ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
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A0A3D3Q9K3 | MTISVEEALGTRPVARTLALRAFGVLGLALTGWVFAATVSDGAGSMRLVVAGLLVFWAATGLLLALRRPAEITLAVVVSGAAALAAAGVRADVVRPFAVALLPWAAMAIVLAMPNGALETKARRVFALLGGVAGLAAGAVLFGRRNHLPAWPFVAMAVIAAGVAAGGFAARYGRTDPTGQRRMKWLAWGAVVAAGVAVAAFGLHVLVEWPRHTGVVATTATALLPVSIVLGTDRRAVKAIDPLMARTIVAAGLTAIVIAVYLAVVLGLGRTPRHDERTLLALSMVAAVVAVLVYLPARGRLKAFATRIVYGHRRDPEDVV... | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A2G8JPC8 | MLPPITSLPVLLGLALLTRLTLIVYGEWQDRVMLVKYTDIDYSVFTDAARYAWEGHSPYERATYRYTPLLAWLLTPNIWLHSTFGKLLFCCFDLLAGFLIYRIISRLTLNKNLIAGSLVLWLFNPLTLVVSSRGNAESIMSFLVLATLDLFISGKYTLSAIVWAISVHFKIYPITYALPMYLSIRGHTGETQNQDATINRTTWKALQDILKLFRPNVERIKFFFISLTTFSFLTVGFYYCYDWEFLQETYLHHLTRSDTRHNFSPFFYLLYLTSAWTQLQKFLSLVVFIPQAILLVVMAMKYYEDLPFCWFLQTLFCVFQ... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum mem... |
A0A0D1EGE3 | MSETDPRHERADPARPEAEEEEPPLFQFEMQDPIEPALAGRFEDLAPRLVTALLLLAVGLASIWIGGLFFTALISLAVGLMIWELATIVRTGPRRAMLLAGTGGVTLFLSSVLPVGFGLPLMMLVPMLAIAVIRKHRRLMVFFPTAIMLAGLALTEHLTNFGFWWMIWLILVVIASDVMGYFAGRMLGGPKFWPRVSPKKTWSGTIAGWVGAGIVGLIWAIWMDAGWETIGISVALAMMAQMGDIAESAVKRRFGVKDSSNLLPGHGGLFDRFDAMLGAALMLLVIESVAEFPPIPGV | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 298
Sequence Mass (... |
A0A7M3Z5W8 | PSGPPSGPPTGPPSGPPSGPPSESVEEEQQEEPEEPPQEEPEAPAPEASEEPVAEDEASAPTESTEEPASTTDTSVSDEAEAEPVTEPSEEPPAPPAPDQHTLDLLAEKEAELERLHMENARLRQSVVGATEVIEELEEPPMPPLVEDNIVIPPYIVSDFVRLGRQLDREHLVRATMGSMAMIHPEQPGVMISTRHMVTLPRMNERSLCAAPLGSTSPRGAPSDWHALEVVLASVSMVTGGPAAVIHMHGPHTTAASCEKDLVLLTPIDEIGKQHIGKIIIVDPDPDHPEDYLRQVAEALNQGGMRCVVIRGNGAYAVGA... | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 4.1.2.17
Catalytic Activity: L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate
Sequence Length: 349
Sequence Mass (Da): 37373
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A0A3A5V2H3 | MKVESPATIKLRPTRGCQSPITADFRLLERGPESGPDSERRNENMSQEGKYVIHASIRTDGNVQRKDVVGAIFGQTEGLLGEALQLRKLQRTGRIGHVDVVLHQNKGKVQGEILVSSSLDQVSTAVIGAALETIDRIGPCKAVIKVKMIENQQSSKRDHVIERGKQLLLKMVNSGVDDSKNILEEVRAVLTLDKETEYHGMTAGPNVTESEAIIIVEGRNDVRNLLKFGIKNAIATMGSGIKPELVELAKSKKGVTAFIDGDRGGKLLLMEINGQLGKALTHVAMAPQSREVEHLEGKVVTKYLQQKEVASKAVPRIQSE... | Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteropolymeric, adenine-rich transcri... |
A0A3N5KV79 | RPSDFAPRLAQVEADPSRACPFCPGAEDATPPALATYPREGGWLVRVVPNLYPAFSGEEPLSVTNDGPVFIAAPASGIHEVLVISPDHEASLADLGDGAAALVMQAVRDRMQEHASHSVVRYTQAIINHGREAGASLAHPHAQLLGMPFVPGAILEEEAGFSRFEGNCLLCATAEAELGDDLRVVVDTDAALVICPYWSGTPFEMLMIPRRHEPHLTATPDTDLSSIGVVLRDAMRMLRDQLGDLAYNVVVHTAPFRHNRQFHWHAHVWPKLVSVAGFERGTGVMINITPPEFAAAQLRTASV | Cofactor: Binds 1 Fe cation per subunit.
