEEAVRREEVLGILDQIVKTWIKTISRAKGLNDQLLHEANAKIFTFGSYRLGVHGPGADIDTLCVGPRHATREGDFFGELQRMLSEMPEVTELHPVPDAHVPLMGFKLNGVSIDLLYAQLPLWVIPEDLDLSQDSILQNADEQTVRSLNGCRVTDQILRLVPNIQNFRTTLRCMRFWAKRRGVYSNVSGFLGGINWALLVARICQLYPNALPNILVSRFFRVFYQWNWPNAIFLCSPDEGSLGLQVWDPRINPKDRLHIMPIITPAYPCMNSSYNVSESTLRIMKGEFQRGNEICEAMESNKADWDTLFEPFAFFEAYKNYLQIDISAANVDDLRKWKGWVESRLRQLTLKIERHFKMLHCHPHPHDFQDTSRPLHCSYFMGLQRKQGVPAAEGEQFDIRRTVEEFKHTVNAYTLWIPGMEISVGHIKRRSLPNFVFPGGVRPSHTSKGTWDSNRRSEHRNSSTSSAPAATTTTTEMSSESKAGSNSPVDGKKRKWGDSETLTDQPRNSKHIAVSVPVENCEGGSPNPSVGSICSSPMKDYCTNGKSEPISKDPPENVVAFSKDPPESLPIEKIATPQAHETEELEESFDFGNQVIEQISHKVAVLSATATIPPFEATSNGSPFPYEAVEELEVLPTRQPDAAHRPSVQQRKPIIKLSFTSLGKTNGK | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Essential protein . Polymerase that creates the 3'-poly(A) tail of mRNA's . Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 80184
Sequence Length: 713
Subcellular Location: Nucleus
EC: 2.7.7.19
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O54820 | MELPGSLCKKAKLGHGAQSWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALGEHLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDACDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAESLPALQINKVDMQWVQVLAEGWATPLGGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATEEDKERLDGCTAFALIYEGRRVAILRNPEFFEHRKEERCARQWGTTCKSHPYIKMVMEQGDWLIGGDLQVLDRIYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHRQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGILNPESTVVAIFPSPMMYAGPTGVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYKPTHGAKVLTMAPGLITLEIVPFRVAAYNKRKKRMDYYDAEHHEDFEFISGTRMRRLAREGQKPPEGFMAPTAWAVLAEYYKALEKA | Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 70396
Sequence Length: 624
Pathway: Sulfur metabolism; sulfate assimilation.
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O43252 | MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEKA | Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway . Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells .
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 70833
Sequence Length: 624
Domain: The N-terminal first 50 residues are required for inhibition by the substrate adenylyl sulfate.
Pathway: Sulfur metabolism; sulfate assimilation.
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O95340 | MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLEKN | Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate/PAPS, the activated sulfate donor used by sulfotransferases . In mammals, PAPS is the sole source of sulfate while APS appears to only be an intermediate in the sulfate-activation pathway . Plays indirectly an important role in skeletogenesis during postnatal growth .
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 69501
Sequence Length: 614
Pathway: Sulfur metabolism; sulfate assimilation.
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Q56XM9 | MKKGGGRNKGFPQDDESSISLRQLMVNEGLIPSLEDEVKRRGVINQLRKIVVRWVKNVAWQHRLPQNQIDATNATILPYGSYGLGVYGSESDIDALCIGPFFASIAEDFFISLRDMLKSRREVSELHCVKDAKVPLIRFKFDGILVDLPYAQLRVLSIPNNVDVLNPFFLRDIDETSWKILSGVRANKCILQLVPSLELFQSLLRCVKLWAKRRGVYGNLNGFLGGVHMAILAAFVCGYQPNATLSSLLANFFYTFAHWQWPTPVVLLEDTYPSTGAPPGLMPIQLPCGSHQYCNSTITRSTFYKIVAEFLLGHNLTKDYLKLNFSWKDLFELYPYANTYTWFTKIHLSAANQEDLSDWVGWVKSRFRCLLIKIEEVYGICDPNPTEYVETYTKQPNIVFYWGLQLRTINVSDIESVKIDFLKNVNSGSFRGTVGRIQLTLVKASQLPKNGECGSNNRSKKVTKTCWRIREDKQCNNVPVYSKHLPGYVVGYQKMVNREADGMEVKC | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Essential protein . Polymerase that creates the 3'-poly(A) tail of mRNA's . Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 57704
Sequence Length: 507
Subcellular Location: Nucleus
EC: 2.7.7.19
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Q8VYW1 | MMVGTQNLGGSLPPLNSPKSYGITKPLSLAGPSSADIKRNVELEKYLVDEGLYESKDDTMRREEVLGRIDQIVKHWVKQLTQQRGYTDQMVEDANAVIFTFGSYRLGVHGPGADIDTLCVGPSYVNREEDFFIILHDILAEMEEVTELHPVPDAHVPVMKFKFQGIPIDLLYASISLLVVPQDLDISSSSVLCEVDEPTVRSLNGCRVADQILKLVPNFEHFRTTLRCLKYWAKKRGVYSNVTGFLGGVNWALLVARVCQLYPNAIPSMLVSRFFRVYTQWRWPNPVMLCAIEEDELGFPVWDRRKNHRDRYHLMPIITPAYPCMNSSYNVSQSTLRVMTEQFQFGNNILQEIELNKQHWSSLFEQYMFFEAYKNYLQVDIVAADAEDLLAWKGWVESRFRQLTLKIERDTNGMLMCHPQPNEYVDTARQFLHCAFFMGLQRAEGVGGQECQQFDIRGTVDEFRQEVNMYMFWKPGMDVFVSHVRRRQLPPFVFPNGYRRPRQSRHQNLPGGKSGEDGSVSHSGSVVERHAKRKNDSEMMDVRPEKPEKRASLSPQSLDIVSPENSAITTGWTPPVCNLRRPPSEEIEADNLNTECTELTDLARNECNSGSEQVLEVDSMAVVQECSDPAEPLGKCVTPDSVDVVACVSGQEENLDRNLRSVSISGTDSPLLPSRSCGQNRDYEGFGFPAANSDPMGKKNLYSQSGMSEDLQSNSLVSGMEKSEDRARSESFQKSQIRLLT | Cofactor: Binds 2 magnesium ions. Also active with manganese.
Function: Essential protein . Polymerase that creates the 3'-poly(A) tail of mRNA's . Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus (By similarity).
Catalytic Activity: ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Sequence Mass (Da): 83943
Sequence Length: 741
Subcellular Location: Nucleus
EC: 2.7.7.19
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A0A061AE05 | MLTPRDENNEGDAMPMLKKPRYSSLSGQSTNITYQEHTISREERAAAVGRHEGFRGCTIWFTGLSGAGKTTISFALERTLNKLGIPCYGLDGDNIRHGLCKNLGFSKEDRQENIRRVAEVAKLFADSGMICLAAFISPFQEDRLDARKIHESENVKFIEVHVSTTLEVCEQRDPKPSELYKKARAGQILGFTGIDSAYEPPENAEIILDAGKDGVQQCVQKVLDHLESKGLLPEQIPDVPAVRELFVSDDLTVAELLKESQNLPTVELTKVDLQWLQVLAEGWATPLSGFMRERQYLQSMHFGQLLDLKHKVAFVGEKSDDKEDSWPMMDDINQSIPIVLPISDDVKKGLEGVTRIALKYNGQVYAILSDPEIFEHRKDERVCRQFGTNDPRHPAVAQVLESGNWLLGGDVAVVQKIQFNDGLDKYRKTPNELRAIFAEKNADAVFAFQLRNPIHNGHALLMRDTREKLLAEHKNPILLLHPLGGWTKDDDVPLDIRIKQHEAVIAERVLDPEWTVLSIFPSPMMYAGPTEVQWHARSRIAAGIQHYIVGRDPAGIQKPGSPDALYETTHGAKVLSMAPGLSALHILPFRVAAYDKTAKKMSFFDTSRKEDFENISGTKMRGLARNGDTPPEGFMAPTAWEVLAGYYKSLQNSN | Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway . The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase) . Required for normal growth and development . Involved in several aspects of both embryonic and postembryonic development, including molting, changes in cell shape, and patterning of epithelial and muscle cells .
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 73172
Sequence Length: 654
Pathway: Sulfur metabolism; sulfate assimilation.
Subcellular Location: Nucleus
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P9WEV6 | MEYRYSYVIDPSSYDNQGLCNGIPLRVHRNADIEEYATISLRNDWRKHVGPLPLTSYGGNLGPKYNFTAVTLPECRPDRLEIVSYIMEFAFLHDDLVDTAQVDEALALNDTWRDGITEGLDTTSAKGKKSGEGLILRNILKEVTAIDPVRAAELMKFWKRDLDVSRDRKHFRDFDDYMEYRIVDCASYFLIALSTFAMALTIPAEDKDEVFTLLTRPVWAAAALTNDVQSWEKEDKLFQKDNATDMTNGVWMLMKQYSIGVEEAKRRILGKAREHVAEFVKTLSQIHNRLDLSLDSRLFVEAMQYMISGNLMWGISTPRYHSDQSLDEMMVARMKYGWPNHREVTKLTSDLENRGTKRTHQDDTEGVQSVKRFNGASTKNGINGTNGINGLNGINGSNGVKIKRHKNKEYSGALTKDSDLVLNMDLNGLSSAIICAPADYIGSLPSKGIRDNVADALSIWLDVPAKELNQIKRAINLLHNASLMLDDVQDGSVLRRAQPTTHTVFGPAQTINSAGHQIIQAMNEIRKLGSDDCLDIFSEELEKLYVGQSHDLYWVYNDSCSPTIEDYFKMVDYKTGGLFNMLARLMTAKSSSSSSPDLTALVGLLGRYFQIRDDYMNLTSADYTVEKGFCEDLDEGKFSITLLHALSAAPEPEALLLRNLMSGRRNDGKLSVVQKNLALSIIEGARSLEYTAAVLQKLYKAIVRELESTERQFGENKPFRFLLSLLKV | Function: Bifunctional terpene synthase; part of the gene cluster that mediates the biosynthesis of the diterpene methyl phomopsenonate . At first, the universal precursor of diterpene, geranylgeranyl diphosphate (GGPP) is provided and is cyclized by the unusual bifunctional terpene synthase PaPS to give phomopsene . The C-terminal prenyltransferase domain of PaPS catalyzes formation of GGPP, whereas the N-terminal terpene cyclase domain catalyzes the cyclization of GGPP to phomopsene . Since the oxidation of a methylgroup to a carboxyl group is frequently catalyzed by a cytochrome P450 monooxygenase, the C-16 methyl group would be oxidized by the cluster-specific cytochrome P450 monooxygenase ORF3 (Probable). Subsequently, oxidation of the allylic position and methylation of the carboxyl group may give methyl phomopsenonate (Probable). Although further study is necessary to identify genes such as a monooxygenase and a methyltransferase, the predicted functions of genes on the cluster are correlated with the structure of methyl phomopsenonate (Probable).
Catalytic Activity: (2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate
Sequence Mass (Da): 81975
Sequence Length: 728
Domain: The conserved DDXXD motifs as well as the NSE/DTE motif are important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
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P0DO57 | MASSQLEFNVERKQPELLGPAEPTPYELKELSDIDDQDGVRLFLTAIFIYPPPTKTSMPTRKTDPASDIRRGLSKAMVYYYPFAGRIREGPNRKLSVDCTGEGIVFCEADADIRLDGLGDVEVLRPPYPFIDKMTLGEGSAILGAPLVYVQVTRFACGGFIITGRFNHVMADAPGFTMFMKAAADLARGATVPMPLPVWERERYRSRVPPRVTFAHHEYMHVDDPPPRPTSEPWSLHSAFFTKADVATLRAQLPADLRKAATSFDIITACMWRCRVSALQYGPDEVVRLIVAVNSRTKFDPPLTGYYGNGLMLPAAVTEAGKLVGSDLGYAVELVREAKGKVTEEYVRSAADFLVLNGRVHFVVSNTFLVSDLRRLIDLANMDWGWGKAVSGGPVDVGENVISFLATSKNSAGEEGAVVPFCLPDSALGRFTSEVKKLVCFRPLENAAASNPDHGYMSRM | Function: Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects . Can use piperidine and benzylamine as acceptors and various CoA-esters with aliphatic and aromatic amines as CoA-donors, including piperoyl-CoA, hexanoyl-CoA and octanoyl-CoA, and, to a lower extent, benzoyl-CoA . Mediates the conversion of piperidine to three piperine isomers in the presence of piperoyl-CoA . Its ability to convert in vitro piperidine to hexanoylpiperidine in the presence of hexanoyl-CoA, and to octanoylpiperidine in the presence of octanoyl-CoA is not confirmed in vivo according to fruits metabolome analysis .
Catalytic Activity: (E,E)-piperoyl-CoA + piperidine = CoA + H(+) + piperine
Sequence Mass (Da): 50566
Sequence Length: 460
Pathway: Aromatic compound metabolism.
Subcellular Location: Cytoplasm
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Q95QA6 | MTSHIATETSVNRWSTEPVVREEGRPPGPEDFPSTKQGREQDGNVIGITPNYKIGEQKPNSELNLGKTGSLPRGSGDYKMTYRQEDYKQTIIDPKVITNANMPYISTRIPDPRRNLAGDFPSEHSKSKIKLDPLEQRRFRSSESRPITTSNYLAESVDRHREMEASRLREYLKAKENEANQPWNKPGWPGPKKNDESLRELETMKQRIETLKRDANKGPVNAELDELSKRAEELRKRDGWSKYKLVESDIYKTDPDPMPANIKDQVRDLLESRNSVETTTTQRDHDKSGYVTDVSTATWNFSTVDYSPRSVVSMNGASHDILKDDKPRSIMKRNDLVRREQMLYPTVDTQVVKSVVKKPTVTETVQRFEETRRTEEVERRVQRREKKERRSRHHSSSRHHSGWEGHTGGYQGHRSSSLSRGGHGGGGQETYYRQETTRRQQHNNYDDNFNRGIAHARYGSLSDSLRRGELQYVPNGEVRQSFYRDGSNGGQRMHKSYSTRDVFTGDGYDDRRSVSSFRRGSQQQVSPFVEFPPTLPRRGGGGDYRREEDAYFRPVSKSRSYADWDDAGRAGMGREVRRYDDDMSRLEAEFRDSLLMPMPAGNMNERDHRTEQLPGGYETFNKERHANSGRRSGRDGKPVDFNEATQEYNYKREQTLNDDRRRR | Function: Required for embryonic morphology and development. Plays both a functional and a structural role in the maintenance and probably biogenesis of fibrous organelles, a hemidesomosome-like junction structure, which ensures muscle stability and muscle connection to the external cuticle.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 76709
Sequence Length: 663
Subcellular Location: Apical cell membrane
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A0A075TRB3 | MVLTTGLKGAHVLITGGTRGMGEAMVHKFLQEEANVSYCARTVTNTEYDDFYSTLAEGNTARAVGTAFDVASKDSLVKWVESSAERLGRIDVIIANASPMHMEGETEHWESSFAIDVMGFVELVKAATPYLEKSPQASIIVQSSFMGREFYRSPPAAYGPCKAAQLQHVQELSHFLGPKGIRVNAISPGPVLCKGGPWELYSKINPEWVEEQRLKIPLKRLGGPTEVANVAVFLASPLASFVSGTNMLVDGGIHVGTQF | Function: Isoepoxydon dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria . PatN catalyzes the conversion of isoepoxydon into phyllostine . The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Catalytic Activity: isoepoxydon + NADP(+) = H(+) + NADPH + phyllostine
Sequence Mass (Da): 28033
Sequence Length: 259
Pathway: Mycotoxin biosynthesis; patulin biosynthesis.
Subcellular Location: Cytoplasm
EC: 1.1.1.-
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A0A075TR33 | MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGHYHRHLPTYTSAGGMAIAQITNSSFLLTPLTLPAYTAAATKKLLGPFLQDLHQLNISYTLNVTESASYFQHYMKLIEPNPTQLVQNAQYGGRLLPLDLIERNNSQLTDAVQKLTADGVTFVGIGLNVSSSVTGDIWNSVLPGWRTAAMTVILTTSWPLGANLTKMKILADKMTTKWVPILTALSPESGCYMSEADPQQPDWKQTFYGRNYDSLYAIKTKYDPLQTFYATTAVGSEDWQVEAGGRLCQATRKN | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria . PatO acts with patJ in the vacuole to convert gentisyl alcohol to isoepoxydon . The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Sequence Mass (Da): 61945
Sequence Length: 571
Pathway: Mycotoxin biosynthesis; patulin biosynthesis.