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 303
Sequence Mass (Da): 32738
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A0A7M3XYV2 | MGVLLELADANVFRIRSYQNGSRTLGTLTDDLWELVQTGRLVEIKGIGKGLASAIDQAMRDGAWPKDWVELHENTPPGMLEMLDIPGLGPKRIRMMHDALGVTSIEDLRTACESGQVAELKGFGAKSQTKLLDGIDLLARFRSRRRLDVGLMYGEAFQSRVATIDGVLHATLAGSARRRRETIGDLDLVVAVEEENHSAVAEAILALPGIADVKGAGSSKISLILDTEIFDDAFALPHLDANVLDAIGGAEYESMEAGGTIDAQVRLVPPHVAPFTLAYFTGSKEHNIAMRQRAIDLGLRLNEFGLIPEALAGDLKGMDA... | Function: Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in ... |
A0A2S6SFE4 | MFSDPQFWVLISFIIFVVLIFNPIKKILTKNLDDKIEQIKTDINNAEKLKNDTQVILSEIKKRQNDVKNEINLINEQAKERIGSIENETHLKLQEQLNKKNAIAAAKIEQMTRDANLEIQQEITQISISASTDLLIKKLSDKDKQNIVKESTEEIGSIIKN | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
Subcellular Location: Cell membrane
Sequence Length: 161
Sequence Mass (Da): 18514
Location Topology: Single-pass membr... |
A0A3D5DN51 | MTPLPPGGTAGAGSGWRWAPDPTLLRSGWKERGDWPGPAGPDVPGPRPGRWPTLAGEQGVMPVDRLTAEDLLMLWPDEIWPQEIGALAVLDGSSLLAPGGCFRIEAVREVIAARLHLVRRFRQLLYVPRRGLGGPLWVDAPSFDLGDHVRIVPLPDPGDEAALLLATERLRRRRLDRSRPLWEMCFLPGLPENRVGMFVKMHHAIADGIAGVATLGALLDAAPGVPTGSAQPWTPAPPPAARDLRTGASPSSAATSAWSRRSPISTARRSTTSCWRSPPAACAGCSAIVANPSTTSSCRSTYPSRCARHRHELRRGET | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
EC: 2.3.1.20
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Sequence Length: 318
Sequence Mass (Da): 34165
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A0A2E7UJ98 | MDNVLVIGSGFLGKNVVNEFKNNGIHVIGTNYNKNSKNEVYVDITNVDSITSCVKKYSPKIIINCAGNVNVDELENNEKLAFSINANGAENIAKVCKHNEIRLLHISSDAVFDGKQGMYVEEDIMNPINTYAKSKMLGERLISEILENYVIIRTNFYGFHSQNKFLFNWILSKLKNNE | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 178
Sequence Mass (Da): 20112
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A0A2E7UK64 | MSSIDNLILNDLATFDSATVQNAAIRIRGYVHENEDYSGSSIRRYTGDINATVVGVATTIKATALHDPKEVGELSVPWKDYYEKLSSFELPTISVFEDVDKPKNRAALFGDNMAFMHSCLGTVGVIVSGAIRDVPGIQRSGLSVWAKGRVPGHGPFNAIGLGEQVAVSGLKINEGDILVADGDGITRVTSDILDQIIDTCEEVRKDESQTQKFFSVKDKSRYKSWISKDYT | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A1Y1KMR8 | NGERKVPRERKVHASGLLKALSFEFLFLVIFELRLADYSCTYFLKVNMISLIHIFIVSVLFCTGYCDSCKNAEISSKSFTTQDATIVTNIAYISEFSVKCGSGSLSHAYANVEGTVVPVFETAPSTFQVSWTEEIKNARRGEIKIRLFDEDGYTALRKALRANEDISTVSPLFSVSVSHPGAFNGPWLKSEFLAVALSVVVAYLALSSRSKLLS | Function: TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 214
Sequence Mass (Da): 23643
Location Topology: Single-pass type I membrane protein
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A0A089NB47 | MSKPRLSIYNRYVPAVVQETGFEGPAYWFIFRAGQLLVAEDSGAAAVPLALSPEELTVASIRTLYLGTFGSIPCFAAEASPEATEPPGLLFRPLRSLYEAMDEDLFHLAGKAVQLLAWDETHLFCGRCGTQTVPSEAEWSRKCPECGLVSYPRIAPAVITAVLKGDEILLAHAGHFQNNMYGLIAGFVEPGETLEDCVQREIMEEVGLKVTNIRYFGSQQWPFPHSLMVGFLADYESGEIAVDGEEIVHADWFRPDSLPVIPAKVSIARKIIDWYIGQYTRC | Cofactor: Divalent metal cations. Mg(2+) or Mn(2+).
Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at th... |
A0A538GHD4 | MRATRYAALRRCARGCASVRRRAQLLALEPSLSIEPLRGNVETRLRKRGERGLDAVVLAACGLDRLGLAGEIGLRFAPEQLLPEAGQGALALQVRVGEEELVAAADDVETRRRVEAEREVVFAIGGGCLAPVAAHHDGETLTALVADEDGAWIERRSGDDPAALAAELTALAQN | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 174
Sequence Mass (Da): 18512
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A0A2H0R6H1 | MCGILGAISAKPEPLLPEWLFFNLSHLQHRGQESAGTAYSDGKQLWIEKGEGLVSHVLTEDKIRKIGNYNPKLIIGQIRYSTSKGTSSRNIQPQWLDTLQGRIALVHNGNIPNLEEKKIELRRESNWQVDIDDEANDSEFILKKIFFLMTLNGNNASKAIGEFMATTNGSYSAALLTKNSVHIFRDPWGNRPLFISSKNGLIFFASETCALEDCSDKIKEVPSGGIIKIEPLGDIVRPFVDIENYQTIKARPRLAHCVFEKIYFARPDSRTFGKEQEGNFRFRLGQKMAELFPVHGADFVSGIPESGRPAAVGFAFQSKL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
EC: 2.4.2.14
Catalytic Activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-phospho-alpha-D-ribose 1... |
A0A1M5XT97 | MTESSAHNIPVYILCGGKSSRMGRDKGLAMLQEKHFIDHIISGINEVSKEIVFVTQNSEYSRFGLPIVNDHYIDKGPLGGIHAALKHTNQERILILSCDIPLLDASVLKRLIAEKKTADIIFAETATNWHPLIGIYSKRILKNLEAHLEKDQLRLFDFIKTNNYRALNFTAERAFTNINTPEVLARVEQELN | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A1Y1MVK8 | MDQLFCHHILSIETLIYLGLLRSLTGNCLLVQIFINVSCSFHEAFQCYASVLIAADKKDSALIYQLACKIYEELKKIVERNVVDNRPSYLHRFTPGHKYTKALWHAIPFVIKPHKELACEWLKFLLDQRLFCQYLRGAWFIQLTIIQTKHLKKYDEVTKTLIDSLQDTSLRNIHRMELNKRAEKIKHNKTYKISQIDFGTISSVQPLPIKNLPYREIDAQAFRSENSGQKRNYYIRIDNGFELYSVEEVALNYYEQNFGLNGIHCENSLLITSFFLLFWDIIYDHTIPSVFVSEIQHYPLDLYSTEFYTSRRRKIGKRLS... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A2G8KH37 | MDALESLKEYGSDDSSDEEPSPKVSELKLPELPSSILSMFKDEIEDDSRSNGELHKGRQRSFPHVPGNWATFVYCNVSVSDAMTRLMADLLGCFNTEDEGEEVKVELMEDVHVSLSKTVTLQYHCIEPLTADLMQGLTATIPQFDFSFDGIKILTNDEKSRSFLALTVGVGSSQLQSAVDVVDKCLGEYSLESFYKDACFHASFAWFLGDASDIITTGLRGRLEVNNWVYQQIVTIKIVQLLRNAFIDTSLHFLNVLIRFGVSLGASNLASN | Function: Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA.