Subcellular Location: Vacuole lumen
EC: 1.-.-.-
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Q62627 | MATGGYRSSGSTTDFLEEWKAKREKMRAKQNPVGPGSSGGDPAAKSPAGPLAQTTAAGTSELNHGPAGAAAPAAPGPGALNCAHGSSALPRGAPGSRRPEDECPIAAGAAGAPASRGDEEEPDSAPEKGRSSGPSARKGKGQIEKRKLREKRRSTGVVNIPAAECLDEYEDDEAGQKERKREDAITQQNTIQNEAASLPDPGTSYLPQDPSRTVPGRYKSTISAPEEEILNRYPRTDRSGFSRHNRDTSAPANFASSSTLEKRIEDLEKEVLRERQENLRLTRLMQDKEEMIGKLKEEIDLLNRDLDDMEDENEQLKQENKTLLKVVGQLTR | Function: Pro-apoptotic protein capable of selectively inducing apoptosis in cancer cells, sensitizing the cells to diverse apoptotic stimuli and causing regression of tumors in animal models. Induces apoptosis in certain cancer cells by activation of the Fas prodeath pathway and coparallel inhibition of NF-kappa-B transcriptional activity. Inhibits the transcriptional activation and augments the transcriptional repression mediated by WT1. Down-regulates the anti-apoptotic protein BCL2 via its interaction with WT1. Seems also to be a transcriptional repressor by itself. May be directly involved in regulating the amyloid precursor protein (APP) cleavage activity of BACE1 (By similarity).
PTM: Preferentially phosphorylated at the Thr-155 by PKC in cancer cells.
Sequence Mass (Da): 35866
Sequence Length: 332
Domain: The leucine-zipper domain is not essential for apoptosis, but is required for sensitization of cells to exogenous apoptotic insults and for interaction with its partners.
Subcellular Location: Cytoplasm
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Q9ZB73 | MDKLVSILVPCYKSKPFLKRFFNSLLKQDLNQAKIIFFNDNVADETYEVLQKFKKEHNNLAIEVYCDKQNEGIGKVRDKLVNLVTTPYFYFIDPDDCFNNKNVIKEIVESIKKEDFDLGVLKSMVYLCFLKHDFIIKFLPLKGIFQGRVKLINNNNVNKLNYIKNNDQYIWNIVINTDFFRKLNLTFESRLFEDIPIWYPMFFSSQKIVFIDVIGTNYFIRNDSLSTTISAPRYLNLIQCYEKLYVNLSQNGSLASFIDPNHKIEARFWRRQMFVWFALFSFEYFKKNFSESKKILEKLFVFLEKNGVYERVFQTKNQGIYYIWVQRLKYFKHVLESKSDN | Function: Processive glycosyltransferase involved in the biosynthesis of both the non-bilayer-prone beta-monoglycosyldiacylglycerol and the bilayer-forming membrane lipid beta-diglycosyldiacylglycerol. These components contribute to regulate the properties and stability of the membrane. Catalyzes sequentially the transfers of glucosyl or galactosyl residues from UDP-Glc or UDP-Gal to diacylglycerol (DAG) acceptor to form the corresponding beta-glycosyl-DAG (3-O-(beta-D-glycopyranosyl)-1,2-diacyl-sn-glycerol), which then acts as acceptor to give beta-diglycosyl-DAG product (3-O-(beta-D-glycopyranosyl-beta-(1->6)-D-glycopyranosyl)-1,2-diacyl-sn-glycerol). Dioleoylglycerol (DOG) is a preferred sugar acceptor than 3-O-(beta-D-glucopyranosyl)-1,2-dioleoyl-sn-glycerol.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol + H(+) + UDP
Sequence Mass (Da): 40881
Sequence Length: 341
Pathway: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
Subcellular Location: Cell membrane
EC: 2.4.1.-
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A3UZK3 | MTTTNQEPILKATHFRSEGDVNTTPAREKWNESLNDDATQAMLKRDSDVFLHQAMSTPCLDTLTAAEGIYIQDATGKKYMDFHGNNVHQLGYGHPHIINKVTQQMASLPFSPRRFTNETAVQCAEKLTQICGGDLNRVLFAPGGTSVIGMALKLARHVTNNFKVVSLWDSFHGASLDAISVGGEACFREGMGPLMAGVERIPPAVSYRGAFPLRDSLSLRGQNSGDANETACDVHYADYLEYVIEKEGGIGAFIAEAVRNTDVQVPSKAYWKRIREICDKHNVMLIIDDIPNGMGRSGEWFTHQAFDIEPDILCIGKGFGGGLVPIAAMITKDKYNTAAQVSLGHYTHEKSPIGCAAALATMEVIEQENLLEKVQADSAFVREQLLQMKEEYPVIGDIRGIGLLWGVELVTDHITKTRAFDEAEAVLYQCLNEGLSFKVSQGNVIQLSPPLIISRNELEVALSVFEKAIAKVCKDFEYL | Function: Involved in phosphonate degradation. Functions as a lyase that catalyzes an elimination reaction on the naturally occurring compound (R)-1-hydroxy-2-aminoethylphosphonate ((R)-HAEP), releasing ammonia and generating phosphonoacetaldehyde (PAA), which can be then hydrolyzed by PhnX, encoded by an adjacent gene. Thus, catalyzes a reaction that serves to funnel (R)-HAEP into the hydrolytic pathway for aminoethylphosphonate (AEP, the most common biogenic phosphonate) degradation, expanding the scope and the usefulness of the pathway itself. Is not active toward the (S) enantiomer of HAEP or other HAEP-related compounds such as ethanolamine and D,L-isoserine, indicating a very high substrate specificity.
Catalytic Activity: (1R)-(2-amino-1-hydroxyethyl)phosphonate = NH4(+) + phosphonoacetaldehyde
Sequence Mass (Da): 52703
Sequence Length: 479
EC: 4.3.1.-
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A0A509AET3 | MKLYLVTFLFFVIYKNKTFVDCVTKKQDVYLDDEFKSFTFFFASSPSANFLSRIVHSNEAKFTQIKNKTDIWNKTIDKAYSINQVSNNIMRVYISLLSLFLFPYFSYIGIFGHSRNKANLTLSSLLAYFALLVSFFLFNGILNIGFVTSLPLVVAVLIFILGVSDCEINFLYKYTRYIFCFIISKLIYDVVTYISKDGANIFDYGFSGHIYMNLLRGKYYIVLKLIHLIILSLISLIIIKICPKIFSNNHLKSPISITFDKYIISFLCSLPIATAISQVFYLLSKTINPIDPSIFFMIPSSINFSSTGTIFSLSIWILMSYLMTFLRNKVEADFNNILNKIPNNLPDFI | Function: Involved in the development of male gametocytes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40208
Sequence Length: 349
Subcellular Location: Cell membrane
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P40750 | MTMLRKIIGWILLLCIIPLFAFTVIASGKEVKQMKSLDQVLDKNIDLKDISLVQNSYMYDRDGSLVSEIVSDHENRVLVPFNKIPEEVKQIFLTSEDRHFYEHKGFDFMGMVRATASNVKDKKIDQGASTITQQLSRNLYLSHERSFSRKLTELAYSYQLEKKYTKNEILEAYLNTIYFNNGVYGVGSAAQFYFSKPLKSLTVGEMAFICAIPNNPTLYDPLKHFDYTKSRQERLLKGLKDAGVITDKELKKAVKQKIKLDVEKREDKYPDYVSYVNDEFTQLVSESEGFDKRLQKASGKQKEKIENELSARVSTLMKDGVKIYTALDPYMQNQVVAQMNSKLPYADVQGGAAVINHQTHQIIALSGGKNYQKYDFNRAYQAYRQPGSSIKPLLDYGPYIEQTGATTSSTIDASKFCSKDYCPQNYNNRTYGTVTLDTAFKNSYNTPAIRMLDRVGIQKAFSYIEPYHFAKLVDSDYLLPAALGGFTNGMTPLEMTKAYTTFGNSGSYTPSHAITKVTDLKGKTLYKWNDKATQIFSVRTNMQLKKLMSSVVKSGTGKKAYFNAPYIGGKTGTSNDYHDMWFVGLTDTYTMGVWVGKDTPTSVEYLHSISPQLSIWKGTLQAAY | Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (Probable). Has a partially redundant function with PBP-2A (pbpA) during spore outgrowth .
PTM: The N-terminus is blocked.