Catalytic Activity: a 3'-end uridylyl-uridine-RNA = a 3'-end 2',3'-... |
A0A2M7JMV3 | MKLIKICLFIVISLAFLIAPAGGAQKNVKKQSVKPSSKTTAKTAQSGTKNKEARDQPQEGTAPFKASIVLEAETGLVIEGENVHEKCPIASITKLMLAILVLDRLESGQIKLDDKVTVSQEASAMGGSQVFLKPGEVFTLDEIMKAVMVASANDAAYAVAEFIAGTRNAFVDIMNERAQKLNMADTQFFSPHGLPPSQDQLADVSSPNDMGILARELVKHPQLLAWSSLNTAPFRDGTLIMRNHNKLMPRFSGMDGLKTGFYREAGYSIVATAKREDMRLIAVVMGSPAAKVRDNIVNEKLKKAFAQYQMVRLVKKGDPA... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
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-alanin... |
E9DNM7 | MAKKEQNSQEKQVLTEWQKRNLEFLRKKESEDSEGIEKENTPIENKVPEKKKVKKKKKAKKKKKNKLKSSSNIPIAQQNLAGLIVFSAAILIVFSLFYISPWSKQKIITVSGTKNALPEDVKVASGILDTDYISYVFLNQNKVARTVEKTNVWVKKANVTYDFPNQFNIAVKEYPIVAYRQTGNGYMSILESGKTGGTVSTGNLPDKFITLKIDDDKKIEELVKELNQLDAKIKNNIQIINLTPTKATSDLLTIELYDGNTIRVPLSQLTTKLPYYQKIKKHLSDGTIVDMEVGIYTTTPEVEASKSEKSDKDKKKDKDK... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Subcellular Location: Cell membrane
Sequence Length: 375
Sequence Mass (Da): 41910
Location Topology: Single-pass type II membrane protein
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A0A538FUR7 | MPGPSGDQSTNHRLGEIADSFFRPPVRDLVPYEPGKPVEEVQRELGLDRVVKLASNEGPFGPFPAALEAIQRSAPDLNRYPDGGAYRLRAALAELHDLRFEEVAVGAGSDGLVDSLSQIALDPGDEIVCGWPSFPSYAIDARKLGAVPTTVPLRDDRYDLETMLGAITPRTKLVYICHPNNPTGTMNTRAELDAYFDRVPVHVLTVLDQAYFEYIDDPDYADGIVEFLKAGRRVVVLRTFSKVFGLAGLRVGYALAPPPVVTALSKVRRAFDITTPAQEAALASLGNPREIERRRLENAEQRTEVERILREHGLEPAGPA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 366
Sequence Mass (Da): 39848
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A0A7V2QEK8 | MGNSGLDDLTVLAPAGVPPDPEALKVLRRLARAPWVAAPPVALPDLHLKPRLETPSSVVVATSGVVVPSLTSPSLHCGMSLVVTDLEEGFATEARLDRLFAHLAARLAPRREGDALGDEGLDQVLCGGMEAWRSRVPQVEMMPTMAGRREGPLDPAALEMIPSWLRAVARREFGTVGLGNHFLEMQVVEEVIDPRRAAAWSVERGRIVFLLHADAGHLGAVLGRLLAHRRKNSWRGRLREWRAKVPYHVRDVRSLRGLVERARLFLPARWVPLREDSAVGRLCRSAASLVARYGAANRLAVWEAVAEALAAVGGPGGLRL... | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.-
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 454
Sequence Mass (Da): 49035
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A0A6I2W413 | MSEQVSDRSGIFERLLKDRIIWLGDEVRDDNANEICAKMLLLAAEDASKDIFLYINSPGGSITAGMAIYDTMQYVPNDIVTVGVGMCASMGQFLLSSGTKGKRYATPNTRVLLHQPSGGFGGTASDIQTQAELILSMKQQLAGITAEQTGKTADEIMAAGDRDRWFTAQEALEFGFIDHIQKHAARATGVGSN | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
A0A2S1U3A2 | TLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFVXIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLTLLLASSMV | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A7V0YFR9 | MGKYSIRVEKDYLKFSAAHFLIFSEKCERLHGHNYAVSVELEGELDETGYVFDFIVLKEFAEQHCNKLDHRTLIPSKNKNIEIVETNGSVEVKFRDKRFVFPESDVLILPIKNCTAELLASYLCQKVKEDLDDIGITNITSIKVGVEESPGQAAYYIEEIG | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 161
Sequence Mass (Da): 18367
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A0A2G4GME3 | MSNAGSYTHNFASRHIGPDEQSRSIMLSALGYQNLEELIFDVVPQSIRLKSEMALGEGLSEVDALAEIRELVSENEPKRSLIGMGYYGTHTPGVIKRNVLENPAWYTAYTPYQPEISQGRLEALINFQTMIADLTGMHLSNASMLDEGTAAAEAMTLALRSYKGSSRTFLIDADTHPQTIAVIQTRAKPLKIHVQLWDSGDPLPDAFGLLLSYPGSSGLVRDISSDITAIHALSGIAVVASDLLALTLVKSPGSLGADVVVGSSQRFGVPMGFGGPHAGFMGVRAGLERSLPGRLVGVSVDDVGTPAMRLALQTREQHIR... | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity... |
A0A1M2YI27 | MVFVLYVDMDYFFAACEEVRHPELKGKPLVVGTAPVNEKFRGVVQTANYEARKFGIHSGMPSIKALDLCKELNYLHSDEEHYESVSAEIIKVLRSYGKPLEVISVDEAAMDITGLTDEEALELSRDIKSRIKKSFGLTCTIGISNGKAFAKMASDKAKPDGLMLVKAQELRSFLDSCSLDKLPGVGSKTHEKLKELGISSISELSKSDPMVLIDAFGSAGKELYMLANGIDESKIVESSEILSIGREVTLKSPATSVDEVTPVLKGLIDEVMKEIEKNGVLFRNVGAKVRYTDFSISAKSYSLHNYSDSREEIEKRAAPM... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A7W1K1T4 | MDAASTRPNVSDELRRLRELDACAVSDALDSLGLGGVVAGIGPLWPAGRLFGTVRTVALRPVVAGEPPSGTHLGATAIDTATAGDVIVVANQGRVDSAAWGGLLSAAAARKGVAGVIVDGACRDVDEAAGAGLAVFARAATPISARGRSVEEATDAPVEIGGVRVATGDLVVADASGVVFVQSDSANEVLEVAERIVEKERSMLHELSAGAPVQAVLDGRYETMLRGERGSLTQTGSEGREGDAHAVD | Function: Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
EC:... |
A0A538HIY7 | MTRVHPLEPLTADEIEAAVAAVRATGRVTEAARFSTITLDEPPKEAIAAFDRGETVERRVRLLIVPSPECAVVEAIVALPSGETVSWEERPDVRPALLFEEAIKAIVAVQENPEWQAAMRKRGIEDFDKVQIDPWPTGNFGIPLEEGRRIARCLFYYREEPTDNGYARPIEGVLATVDMARGVVLEVVDYGVVPIPEERGSYYPEDNEPQRTDLRPLEITQPQGPSFTVEGNLVRWQKWSLRVSMDPVEGLVLHTVGYEDGGRVRPILHRASICEMVVPYGDPGPMHSWKNAFDAGEWGLGRMANSLALGCDCLGEIRYF... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
Catalytic Activity: an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
EC: 1.4.3.-
Sequence Length: 333
Sequence Mass (Da): 37008
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A0A2G8KAV5 | MESTVVGYRVVRGPDWRWNDQDGGEGNLGTVVEVGKKGSSTSPEKTVIVQWDNGSRTNYRMGYHNAYDLLIYDNATVGIQHVNILCDACNKQGFMGMRYNCTQCQDFDLCASCYHSDKHDLSHHFLLYITPSSVGVKLPPRSSAIKIGYRGLVPGAKVMRGPDWDWGNQDGGDGKIGRIKDIRGWDSESDRSVANVQWSNGNTNVYRVGHKGKVDLRCLDSVKGGTYYKDHLWKLGQKVAKNSVSAYGKKWSFVHGEKVKVNLDVAVLKIMQGDHGGWNAKMEEYVGQEGYVHRITEKGDIRVQYSDGIKWTFHPGALTK... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 830
Sequence Mass (Da): 91611
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A5CZS8 | MPEQAKPYPPLAEVTKNQPVFEMRNVRGSVVGFYCPPYIEGLNVPGYHLHFVTEDRRQGGHLLECSLQEGTLQMDQTRGFYMTLPAGSDFAKADLTTGRTEELKKAES | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 108
Sequence Mass (Da): 12120
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A0A538CP68 | MKRFTIIAVLGAVTLAVTLSVGAWGKGQGKGHIKAKGHSVTVIEHPTTDTTTDTGAAGDSVGDILTFANDVFDAKDSAKVATDQGYCIRVVAGESYECNWTTFLPRGQITVEGPFYDAKDSTLAITGGTGRYRHVRGTMDLQSKGDGKYAFVFHLNS | Catalytic Activity: (9Z,13S,15Z)-12,13-epoxyoctadeca-9,11,15-trienoate = (9S,13S,15Z)-12-oxophyto-10-15-dienoate
EC: 5.3.99.6
Subcellular Location: Plastid
Sequence Length: 157
Sequence Mass (Da): 16677
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A0A6B8K4Q6 | MLNKSILAAWLVALTATIGSLFFSERMGFIPCTLCWYQRILMYPLVFLLGVAFYRNDKKIYVYALPLSIIGICVSSYHYALQKIPSLQEFSACTSGVPCSGQYINWFGFVTIPFLALLAFVMITVFMLGLWKKK | Function: Required for disulfide bond formation in some proteins.
Subcellular Location: Cell membrane
Sequence Length: 134
Sequence Mass (Da): 15217
Location Topology: Multi-pass membrane protein
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A0A7N0V7P1 | MIDYYFKAHHASSDSNLKFRNPKYLSILNHLRFYLPEIFPRLNKVVFLDDDLVVQKGISGLWSIDLKGNVNGAVETCGENFHRFDKYLNLSNPLIASNFDPRACGWAYGMTILI | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 114
Sequence Mass (Da): 13114
Location Topology: Single-pass type II membrane protein
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A0A7J9X0H9 | MGTQIVAYQGEAGAYSEEGVISTFPDAEHLPLQSIRKVFESVEVGKADYGLVPMDNSQAGSINQTYDLFLKHGLHLVAETVVRVNHCLMALPGTHMDDLVEVISHPQAIAQSEEFLTSLDVSVRAEYDTAGAARKIVDDKLEHTGAIASKRAAEFYGLDILAERIQTYPDNYTRFGGLARNPEPLR | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 186
Sequence Mass (Da): 20391
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A0A6V8DM08 | MSAKDAAKIPKRIEAIKFTLMDPNEIRKMSSVEVKTADTYKDDGHPFKQGLMDPKMGVIDPGVRCETCGNKHDECPSHFGHIALELPVMHIGFTNLIKTSLKCTCNTCSKILLHDKPDTHPVDPEKSEQDYYTDKVKDVIIKHGVGSTEFKNTIKDIEKECSSKKRTICMHCGAEQGKIILDKPSTFKEKKDNKGEHKLNARDIREWLERIPDEHLIFLGMDKDAARPEWTIMKVLPVPPITVRPSITLDSGDRSEDDLTHKLVDVLRINQRLRENRDAGAPQLIVEDLWELLQYHCTTYFDNQTSGIPPARHRSGRPLK... | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 401
Sequence Mass (Da): 45460
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A0A2W4J8I6 | MLEAVGYTSLESLVETAVPEAIRHDDILDLPEPLTEAQALAALEDFAARNTQAIEMIGQGYYDTITPAVIRRGILENPAWYTAYTPYQAEISQGRLEALLNFQTVVSDLTALPIAGASLLDEATAVAEAMLLMVRASGK | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity... |