Location Topology: Peripheral membrane protein
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Sequence Mass (Da): 70659
Sequence Length: 624
Subcellular Location: Cell membrane
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P32959 | MKQNKRKHLQTLFETLGEKHQFNGTVLAAEGGDILYHHSFGYAEMTEKRPLKTNSLFELASLSKPFTALGIILLEEKGILGYEDKVDRWLPGFPYQGVTIRHLLNHTSGLPDYMGWFFANWDSHKIAVNQDIVDMLMNEGLSGYFEPNEGWMYSNTGYVLLAVIIEKASGMSYADFIKTSIFLPAGMNETRVYNRRLSPERIDHYAYGYVYDVHSETYVLPDELEETNYVVYLDGIQGDGTVNSVTSDLFRFDQALYQDDFISKASKESAFSPVRLNNGETIDYGFGWVLQNSPEKGRIVSHSGGWPGYSTMMIRYIDHRKTLIYLSNKEEDTEYEQAILKAAEHILFGQPYDVPERPADKKKKAIDTAIYSRYVGSYLLQDGTAAQVTTENERLYLEIAGQLRLELFPSSETRFFLRALSVEVEFTLGEDAAKSFILYEDGSEEEAVRTK | Function: Probably involved in peptidoglycan modification during cortex synthesis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51437
Sequence Length: 451
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Forespore outer membrane
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P38050 | MFKIKKKKLFIPIIILVLTAFLALIGYISIIFLGHYVIDEKKLILHASSKIVDQNGDEVASLYTENREPVSINEIPKQVREAFIAVEDKRFYEHHGIDAKSVGRAVYRDILAGGKVEGGSTITQQLAKNIFLTHDKTFLRKTKEVIIAINLERDYSKDKLLEMYLNQLYFGHGVYGIQAASHYYFNKEVKDLTVSEGAVLAAIPKAPSTYSPILHPDKNKERRDTILGMMNDQGYISAKEAVTAQGRTLGLHVKKQSETPWFDSYIDLVIKEAEDKYSISGEQLLQGGYTIKVPLDSKLQKTAYQVMKEGSYYPGTDQNAEGSAVFINNKTGGVEAAIGGRDYTSKGYNRVTAVRQPGSTFKPLAVYGPAMQEKKFKPYSLLKDELQSYGDYTPKNYDSRYEGEVTMSDAITYSKNAPAVWTLNEIGVETGKSYLKANGIDIPDEGLALALGGLEKGVSPLQLAGAFHTFAANGTYTEPFFISSIIDEDGETIADHKEEGKRVFSKQTSWNMTRMLQQVVKKGTATSGTYHGDLAGKTGSTSYTGVSGATKDAWFAGYTPKITGAVWMGYDKTDQNHYLKAGSSYPTRLFKDILTQAGETGHVFTKPKNVKELESPIELKPVKTLTADYTFKAAGLFTIELKWDAQEDDRAVYRIYVNKDGEETLLDSVEGKGSYEIPYANLFSGASYKIVPYNTQTKREGEGTDYVQPKLFSS | Function: Cell wall formation. May be involved in outgrowth of the germinated spore or it could function in the synthesis of the germ cell wall.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 79265
Sequence Length: 714
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
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P70997 | MDAMTNKRLRLTLKTVRAFIFLGAFAALAAAAVFMTVILIAKYQGAPSVQVPQSTILYASDGSKLGETNYGEKRYWVPLKDMNPTIVKATVAIEDQNFYDHHGFDYKRMAGAALADLKAFAKVQGASTITQQYARNLYLEHDKTWKRKWNEAFYTIRLEQNYSKDEILEGYLNTIYYGHGAYGIEAASRLYFGKHAKNLTDAEAALLAGIPKGPSGYSPYVNETKAKERQKTIVRMMEKQQMISQKKADELIKEPLSYQPLNKQVSKRKAPYFYDNAMRELEKKLGMTREQIETSGLNVYTTVDKRMQRIAEETITETVNAGSDIQVGFSAIDPRTGNVLALVGGRDYQKSPFDRTTQAKRQPASTIKPLLYYKAIQSGFTPVTLMKSEETEFQIDAKGETYSPSNYNGYYANKPITLLQALALSDNIYAVKTHLFLGTNKLVKTAKEFGITAHLQALPSLALGTEPVRPIEMVNAYAMLANGGKKIEPTFISRVTDAAGHVLYENPNQHKQVLDEKAAFVTASMMTGMFDIDLNGYTSVTGRTIANRLTRTYAGKSGTTSADSWMIGFNPKLAAGVWTGYDKNSTIDSVEEKSYAKTIWADFMEDALKGEPETAFKPPKGVTGVYIDPETGYSSGPGCAAKHYTYFVKGTEPANVCYGAEPAKQTKDRLPSKEKPASEKKWWDKWLGRHH | Function: Involved in the polymerization and cross-linking of spore peptidoglycan. May be required for synthesis of the spore germ cell wall, the first layer of peptidoglycan synthesized on the surface of the inner forespore membrane.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77037
Sequence Length: 691
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
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Q796K8 | MTEIGREPKKKSKGNRAIRMNLFFLAVFVLFTALIFKLGVVQIVEGEQHEEDAEKSNAKTAYYPAPRGKMYDRNQKVAVDNQSVPEIVYVSTSSTKTEDKIKTAKRLASFIHIDTEFLKERDLRDYWIAAHPKKAAALLKESESNLKGDQAYKLQIERVPDQELKAIQQDDEEMETAAIYTRFSSGNAYEPQIVKAMNPNKSNSNGKNGALLDEKKNSSQRPKNDLTYDEISIVSEHLEELPGIDIVNDWTRKYPYDKTLYSVFGGVTTPDQGLLSDRKDFYLTRGYANNDRVGKSYLEYQYEEYLNSHKEKVEYVEDNKGNVVSQKTIDKGSRGYDLQLSFDMELQAKVEKIIEEEVRNSRARGNYMLDRAFAVMMDPNNGDILSMAGKKIDLKTNKIEDYAIGAFTTQYEMGSAVKGATVLAGYQDGIPHYKYYIDAPMLLGTNLIKKSYTNMGTINELTALQKSSNVYMFNVAMHIAGVTYKPHGSLPADQNDLLKMRNYYSQFGLGVKTGIDLPQESAGMQTTPKTVGGLILDLAIGQYDTYTPLQMAQYISVIANGGYRVQPRIVTSIHKPGKKDQLGKAIEHRKPKVLNKINNSESDLKQVQTGMKLVTSSGTAKNTFTEDVSGKTGTAETFYYGTNRNWWGKKTYNLTFVGYYPSKKPKVAFSVVVPSVDDDDKINKIIAKRAIHAYAELEKKHSKK | Function: Involved in the polymerization of peptidoglycan. Plays a redundant role with PBP-2A (pbpA) in determining the rod shape of the cell during vegetative growth and spore outgrowth.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 79348
Sequence Length: 704
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 3.4.16.4
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O32032 | MKISKRMKLAVIAFLIVFFLLLLRLAEIQLFFTESFSKKKINLIQESVKQRTEEVLISDGRGSFLDRNGRALTGQSEPAVVLFPFLLTQDWPIKKVADILGMSEDDLRQTLGQAKKPVILQQKKIKTLSKQSITKINSLKYPGIYGVYMENEDKPSLASHTIGSTNQDPALLRKKYPDKESLPITTEIGTTGLERTFDEFLLPEQDTKLLYHVDGKGNPLFGMDVKYTAEANTFYPLQIKTTIDQSIQKAMEEVLDEQGLKKGGAVLLDIENSSVLGIVSKPDADVSRQNTLQNYMLTPIYPGSVFKTVIAAAAIENNMVKPSQTFNCNLNLYGEPGDDKGTLSFDESFAQSCNYTFTSLAEQLMKKDSSVIEDMSEKLALTDRAGWEGKLYHETDFRQLYNEKSGVIWGDEKDKSVKKAIAQTAIGQKNVKVTPLEVANMMATIARGGEKRQVKIAEQIEYKNGTTLVTFKDQKLKGETIDKYTSQQLQKILRRVVESPSGTGRRFQDLPYTVAGKSGTAQTGKLSKEKETLYEKWFAGYFPADKPKYALVVLHMDTPGDKALTNSVFYDIVKKVHEIEINQK | Function: Penicillin-binding protein with an unknown catalytic activity. Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis.
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 65522
Sequence Length: 584
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 3.4.16.4
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P59676 | MKWTKRVIRYATKNRKSPAENRRRVGKSLSLLSVFVFAIFLVNFAVIIGTGTRFGTDLAKEAKKVHQTTRTVPAKRGTIYDRNGVPIAEDATSYNVYAVIDENYKSATGKILYVEKTQFNKVAEVFHKYLDMEESYVREQLSQPNLKQVSFGAKGNGITYANMMSIKKELEAAEVKGIDFTTSPNRSYPNGQFASSFIGLAQLHENEDGSKSLLGTSGMESSLNSILAGTDGIITYEKDRLGNIVPGTEQVSQRTMDGKDVYTTISSPLQSFMETQMDAFQEKVKGKYMTATLVSAKTGEILATTQRPTFDADTKEGITEDFVWRDILYQSNYEPGSTMKVMMLAAAIDNNTFPGGEVFNSSELKIADATIRDWDVNEGLTGGRMMTFSQGFAHSSNVGMTLLEQKMGDATWLDYLNRFKFGVPTRFGLTDEYAGQLPADNIVNIAQSSFGQGISVTQTQMIRAFTAIANDGVMLEPKFISAIYDPNDQTARKSQKEIVGNPVSKDAASLTRTNMVLVGTDPVYGTMYNHSTGKPTVTVPGQNVALKSGTAQIADEKNGGYLVGLTDYIFSAVSMSPAENPDFILYVTVQQPEHYSGIQLGEFANPILERASAMKDSLNLQTTAKALEQVSQQSPYPMPSVKDISPGDLAEELRRNLVQPIVVGTGTKIKNSSAEEGKNLAPNQQVLILSDKAEEVPDMYGWTKETAETLAKWLNIELEFQGSGSTVQKQDVRANTAIKDIKKITLTLGD | Function: A transpeptidase that forms peptide cross-links between adjacent glycan strands in cell wall peptidoglycan (PG). Part of the divisome machinery that synthesizes the septal cross wall. Beta-lactams inactivate the PBPs by acylating an essential serine residue in the active site of these proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 82343
Sequence Length: 750
Subcellular Location: Cell membrane
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O23215 | MKCPYCSSAQGRCTTTSSGRSITECSSCGRVMEERQTQNHHLFHLRAQDTPLCLVTSDLQTAAQPSPEDEEDPFEPTGFITAFSTWSLEPSPIFARSSLSFSGHLAELERTLELASSTSNSNSSTVVVDNLRAYMQIIDVASILGLDCDISEHAFQLFRDCCSATCLRNRSVEALATACLVQAIREAQEPRTLQEISIAANVQQKEIGKYIKILGEALQLSQPINSNSISVHMPRFCTLLQLNKSAQELATHIGEVVINKCFCTRRNPISISAAAIYLACQLEDKRKTQAEICKITGLTEVTLRKVYKELLENWDDLLPSNYTPAVPPEKAFPTTTISTTRSTTPRAVDPPEPSFVEKDKPSAKPIETFDHTYQQPKGKEDKQPKFRQPWLFGTASVMNPAEMISEPAKPNAMDYEKQQLDKQQQQQLGDKETLPIYLRDHNPFPSNPSPSTGISTINWSFRPSVVPGSSSNLPVIHPPKLPPGYAEIRGSGSRNADNPHGDF | Function: Plant-specific TFIIB-related protein that may be involved in an intracellular signaling pathway between plastids and the nucleus . May act as general transcription factor (GTF) of RNA polymerase I-dependent transcription and rRNA synthesis. Forms a ternary complex with TBP2 and the rDNA promoter region .
PTM: Ubiquinated. Subsequent degradation by the proteasome pathway.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55672
Sequence Length: 503
Subcellular Location: Plastid
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I3R7F1 | MTMEDRIDELREKREEALKGGGEDRIASQHDKGKMTARERIDYFLDDGTFREFDQFRTHRNHKFGMEETKLPGDGVITGHGEVDGRTVFVFAHDFTVFGGSLGEVFAEKICKVMDKAMEVGAPVIGLNDSAGARIQEGVQSLGGFGEIFRRNTEASGVVPQISAIMGPCAGGAVYSPALTDFTFMVRDTSHMFITGPDVIKTVTGEEVTFDELGGATTHTSTSGVAHFATDTEEQALDDIRHLLSYLPQNNVEDPPRVEPWDDPERVADELEEIVPDQPRKPYDIHDVLNGVLDEGSFFGVQEDFAKNIVVGFGRLDGHSVGIVANQPRVNAGTLDIEASEKGARFIRFCDSFNIPILSFVDVPGFLPGTDQEHNGIIRHGAKLLYAYSEATVPLMTVITRKAYGGAYDVMASKHLGADVNYAWPTAEIAVMGPQGAVNILYRDELEAADDPDARRDELIEEYREEFANPYTAADRGFVDDVIEPGDTRNRLIADLRMLKSKRKSQPDKKHGNIPL | Function: Part of the propionyl coenzyme A carboxylase (PCC) complex involved in propionate utilization and in the production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as intracellular energy reserve material when cells grow under conditions of nutrient limitation. The complex catalyzes the carboxylation of propionyl-CoA to methylmalonyl-CoA. PCC is also able to catalyze the carboxylation of acetyl-CoA.
Catalytic Activity: ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate
Sequence Mass (Da): 56903
Sequence Length: 516
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
EC: 6.4.1.3
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P05166 | MAAALRVAAVGARLSVLASGLRAAVRSLCSQATSVNERIENKRRTALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFVESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPDVVKSVTNEDVTQEELGGAKTHTTMSGVAHRAFENDVDALCNLRDFFNYLPLSSQDPAPVRECHDPSDRLVPELDTIVPLESTKAYNMVDIIHSVVDEREFFEIMPNYAKNIIVGFARMNGRTVGIVGNQPKVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKVTVITRKAYGGAYDVMSSKHLCGDTNYAWPTAEIAVMGAKGAVEIIFKGHENVEAAQAEYIEKFANPFPAAVRGFVDDIIQPSSTRARICCDLDVLASKKVQRPWRKHANIPL | Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites . Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA . Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA at a much lower rate . Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Catalytic Activity: ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate
Sequence Mass (Da): 58216
Sequence Length: 539
Domain: The beta subunit contains the carboxyl transferase (CT) domain.
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
Subcellular Location: Mitochondrion matrix
EC: 6.4.1.3
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Q168G2 | MKDILEQLEDRRAAARLGGGQKRIDAQHGRGKLTARERVDLLLDEGSFEEFDMFVTHRCTDFNMQDQKPAGDGVVTGWGTINGRVVYVFSQDFTVLGGSVSETHSKKICKIMDMAMQNGAPVIGINDSGGARIQEGVDSLAGYGEVFQRNIMASGVVPQISMIMGPCAGGAVYSPAMTDFIFMVKDSSYMFVTGPDVVKTVTNEQVSAEELGGATTHTRKSSVADAAFENDVEALAEVRRLVDFLPLNNREKPPVRPFFDDPDRIEPSLDTLVPDNPNTPYDMKELIHKLADEGDFYEIQEEFAKNIITGFIRLEGRTVGVVANQPLVLAGCLDIDSSRKAARFVRFCDAFEIPLLTLIDVPGFLPGTSQEYGGVIKHGAKLLYAYGEATVPMVTVITRKAYGGAYVVMSSKHLRADFNYAWPTAEVAVMGAKGATEIIHRGDLGDPEKIAQHTADYEERFANPFVASERGFVDEVIQPRSTRKRVARAFASLRNKSVQMPWKKHDNIPL | Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), the enzyme catalyzing the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA . Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then tranfers the carboxyl group from carboxylated biotin to propionyl-CoA (Probable).
Catalytic Activity: ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate
Sequence Mass (Da): 56100
Sequence Length: 510
Domain: The beta subunit contains the carboxyl transferase (CT) domain.
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
EC: 6.4.1.3
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P53003 | MSSATEPVGVPPAEAPDIHTTAGKLADLYRRNHEAVHAGSERAVAKQHAKGKRTARERIDMLLDEGSFVELDEHARHRSTNFGMDADRPYGDGVVTGWGTVDGRRVCVFSQDFTVFGGSLGEVFGEKIVKVMDLAMKTGCPLVGINDSGGARIQEGVAALGLYAEIFKRNTHASGVIPQISLIMGPCAGGAVYSPAITDFTVMVDQTSHMFITGPDVIKTVTGEDVSFEDLGGARTHNERSGNAHYLATDEDDAISYVKELLSFLPSNNLSSSPVFPGAEVEEGSVADGVGDADLELDALVPDSPNQPYDMREVITRLVDEGEFLEVSALFAPNMLCGFGRIEGASVGVVANQPMQLAGTLDIDASEKAARFVRFCDAFNIPVLTLVDVPGFLPGTGQEWNGIIRRGAKLLYAYAEATVPLVTVITRKAYGGAYDVMGSKHLGADINLAWPTAQIAVMGAQGAANILYRRQLAEAAERGEDVEALRARLQQEYEDTLCNPYVAAERGYVDSVIPPSHTRGHVARALRMLADKREALPAKKHGNIPL | Catalytic Activity: ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate
Sequence Mass (Da): 58526
Sequence Length: 546
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
EC: 6.4.1.3
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I3R7F2 | MTEDLLSGLSIPDDADSEEAAAIAAAVGAHLHDQTAAAVAAAADEEETWDEKRWQYAGRLDSVTGCARRVPSGAPTNAWAASGRTDRF | Function: Part of the propionyl coenzyme A carboxylase (PCC) complex involved in propionate utilization and in the production of the poly(3-hydroxybutyrate-co-3-hydroxyvalerate)(PHBV), which is a water-insoluble biopolymer used as intracellular energy reserve material when cells grow under conditions of nutrient limitation. The complex catalyzes the carboxylation of propionyl-CoA to methylmalonyl-CoA. PCC is also able to catalyze the carboxylation of acetyl-CoA. PccX could be responsible for the interaction of the biotin carboxylase and carboxyltransferase subunits.