A0A1C8XYP9 | FGAWSSMVGTSLSMLIRAELGYPNALXGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLSAPDMAFPRLNNMSFWLLPPSLTLLLTSSLVESGTGTGWTVYPPLSSTLSHSGASVDLSIFSLHLAGISSILGAVNFISTIINMRAPGMSFDKMPLFVWSVLITAILLLLSLPVLAGAITM | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A7V9BFX2 | MLITGAGGQLGQALAEEFPEALALTRSEWDVALPAPSLLPRPDVVLHAAAWTDVDGAEDDPQGAVAVNVGGTANVAELGAPLVYFSSDYVFDGFKREPYVESDGPRPLSAYGRSKLHGEAAAGEGSWIVRSAWLFGPTGHNFVRTMLR | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 148
Sequence Mass (Da): 15666
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A4VBP8 | YILILPGFGMISHIISQESSKKETFGTLGMIYAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLNYSPSLIWALGFVFLFTMGGLTGVVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLFTGLVMNSKYLKIQFIIMFIGVNLTFFPQHFLGLSGMPRRYSDYPDAYTTWNIISSIGSLISLVSIFMFLFIIWESFISMRKSIGTLSMTTSIEWLQAMPPAEHSYNELPLL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A3M1E0E7 | MGSVEAALTLLGAVALDLLFGEPQGAFHPVVWMGRWLEGWWRLRPQEGRVRQFLFGMTAVLLGVVLFALPGWFLARASLPLFWLWSAPLLKVTFALRALLRAGEEVLEALERGDLPEARRRVRWHLVGRETADLPEP | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 15481
Location Topology: Multi-pass membrane protein
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A0A6V8EQG2 | MEQIQPMSPNGIFQYKLPPSKSHMIRELMLASKSSEVTEINFQGTPGEDIISMANCLEKMGVKIEKRTTKWIVYPPKKGLISPKGAIYCGNSGTVARIMTALAATFDSEITIDGDNSLRNRSNSTLSSCLKQLGCEISSDGFPCTVKGPINPKDIEIDASESSQPISALILCSSDFKSAMNLTIIGQEVSRGYLQLTCKIAEKWGLKQNIVDNKIELSGWEIITPKTVKIPSEMSLYPMAILLDNLHQNLQVEIEEQDIDELLFNTLELLEDPDINMINLRDASDIITPAAALMAISSGGDIIGAAHSKGKETNRILRTC... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
EC: 2.5.1.19
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Length: 400
Sequence Mass (Da): 43910... |
A0A6I2XT56 | MTAATLTAPQSAPARDLAGLPDRLSPPMPSHGIRGWIGPLVVMAIGAVLRIWNLGQPHAIAFDETYYVKDALSLLRFGVERDMVEGANETLLASDGNWRTIDIFKDAPEYVVHPPLGKWTIAAGEYFFGATPFGWRIAVSILGVIAILMTARILRRMTRSDLIGTLAGLLLAVEGIHLVMSRTGLLDMVLGFWVLAAFGLLVLDRDHTRARLARLVRDEGLDPLATPYGPRFGLRPYRWAALVALGLACSVKWSGLWFVAFFVIMSLVW | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Location: Membrane
Sequence Length: 269
Sequence Mass (Da): 29564
Location Topology: Multi... |
A0A538L6R6 | MLRRLPSAGERVLQGPGENAGVLDLGDGLAVAFKVESHNHPSAVEPFQGAATGVGGILRDIVAMGARPIALLDGLWFGSDGHDFDRAVAGIGHYGNCVGVPNVGGETVWHEAYRGNCLVNAMCVGLLDAQRLQTAKAHGPGNVVILFGATTGRDGIGGASVLASQELGEDDADKRPSVQVGDPFTGKKLIEVSVELVESGLVESLQDCGAAGLASALSEMAHDGAGIDVHLDRVPLREEGMEPWEIMISESQERMVAVVRPQMLDAVCALCAKWELESADIGSVSDTGVLRAVYNDDVVGEIPAALLTDECPRYEVEQRK... | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent ... |
A0A6L5FUK0 | MMMGDLGAEGPEWRERAACLRHPAVLFFGMDDAEAPGDRREREERAKLVCRECIVRLECLSHALEAREPYGIWGGLNEVERKARLRAMAKAART | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
A0A538ADM7 | PLLFQFPVFIALYLVLRHFSKHPPGGKLAVHRGDFSWFGHHFVPDITQHANAHWSGYLLLVIYVGSQLASTYFMSTTMDRTQRTLMMILPVAFVPVLVNFPTGLVVYWVTSTG | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
H6YW16 | SLSLLIRAELGNPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNXMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRINGLSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A0F2IXK2 | MREALIHRKTAETDITVDINLDGEANYKIDTSAPFLDHMLSLFAKHSMFDLKINAIGDTEIDYHHLIEDTGIVFGLALKEALGNKEGIARYGASIVPMDEALAEVILDLSGRPFLVYRVEKTEGFFIKDLPVSLFEDFFQALTNHSMMSLHIIVRYGRDLHHIYEAIFKAFARALSIAVTKNDRIKGVLSTKGTL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
EC: 4.2.1.19
Subcellular Location: Cytoplasm
Sequence Length: 195
Sequence Ma... |
A0A3A5VX39 | MLWPERRLLTSLMSRHTHLRFMPEATARQGGHITLLFTVESEQRLPRDQGSCGAGFTVHHGVEAAGTLTLVRQQPSAQSAGVEPDQRITDPVAQRADITVTDRHGSAINDDRIYRSYIESCRFATLLRPHEHLTLQVRLDCPPSQGFGMSAAGLMALGGLLLKLTGRGSRRQYLKIAHQVERQHSGGLGDVLGASVGGVELRTHPGAPGWPGQVESFGAETPVLLVWESTQQRHTSSYIDDAGWKSAITKAGHDCMKRLTQIPWDAKAWPRLIEESATFAEASGMMEEDGRSSLLTTVREAMKKTDLESLAVPCLCMLGT... | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Phosphorylates (R)-pantoate to form (R)-4-phosphopantoate in the CoA biosynthesis pathway.