Catalytic Activity: ATP + hydrogencarbonate + propanoyl-CoA = (S)-methylmalonyl-CoA + ADP + H(+) + phosphate
Sequence Mass (Da): 9215
Sequence Length: 88
Pathway: Metabolic intermediate metabolism; propanoyl-CoA degradation; succinyl-CoA from propanoyl-CoA: step 1/3.
EC: 6.4.1.3
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P54418 | MNSVDLTADLQALLTCPNVRHNLSAAQLTEKVLSRNEGILTSTGAVRATTGAYTGRSPKDKFIVEEESTKNKIDWGPVNQPISEEAFERLYTKVVSYLKERDELFVFEGFAGADEKYRLPITVVNEFAWHNLFARQLFIRPEGNDKKTVEQPFTILSAPHFKADPKTDGTHSETFIIVSFEKRTILIGGTEYAGEMKKSIFSIMNFLLPERDILSMHCSANVGEKGDVALFFGLSGTGKTTLSADADRKLIGDDEHGWSDTGVFNIEGGCYAKCIHLSEEKEPQIFNAIRFGSVLENVVVDEDTREANYDDSFYTENTRAAYPIHMINNIVTPSMAGHPSAIVFLTADAFGVLPPISKLTKEQAMYHFLSGYTSKLAGTERGVTSPETTFSTCFGSPFLPLPAHVYAEMLGKKIDEHGADVFLVNTGWTGGGYGTGERMKLSYTRAMVKAAIEGKLEDAEMITDDIFGLHIPAHVPGVPDHILQPENTWTNKEEYKEKAVYLANEFKENFKKFAHTDAIAQAGGPLV | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 58272
Sequence Length: 527
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.49
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Q96UL8 | MAPGANIHIPPAGPPEPGPLYSDFYQQQIERQRNNNYHSTSLRNMVATSVNRTALHPGGVQPGKGHTELEEELHEHAHIDYDRVAIIANPSVAALYEDALVYETGTAITSSGALTAYSGAKTGRSPSDKRIVKEESSEKEVWWGPVNKPMTPDVWRINRERAVDYLNTRNRIYVIDGFAGWDERYRISVRVVCARAYHALFMRNMLIRPSAEELKHFHPDYVIYNAGSFPANRFTEGMTSATSVAINFAEKEMVILGTEYAGEMKKGVFTILFYEMPVKHNVLTLHSSANEGQNGDVTVFFGLSGTGKTTLSADPKRALIGDDEHCWTDRGVFNIEGGCYAKCIGLSAEKEPDIFNAIRFGSVLENVVFDPISRVVDYDDSTLTENTRCAYPIEYIENAKVPCLSDSHPSNIILLTCDARGVLPPISKLTTEQTMFHFISGYTSKMAGTEDGVTEPQATFSSCFAQPFLALHPMRYARMLADKISQHKANAWLLNTGWVGAGATTGGKRCPLKYTRAILDAIHSGELAKAEYETYDVFNLHVPKSCPGVPDELLNPKNSWTATTSFSDEVNKLAKLFNENFQKYADQATKEVIAAGPVVQ | Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 66430
Sequence Length: 600
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.1.1.49
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P35558 | MPPQLQNGLNLSAKVVQGSLDSLPQAVREFLENNAELCQPDHIHICDGSEEENGRLLGQMEEEGILRRLKKYDNCWLALTDPRDVARIESKTVIVTQEQRDTVPIPKTGLSQLGRWMSEEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGTPVLEAVGDGEFVKCLHSVGCPLPLQKPLVNNWPCNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGITNPEGEKKYLAAAFPSACGKTNLAMMNPSLPGWKVECVGDDIAWMKFDAQGHLRAINPENGFFGVAPGTSVKTNPNAIKTIQKNTIFTNVAETSDGGVYWEGIDEPLASGVTITSWKNKEWSSEDGEPCAHPNSRFCTPASQCPIIDAAWESPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKIIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKEGKFLWPGFGENSRVLEWMFNRIDGKASTKLTPIGYIPKEDALNLKGLGHINMMELFSISKEFWEKEVEDIEKYLEDQVNADLPCEIEREILALKQRISQM | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis . Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle . At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle . At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate . Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor . The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes .
PTM: Acetylated. Lysine acetylation by p300/EP300 is increased on high glucose conditions . Lysine acetylation promotes ubiquitination by UBR5 . Acetylation is enhanced in the presence of BAG6. Deacetylated by SIRT2. Deacetylation of Lys-91 is carried out by SIRT1 and depends on PCK1 phosphorylation levels .
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate
Sequence Mass (Da): 69195
Sequence Length: 622
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Cytoplasm
EC: 4.1.1.32
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P21642 | MFWLRGGAQSCRGGETEDRMQRGMWGVGLARRRLSTSLSALPAAARDFVEEAVRLCRPREVLLCDGSEEEGKELLRGLQDDGVLHPLPKYDNCWLARTDPRDVARVESKTVLVTPEQSDAVPPPPPSGGPPQLGNWMSPNAFQAAVQERFPGCMAGRPLYVIPFSMGPPTSPLAKLGVQVTDSPYVVLSMRIMTRVGPAVLQRLDDDFVRCLHSVGRPLPLTEPLVSSWPCDRSPVLVAHIPSERRIVSFGSGYGGNSLLGKKCFALRIASRMAQQQGWLAEHMLILGVTSPSGEKRYMAAAFPSACGKTNLAMMTPSLPGWRIHCVGDDIAWMKFDDEGRLRAINPERGFFGVAPGTSSRTNPNAMATIARNTIFTNVGLRSDGGVYWDGLDEPTEPGVTYTSWLGKPWKHGDPEPCAHPNSRFCAPADQCPIMDPRWDDPEGVPIDAIIFGGRRPRGVPLVVEAFGWRHGVFMGSAMRSEATAAAEHKGGRLMHDPFAMRPFFGYNAGRYLEHWLSTGLRSNARLPRLFHVNWFLRDNEGRFVWPGFGHNARVLAWIFGRIQGRDTARPTPIGWVPKEGDLDLGGLPGVDYSQLFPMEKGFWEEECRQLREYYGENFGADLPRDVMAELEGLEERVRKM | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle. Facilitates the recycling of lactate carbon in the liver.
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate
Sequence Mass (Da): 71106
Sequence Length: 641
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Mitochondrion
EC: 4.1.1.32
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Q869Z4 | MLKNFIQKGKLINSISSSSSFQSSTFLNNNGFNSGAWVGSRFFSLEQLKKKTKNQKLINWVEEQAKLCKPDNIYICDGSEEEFKKFTDDMVKSGTLIKLNSKRPNSFLARSDPSDVARVESRTYICAKTKEDAGPTNNWMDPNQMKQTLKPLFNGSMKGRTMYVMPFSMGPLGSDISHIGVQVTDSPFVVCNMKIMTRMGDKVLNQIKENDDFVPCLHSVGAPLAKGQKDSHWPCNPNKYIVHYPEERSIQSFGSGYGGNALLGKKCFSLRIASSMAKEGGWLAEHMLILSLTNDKGEKKYIAAAFPSACGKTNLAMANSVLPGYKVQVCGDDIAWMTMRNGQLYAINPEFGFFGVAPGTSASSNPNALAAISKNTLFTNVALTPDNDVWWEGLSSPPPTAIDWLGNEWHPNGEGNNTFAAHPNSRFTAPLSQCPSIDPEWNNPTGVPISAVIFGGRRSSTVPLVYQALNWKHGVFMGASTASELTAAAEGTVGTLRHDPFAMLPFCGYNMGDYFAHWLSMEQKAGSNADKLPKIFYVNWFRKNKTSGKFLWPGFGENVRVLKWIFDRCNSTLDTTDGKATQTPIGFVPSNNSIDLNGLEINKSSLKELFSLNKSEWLHDLKSMRQFCQQFGDRLPNEIKNQMDQLENRLNKD | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate
Sequence Mass (Da): 72462
Sequence Length: 653
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Mitochondrion
EC: 4.1.1.32
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Q16822 | MAALYRPGLRLNWHGLSPLGWPSCRSIQTLRVLSGDLGQLPTGIRDFVEHSARLCQPEGIHICDGTEAENTATLTLLEQQGLIRKLPKYNNCWLARTDPKDVARVESKTVIVTPSQRDTVPLPPGGARGQLGNWMSPADFQRAVDERFPGCMQGRTMYVLPFSMGPVGSPLSRIGVQLTDSAYVVASMRIMTRLGTPVLQALGDGDFVKCLHSVGQPLTGQGEPVSQWPCNPEKTLIGHVPDQREIISFGSGYGGNSLLGKKCFALRIASRLARDEGWLAEHMLILGITSPAGKKRYVAAAFPSACGKTNLAMMRPALPGWKVECVGDDIAWMRFDSEGRLRAINPENGFFGVAPGTSATTNPNAMATIQSNTIFTNVAETSDGGVYWEGIDQPLPPGVTVTSWLGKPWKPGDKEPCAHPNSRFCAPARQCPIMDPAWEAPEGVPIDAIIFGGRRPKGVPLVYEAFNWRHGVFVGSAMRSESTAAAEHKGKIIMHDPFAMRPFFGYNFGHYLEHWLSMEGRKGAQLPRIFHVNWFRRDEAGHFLWPGFGENARVLDWICRRLEGEDSARETPIGLVPKEGALDLSGLRAIDTTQLFSLPKDFWEQEVRDIRSYLTEQVNQDLPKEVLAELEALERRVHKM | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
Catalytic Activity: GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate
Sequence Mass (Da): 70699
Sequence Length: 640
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Mitochondrion
EC: 4.1.1.32
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P53259 | MSGVSSVMLGLRPATRIFFRSNISVSPSRTFVSYIGRSQSTSILKNAPNLEDNVTNLQKIIPKRFFSQTSILKSRWKPIFNEETTNRYVRLNRFQQYQQQRSGGNPLGSMTILGLSLMAGIYFGSPYLFEHVPPFTYFKTHPKNLVYALLGINVAVFGLWQLPKCWRFLQKYMLLQKDYVTSKISIIGSAFSHQEFWHLGMNMLALWSFGTSLATMLGASNFFSLYMNSAIAGSLFSLWYPKLARLAIVGPSLGASGALFGVLGCFSYLFPHAKILLFVFPVPGGAWVAFLASVAWNAAGCALRWGSFDYAAHLGGSMMGVLYGWYISKAVEKQRQRRLQAAGRWF | Function: Mitochondrial rhomboid serine protease processing the mitochondrial membrane fusion regulator MGM1, and the cytochrome c peroxidase (CCP1). Required for TIM11 stability, ATP synthase complex assembly, mitochondrial morphology, cytochrome c (CYC1) storage and mitochondrial genome maintenance.
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38815
Sequence Length: 346
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.21.105
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P80483 | DGIADASKKFSDATYPIAEKFDWGGSSAVAKYIADASASNPRQAALAVEKLLETGLTMDPKLVRAAVAAHSKALDTAVSNPKLVASKEDFAAVNEALARMIASADKQKFAALRTAFPESRELQSSLFAGNNGYEAEKAYDSFKALTSAVRDASINGANAPVIAEAARSERYVPDGPVGRAAKKFSEATYPIMEKLNWVKSPEISKYLATASSKDPKMMAPGIDKTLEVALTMNQNLINNAVYAHVRAIKGALNTPGFVAERDDFARVNLALAKMIGSADPAKFKALLTAFPGNADLQMALFAANPEQAKAAYETFVALTSAVV | Function: Water-soluble antenna for capture of solar energy in the blue-green range. Peridinin is an asymmetric carotenoid.
Sequence Mass (Da): 34230
Sequence Length: 323
Domain: The mature protein is composed of 2 almost identical repeat units.
Subcellular Location: Plastid
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P42535 | MSTYPINAPGQSADAAVLIVGGGPTGLIAANELLRRGVSCRMIDRLPVAHQTSKSCTIHARSMEMMEHIGIAARYIETGVRSNGFTFNFENTDANALLDFSVLPGRYPFITIYNQNETERVLRHDLEATYSFQPEWGTQLLALNQDENGIRADLRLKDGTKQTISPRWVIGADGVRSRVRECLGIAYEGEDYEENVLQMMDVGIQDFEAGDDWIHYFIGQDKFVFVTKLPGSNYRVIISDLGGANKSNLEETREAFQGYLSSFDDHATLDEPRWATKWRVWKRMATAYRKGNVFLAGDAAHCHSPSGGSGMNVGMQDAFNLGWKIAMVERGEAKPDLLDTYHTERTPVAQQLLEGTHAMHEIIMGHGKGLTDRIELTQAPGWHDAATYRVSGMSYNYRDQLVSFNDDRLAGPSAGDRIPDAELAPRIRLFDLVRNTRPTLLVAPATEAEVAEAEKLRDLIREQWPLVKPVLVRPQGSEESIEGDVHVDSYGQLKREWGDNAKGWAALLRPDNYIHARAGLDRGDLLVQAIDAMLVRCA | Function: Dechlorination of pentachlorophenol to tetrachlorobenzoquinone. Removes also hydrogen and nitro, amino, and cyano groups from benzene ring at the para position in relation to the hydroxyl of phenol.
Catalytic Activity: H(+) + NADPH + O2 + pentachlorophenol = 2,3,5,6-tetrachloro-1,4-benzoquinone + chloride + H2O + NADP(+)
Sequence Mass (Da): 59992
Sequence Length: 538
Pathway: Xenobiotic degradation; pentachlorophenol degradation.
EC: 1.14.13.50
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Q03520 | MPEVSLYNYTMSICSMKTRLAMEEFGVDYDDKQVDIGFALENFEPDYVRLNEKAVVPTLVVGDRVVTNSYNIVLEAAKLGKVGIPADPVENKAALDWFQKGDQVNFQVITYGHKGVPRGDELLIARRERAKEYAEKYPELRSIYQAAHDRIVEHGNCAYDADTVAQAEVDLQKRLDELDAHLADKPFIAGSNYSIADIMWTVLLARIEMLNMTAWISERPNLLAYYQRMKARRSFETARVMPNWKGGI | Function: Sequential reduction of tetrachloro-p-hydroquinone to monochlorophenol, using glutathione as the reducing agent.
Catalytic Activity: 2,6-dichlorohydroquinone + chloride + glutathione disulfide + H(+) = 2,3,6-trichlorohydroquinone + 2 glutathione
Sequence Mass (Da): 28246
Sequence Length: 248
Pathway: Xenobiotic degradation; pentachlorophenol degradation.
EC: 1.21.4.5
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Q47914 | MTNPVSTIDMTVTQITRVAKDINSYELRPEPGVILPEFTAGAHIGVSLPNGIQRSYSLVNPQGERDRYVITVNLDRNSRGGSRYLHEQLRVGQRLSIVPPANNFALVETAPHSVLFAGGIGITPIWSMIQRLRELGSTWELHYACRGKDFVAYRQELEQAAAEAGARFHLHLDEEADGKFLDLAGPVAQAGQDSIFYCCGPEAMLQAYKAATADLPSERVRFEHFGAALTGEPADDVFTVVLARRSGQEFTVEPGMTILETLLQNGISRNYSCTQGVCGTCETKVLEGEPDHRDWVLSDEKKASNSTMLICCSLSKSPRLVLDI | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Involved in the degradation of the xenobiocide pentachlorophenol (PCP) . Catalyzes the reduction of tetrachlorobenzoquinone (TCBQ) to yield tetrachlorohydroquinone (TCHQ) . Also able to reduce 2,6-dichloroindophenol (DCIP) .
Catalytic Activity: 2,3,5,6-tetrachlorohydroquinone + H(+) + NAD(+) = 2,3,5,6-tetrachloro-1,4-benzoquinone + NADH
Sequence Mass (Da): 35598
Sequence Length: 324
Pathway: Xenobiotic degradation; pentachlorophenol degradation.