EC: 2.7.1.169
Catalytic Activity: (R)-pantoate + ATP = (R)-4-phosphopantoate + ADP + H(+)
Sequence Length: 364
Sequence Mass (Da): 39855
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A0A5N4A8D0 | MKRITRNSTKENPGRATTSSEAVETGTKPNLSQFKLEPKRNLHSKRTHVPVEYEEPTNPKKPSKLIEKTFASSAPKDWEKAFRNLREMRKDYDAPVDTMGCDRCAEDGAPPEDQRLQSLISLMLSSQTKDQINHATMLKLREYGCNLTGMLEISEEKLGEIIRPVNFWKTKTKNIKRAVEMIRDEFNSDIPKTVEGLCRLPGVGPKMAHLCMKTAWGEISGIGVDTHVHRITNRLGWVKTKTPEDTRKALEAWLPRELWNDINLLMVGFGQQLCQPVKPQCHNCLNSDLCPTGMKELKSQKGKGK | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Function: Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base exc... |
A0A2E9XF65 | MSIFHAVFLGIIQGLSEFFPISSSGHLELLPRVLGWNDFNSDNRLENTFDVALHVGTLAGAITFLWADVKRYGMALLRASARKAKWTQDGKIGLCLLLSAAPAALCALAIEPVLLVLAESLSLIAILLILFGFFMGLADWKRTQERQRGDASPSHIAIFALAQAVALVPGVSRSGVILTVARILKFERTAAARLAFLMALPVIFGAGLYRGTDIALTGIPDDFLLPLVAGMVSAGVTGWIAVWVVFRLLRFGSLMPFVIYRVVLGLSILLSLAFGFQA | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 278
Sequence... |
G5JM02 | MDDKPNNDQQSNNGNDEMELFRRNKSKKRRQRKRQLSSEGDSHSVASRDVEEKFDEDLYLINKDFKQHESNEAQEDSSEDIKSSDLNHQQGVSNESDDIAEELQDNFDEHQTNSSHLTDVKNNKDKKQSKVTHITPLTLEEKRKIRRRRQRRIQYSIITLLILLIAIILIYMFSPLSKISHVNISGNQHVSTSQVNKILNVDSNSRMYTYSKRKAIENLKDNPLIKDAEISKKLPNTLNVTIHENSIVALVKVKGKYVPLLESGKTLKTTDDVKINDVPIIDGFKGDKEDDIIKALSEMSQTTRQYIAEVTYAPNKNKQN... | Function: Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
Subcellular Location: Cell membrane
Sequence Length: 421
Sequence Mass (Da): 47993
Location Topology: Single-pass type II membrane protein
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A0A7N1A2Z6 | MALQWMILGYVVAAEAVVALLLTLPSPTVVKSRIISLVSLILQPAMSIVPFAGFQLLDLYWKKEHRLMCTAEVCTAAERDRYEKAVSPSFRLWFGYVRD | Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 99
Sequence Mass (Da): 11204
Location Topology: Multi-pass membrane protein
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A0A3N5LZD4 | MAVAEDAEPARRAAAWAGIPWDAGTEAALSRYAEWLRSEAIPAGGLGPAEADRIWSRHIADSLLFAGCWRHPQPPADLMDIGSGVGLPGIPLAVVWPACSVTLLDRSQRRATLARRAVHILGLGNVEVVVGEAHGHARKHSLVVSRATLAPEEALALGRSLCRPGGVVIVGLTHGGDAAEPVLAGVETVVVPEAVLDSPARLLRMAIDGA | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 210
Sequence Mass (Da): 21857
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A0A2E2WXD4 | MATGVVPVAELRRFLGDAWLVAARDLRIEARSRVVVDQVVPFALLVLVLFGFALDADHRTLRTFAPGLFWVAVLLSALLAVHRSASVDQSDGTLDALRMSGLPPSSLFLGKAAAVFVQLVLLEAVLVGGLLVLYGVEVVDPVLLVVAGLLAGVAVAAAGTLYGALASGLGVRETLLPILLLPVLAPVLIGATRAFDDALGAAAVDGWAWTGLLAVAALVVTVVGALAHGVLIED | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 234
Sequence Mass (Da): 24049
Location Topology: Multi-pass membrane protein
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A0A537WQF3 | METLDRIGVLARFLPEWEPVRCRPQRDPYHLNSVDVHLLHTLAGMSRLLDGGDESDPLVAEAAAATEDRDALLLGALLHDIGKTGGGNHVPVGVEQATAALERMRLRARTRDLALFLVAEHLLLSDTATRRDLEDDDLVLDVAARVGDPERLAGLYLLTVADAKATGPLAWTPWRATLVRELVAKVQRVLERGELGPRAAERLEALGEGLRDLLPNEGPAEVDRFLERMPRGYLLATPAEQAAQDFPLLRPPVGAHEVRTLSGPGARPGTYALTVVASDRPGLLSWIAGSLSLAGLSILTAQVFTTDDGVAMDVFEVEGA... | Function: Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher ... |
A0A168GPW9 | MIAPIAGKFRKQVIKDITISLTLGAAGGAAWWNLYHIPNVQRRDAYYAKLEASKQ | Pathway: Energy metabolism; oxidative phosphorylation.