EC: 1.1.1.404
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Q8KN33 | MGLLIDGVWRDAWYDTKSSGGRFVRKESQYRGGLDAGFRGEPGRYHLYAGFACPWAHRVLIMRALKGLEEMISVSMVNAYMGENGWTFLPGDDVVPDSINGADYLYQVYTAADPTYTGRVTIPILWDKVEKRILNNESSEIIRILNSAFDDVGALPGDYYPAEFRPEIDRINARVYETLNNGVYRSGFATTQEAYEEAFYPLFDTLDWLEEHLTGREWLVGDRLTEADIRLFPTLVRFDAIYHGHFKCNLRRIADYPNLSRLVGKLASHERVAPTINLRHAKAHYYGSHPSVNPTGIVPVGPAQPLPGLTLQS | Function: Catalyzes glutathione (GSH)-dependent reduction of glutathionyl-hydroquinones (GS-HQs) to the corresponding hydroquinones. Can act on halogenated substrates such as GS-2,6-dichloro-p-hydroquinone (GS-DiCH) and GS-trichloro-p-hydroquinone (GS-TriCH). Involved in the degradation of pentachlorophenol (PCP), a toxic pollutant.
Catalytic Activity: 2-(glutathione-S-yl)-hydroquinone + glutathione = glutathione disulfide + hydroquinone
Sequence Mass (Da): 35382
Sequence Length: 313
EC: 1.8.5.7
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O34790 | MYDVTEWKHVFKLDPNKDLPDEQLEILCESGTDAVIIGGSDGVTEDNVLRMMSKVRRFLVPCVLEVSAIEAIVPGFDLYFIPSVLNSKNADWIVGMHQKAMKEYGELMSMEEIVAEGYCIANPDCKAAALTEADADLNMDDIVAYARVSELLQLPIFYLEYSGVLGDIEAVKKTKAVLETSTLFYGGGIKDAETAKQYAEHADVIVVGNAVYEDFDRALKTVAAVKGE | Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Cannot use glycerol-3-phosphate (G3P) or 3-phosphoglycerate (3PG) as an acceptor.
Catalytic Activity: all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate
Sequence Mass (Da): 25088
Sequence Length: 228
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
EC: 2.5.1.n9
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B1YJ15 | MLLPYNEWRHVFKLDPAKEIEEAALQAIATSGTDAIIVGGTDDITLDATLDLLMRLRRYPVAVALEVSELEAATMGFDAYLTPSVLNSGTLEHVIDKQVEALEEVGHMLAHQDLVGEGYIVLNADAKVARVTQAKLLNDDQVVAYAQLADSVFRMPIIYLEYSGMYGDPSLVASVKRVLKQGRLFYGGGIDSIERAQEMLTHADTIVVGNIIYDNLEAALATVAATR | Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales.
Catalytic Activity: all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate
Sequence Mass (Da): 24751
Sequence Length: 227
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
EC: 2.5.1.n9
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Q9KF39 | MMLEFQEWRHVFKLDPNKELNDDDLEAICESGTDGILVGGSDGVTLDNTLQLLARIRRFSVSCALEVSNLESITPGFDHYFIPSVVNSGEVKWISGLHHEAVKEFGPIMNWDEIVMEGYCIMNPDSKAATLTSAKTDLANEDVVAYARMVENMYQFPVFYLEYSGTFGDPQLVEEVSQVLTKTKLFYGGGIRTVEQAEQMAPFADTVVVGNVIYDDVQAALATIAAVKK | Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales.
Catalytic Activity: all-trans-heptaprenyl diphosphate + sn-glycerol 1-phosphate = 3-heptaprenyl-sn-glycero-1-phosphate + diphosphate
Sequence Mass (Da): 25391
Sequence Length: 229
Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
EC: 2.5.1.n9
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P20372 | MSQIIWGAYAQRNTEDHPPAYAPGYKTSVLRSPKNALISIAETLSEVTAPHFSADKFGPKDNDLILNYAKDGLPIGERVIVHGYVRDQFGRPVKNALVEVWQANASGRYRHPNDQYIGAMDPNFGGCGRMLTDDNGYYVFRTIKPGPYPWRNRINEWRPAHIHFSLIADGWAQRLISQFYFEGDTLIDSCPILKTIPSEQQRRALIALEDKSNFIEADSRCYRFDITLRGRRATYFENDLT | Cofactor: Binds Fe(3+) ion per subunit.
Function: Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Catalytic Activity: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 27548
Sequence Length: 241
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 3-carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1.
EC: 1.13.11.3
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P15110 | MDSPTILTPRDWPSHPAYVHPDYRSSVKRGPTRPMIPLKERLRDQYAPVYGAEDLGPLDHDLTKNAVKNGEPLGERIVVTGRVLDEGGKPVRNTLVEVWQANAAGRYVHKVDQHDAPLDPNFLGAGRCMTDAEGRYRFLTIKPGAYPWGNHPNAWRPNHIHFSLFGDYFGSRLVTQMYFPGDPLLAYDPIFQGTPEAARDRLISRFSLDTTEEGHALGYEFDIVLRGRDATPMER | Cofactor: Binds Fe(3+) ion per subunit.
Function: Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Catalytic Activity: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 26550
Sequence Length: 235
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 3-carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1.
EC: 1.13.11.3
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P00437 | MPAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC | Cofactor: Binds Fe(3+) ion per subunit.
Function: Plays an essential role in the utilization of numerous aromatic and hydroaromatic compounds via the beta-ketoadipate pathway.
Catalytic Activity: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate + 2 H(+)
Sequence Mass (Da): 26793
Sequence Length: 239
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 3-carboxy-cis,cis-muconate from 3,4-dihydroxybenzoate: step 1/1.
EC: 1.13.11.3
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P49584 | MDAQSSAKVNSRKRRKEASSPNGATEEDGIPSKVQHCSVGLRQPAPFSDEIEVDFSKPYVRVTMEEACRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYPIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEERSIDLIQTWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPRQSPSSSPTHERSPSPSFRWPFSGKTSPSSSPASLSRHKAVTCDISEDEED | Function: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
PTM: Phosphorylated . The serine residues of the C-terminus are phosphorylated (By similarity). The inactive soluble form is stabilized by phosphorylation, the active membrane bound form is promoted by anionic lipids or diacylglycerol, and is stabilized by dephosphorylation (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: CTP + H(+) + phosphocholine = CDP-choline + diphosphate
Sequence Mass (Da): 41717
Sequence Length: 367
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.7.15
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P49585 | MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYVRVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHNFKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDDVYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKYHLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALKHMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYDISEDEED | Function: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
PTM: The serine residues of the C-terminus are phosphorylated. The inactive soluble form is stabilized by phosphorylation, the active membrane bound form is promoted by anionic lipids or diacylglycerol, and is stabilized by dephosphorylation (By similarity).
Location Topology: Peripheral membrane protein
Catalytic Activity: CTP + H(+) + phosphocholine = CDP-choline + diphosphate
Sequence Mass (Da): 41731
Sequence Length: 367
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.7.15
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Q9Y5K3 | MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHEKLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHKFKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDDVYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRYRFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWKQMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISSMSEGDEDEK | Function: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis.
PTM: Phosphorylated.
Catalytic Activity: CTP + H(+) + phosphocholine = CDP-choline + diphosphate
Sequence Mass (Da): 41940
Sequence Length: 369
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
Subcellular Location: Cytoplasm
EC: 2.7.7.15
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P49583 | MFIHKQEKMPQRKRTMDSPQEEDVEVKKKATEVEYVVRSLASDEPAPFSDEALAITTREAVDYSKKITLAMAEANEAGRPVRIYADGIYDLFHHGHANQLRQVKKMFPNVYLIVGVCGDRDTHKYKGRTVTSEEERYDGVRHCRYVDEVYREAPWFCTVEFLKNLKVDFIAHDAIPYVAPGEEDLYEKFRREGMFLETERTEGVSTSDVVCRIIRDYDKYVRRNLQRGYSPKELNVGFLAASKYQIQNKVDSLKSKGIELLSTWKSKSDDIIRDFIDTFHKDGGLNAFGGRLKGIMSMSRSPSPSPHEGSPTGIEHHLETQDEEEEEEALEEEKVVEQKIVEKKEVVKKRSSRNKAKTPLEY | Catalytic Activity: CTP + H(+) + phosphocholine = CDP-choline + diphosphate
Sequence Mass (Da): 41769
Sequence Length: 362
Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
EC: 2.7.7.15
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