Subcellular Location: Membrane
Sequence Length: 55
Sequence Mass (Da): 6145
Location Topology: Single-pass membrane protein
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A0A7C3T377 | MLSVEEARKRILDSVVPLEAVEVPLLDSLGLALAEVVVARHDIPPFDNSAMDGYALRSEDVKGASEENPVTLEVLGDLPAGRAPGDAVGRGQAVRIMTGAPLPPGADAVVPVESTRPGEGTVLVLEAVKPGAHVRLAGEDVKAGEEVMSPGTAIGPAELGMLASLGYARVRCVRRAVVGILSTGDELVGVEEDLAPGKIR | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 200
Sequence Mass (Da):... |
S9ZRG7 | MSLEHGVEPGDMTTPASAVETPDSGTEPGRILRRLVVPTLTVLLLALAWFAVRRLAADVSYESLQSAIASIPVATLIAALALTALSFAALTVYDLGALAFVGRQLPLPIVALTSFSAYAVGNTVGFGALTAGAIRYRFYTSQGIEPEEIGGIVAFVTVSFGLGLAGVAGLGMLAAAGEFAHLPLPASSIKWMGAALVASLAALVLAAGEGRDVRLLGRAWRLPSRHLMLRQFLATAVDVSASAAVLWVLLPANSVDLPAVIALYAVAVGLGVLSHVPAGLGVFETVIVAGLGEQVGIDAVLGALVLYRVIYHLVPLVLAV... | Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Membrane
Sequence Length: 873
Sequence Mass (Da): 92539
Location Topology: Multi-pass membrane protein
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A0A538FSH8 | MVVFSRSVLGAVLLWSGAAKVVARSWAGTAAEFGVPRALRPAIPLSELVLGASLITGLARPWTALATTAMLAAFSAAIALHLARGQAVPCGCFGDVSSRPVGPPDLVRNASFICLAAVAAGPPRAAAVFAFGAAALGGGVWIGLEVVTASRRHRPPSPGGHPHRRG | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 166
Sequence Mass (Da): 16775
Location Topology: Multi-pass membrane protein
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A0A4P5R5S6 | MSITRLTDSKNISANEVLVVGFAQTDNGPEFLEPAISFEAASKNEIIEAIKLTDFSGKKSELAYLTIKSGVLCVGLGKVTKTQPLEMETLRRASGVAARSLVGKSSALFALPTNTTVAAHAVTIGVELGAYSFTEFKTKNEKTSETLKQASILVHDQFVNKASFQEAQIIAESIKNVRNLVNTPPSHMYPETFASYVKKTFKKNSKLTVEILEEKALKKQGFGALIGVGQGSINPPRFIRLAYKSRGADFHLALVGKGITFDTGGISLKPPSSMHTMKCDMAGAATVVETLRAIMDLDLKINVTAYAALAENMPSASAQR... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xa... |
A0A7X8YWR7 | MRSLLSIAGLDPSSGAGLTKDLEVFAGLGFHGLHACTALVIQGPQGVQRVVPCGVEEFTLTLTLLEEQSEIAGIKLGVLPGEGQVEQVARFLTDVRGVPVVLDPVIRAKNGTTLTSSAALSRLVSEILPLGPVITPNLSEAGVLSGRSVRDLPAMRESARALHARGARSVVVTGGHLAGDPVDLLFDGRTFTEYRRERLPTEVHGTGCVFSALLLGYLVWGYPVAEAFWAAETRMTELLIASYQLGKGGYHYTSMGVLSANRAERSQVLEALRDAARELAGLAPVELVPAVQMNLGFALPTAREVGEVAAFPGRIGAHAG... | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
A5D4M0 | MKAGCQVKICGITSIEDARLAAGAGADFIGVVVEIGFSPRSLTVEEAKAVFASAPVPAVALVFEMKPERIEHMVLKLKPFAVQFISPEGPDLAGRLKRLQPRLNIWQSLHLPAKAGSSGVSFDEREVLRRVRQCREAGVDAVLFDTAAVLNGVTRLGGTGQTSNWEVAGRLVKASPLPAFLAGGINPANVRQAVEKVRPYGIDLCSGVEKSPGKKCPVKLKALMESLRQAGGTGNV | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 236
Sequence Mass (Da): 25008
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A0A2G8KU38 | MWDWIHGNRTVGQRWVMVTEESPYYSPGIQPPEKYSAVTYDWVGSYSQDADFHQPYGYYKPFREGHPPVRLDREKILNKTGLTIWLGSHCKTLQWDRLRFVEDLGKFMSLKKMGRCGDEIIPWNREEVLKQTLSPFRFYLSLENSCCKHYITEKFWRTLQFGLVPIVVGAPLEDYEKLAPPNSFIHPDQFDSMVAMATHILEVATDKERYLEYFQWKTKGEIVVYTQEEYYVHPLTNSSNCDIVQKYLNSKPSDHSKLDYFGPKWFGSCTECSTKKWLNDKYTHRKNYSILPGKLWD | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 297
Sequence Mass (Da): 35151
Location Topology: Single-pass type II membrane protein
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A0A6I2YLL1 | MSSDAPLYDLPAGYQHIYSGKVRDLYSTPEDRLLFVASDRISAYDWVLPTTIPDKGRILTQLSLWWFKQLEGVVPNHLRSTSVPAAVKGRAMICDRLEMLPIECVVRGYLTGSGLTTYLESRSICGLGLPPGLKDGS | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(... |
A0A6L6D1B1 | MRRAKIVATLGPASSTYDQIRAIVEAGVDVARMNLSHGSHSVHEEIYNTVRKVAKDLQKPIGIFVDLQGPKIRLEKFESGPHLLEKGDVFKITINDVVGTKEICGTTFKGLCGDVKVGDQLLIDDGKVALRATEVTADTVVTVVEVPGYVSNNKGINLPGVAVNVPALSEKDEDDLRWAIGIGADMIALSFVRNASDIIRVHEIMD | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
EC: 2.7.1.40
Catalytic Activity: ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate
Sequence Length: 206
Sequence Mass (Da): 22273
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A0A2G8JZW5 | KLTDERDRRKLHDNQEGEVKGLGDKLPPEKSPVLPVEDLPQNRNPKAVIPVLVIACNRPSAIKRSLETLLKNRPSKDQFPIVVSQDCGHAETATVIEQFGDQISFIKQPNLGKIQDIPSNLKKFEGYYKISRHYKWALVRCLMS | Cofactor: The cofactor is mostly bound to the substrate.
Pathway: Protein modification; protein glycosylation.
Function: Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
EC: 2.4.1.101
Subcellular Location: Golgi apparatus membrane
Catalytic... |
S7QEJ9 | MLSLRRDALLCRRVVFLRDARINTRRCLADAAGSSATSSSSSATPPVSRPEEEKKAAEAWLFADSVFPVRLATWDLRHYIGIFREETILAKLKHILQGVNAHGFELVSLEPHFKDGGVFIHFRYNASEGSSTLEDIEKHVRDQAAKQGGVPSWSGVSRGSIWLVKGHPWREDMHRFASPMLTVAFEGPDVPEESLYRLLRPFGRMQDLRNPSPVPAGSLRFSTIFYNQVRSATIAKNVIHGLAIPSTPSGGRTILRLGYREPLQAHVIRDWIFSHPRIVLPIVVFFLGTLTYTVFDPIRAFMIQGKVQDWFDYKQSRIYR... | Function: Plays a role in maintaining the mitochondrial genome and in controlling the mtDNA escape. Involved in the regulation of mtDNA nucleotide structure and number. May have a dispensable role in early maturation of pre-rRNA.
Subcellular Location: Membrane
Sequence Length: 890
Sequence Mass (Da): 99771
Location Top... |
A0A7V8WKM7 | MVRAAYWLLASFVGVGAILVLLKAEFVGLVLMLMMAGEMTIMAFVMVMFMMNPAGLNPMLMVHQHKTAIAAGVTSFLVLAGAALLTDFPNAPATQTSRATEELGTELLGESMLVFETAGAALLGTMVGAVAVASRRGRYGDAEEGSIEPPLQPDEEWAQASAHRTEEDEHEPSVHGGHS | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A2G8KMU5 | MADFGEFENTNAENAAPAAEEVDPAAEFLAREQDQLAGIEDDNLGGDSTPADTENDFLGGEDKPTGDLVDEFGGAGDPIQGDDFPQTNGPSDSYSAISSIDRSENEPEKIKIWREEQVKMLDKKDEESQNLQEAWRKQAQKELDDWYNREADQLTKSKASNRAAEEAFIKERDEETPGQEWNGSRGSAISTQRITKIQKT | Function: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 200
Sequence Mass (Da): 22206
Location Topology: Peripheral membrane protein
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A0A2G8KAA0 | MYTDAHRLVVQTFLARGVMNTKDVADVIQKACERCGVTNSGQNVDNFIHQINTKLRINTMEIKKKREEETGEEVYALVQTAETEVGKLATDYHPKELELFKEIVGKIVTSEEGEASSTECLNLADSLDRRISKDDAQTAIKKFVEERWLYMDEEGQISLAARGILELEMFMKESYSDFISICYLCQDLVVKGQLCDACGKVKLHYFCAQRLFQTRPNPKCPSCEKAWRHQIPRLNGDVNDKRQNEGRDTRDTQVDPTQPSTSGRRKRVAPR | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 271
Sequence Mass (Da): 30973
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A0A7W0WBK0 | MLKIILLAIVNAVAVWGGTVLAADEKWVALGVLAAATLALDAIYLSPRRAIPLKFLIPGTVFLIAFQIVPIVYNVNVGFTNWSTGHILVKSEAIEGIKRNSLGQPADGTAYSMAPARDADGELVLLLVDEADGKSYVGTTEELRPLDEGALKLGEFGTIESASGYQIVRGGDLLALDKELAGFTVPTASGAIRAEGTETALELAPT | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 206
Sequence Mass (Da): 21591
Location Topology: Multi-pass membrane protein
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A0A3G1NN39 | AFPRMNNMSFWLLPPSLTLLLMSSMVETGAGTGWTVYPPLSSNITHSGASVDLAIFSLHLAGISSILGAVNFITTVINMRSVSLTLDRVPLFVWSVVITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPSGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A5C7PFT9 | MVGLVSQVAGSFSTPATQDPSSAMMRRAFHDLGYPVEYLNLDISALRLGDAVTGARAMGWMGFLVGEPHKVSVVAHLDGLAESAALIGSATVAARRGDALVGENTEGWALVEGVEESMDLEHSRVVILGAGGAARAAAVEFARAGASHITIVNRRPARARQLAANLAGVEGLTVSVLGVEGRLRLPSTTDVLVNATSAGADYDPQPLMNLDYETLRPQMVVADYVPVLGGTALLKEAAALGAQTLDGIEIRARQGALAVRMWTNADADWTAMRAELEDSLARLA | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 284
Sequence Mass (Da): 29697
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A0A354SAD9 | MTKAPIAVALDAPDLAVLRAWSRAVAPVVSTLKVGLEVFCRDGAAAVHAARLGASEVGSADVQIFLDLKLHDIPATVA | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 78
Sequence Mass (Da): 8018
|
A0A1C9K6P6 | ILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPXXLTLLLISSMVENGAGTGWTVYPPLSSNIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITFDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTD | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A836X865 | MVKEKIEAILADVASALPEDLQFFRKDIEKNLRATLNATFSKMELVTREEFDIQTASLQRTRTQLDALQEKLSKLEEQLDKTKNYTDT | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for efficient ubiquinone (coenzyme Q) biosynthesis. UbiK is probably an accessory factor of Ubi enzymes and facilitates ubiquinone biosynthesis by acting as an assembly factor, a targeting factor, or both.
Subcellular Location: Cytoplasm
Sequen... |
A0A2E5EUD2 | MSGPHLQVSETFFSQQGEGVSMGTPSLFCRLQGCNLSCGGQHTVRTGDLDSGATWRCDTIEIWTQGQRYSFDQLIDDWSQKGWLRALQDGAHLIITGGEPLLQHAQLAPFLSHLRRHCTPVYVEVETNGTLAPSASLIEQVQQWNVSPKLANSGMALQKRRVESAIQVFCDLSPAAWFKMVVSDPSDLQEIESAFISPFQVPKSQVLLMPAASDPVTLEQVLTWLVPLADAKGYRWSHRQQIAQNFR | Cofactor: Binds 1 S-adenosyl-L-methionine per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
Function: Catalyzes the complex heterocyclic radical-mediated conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-deazaguanine (CDG), a step common to the biosynthetic pathways of a... |
S7R9N7 | MFSFLKGNQRYEGKPTVLEACDLASIVKYMKSDKCKRVFIMNGAGISTSSGIPDFRSPDTGLYANLARLNLPYPEAVFEINFFRRNPKPFYMLAKELYPGNFRPTPAHSFIKVLDNHKKLVKCFTQNIDTLERRAGVPDDKLVEAHGSYASQRCIDCKRPYDAQKLKDKLYKEEVARCEKCGGLVKPDIVFFGESLPPLFHRSIPLLQSADLLIVMGTSLVVHPFASLVDLVPEDCPRLLINLEHVGDFGSRPNDVVYLGKCDDGVRELCRLLGWDKELEREWEKTKYTLERLQEDVAKTEVKEKEAEEKVSQARTDAEK... | Cofactor: Binds 1 zinc ion per subunit.
EC: 2.3.1.286
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Length: 406
Sequence Mass (Da): 46046
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A0A851YE37 | RNHFARVRLRALSAEDIEAIRQKKYVASKLRFIPKENGLRPIVKVSSVVDAPAFSKESREKKVQQYNTELKNLFSVLNYERTINSSFIGSSVFGKDDIYRTWKNFVTEVLETYDEIPHFYYVKADVSRAYDTIPHNKLVEVVSRILKPQKKTSYCIRRYAMVMITASGKARKSYRRSV | Function: Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Catalytic Activity:... |
Q0A613 | MKERLLAHWQGLEPRERRILLAGALVLAVLLPWGGIWLPLSDRAETLRGEVAEARAQQAWMAAAAERVRQAGGATAVPGEGRADSLLGRVDRSAGDYGLGERLERLQPDGDQRVRVWLERADFDQMLYWLDALAETGVRVHALSLEPLDAPGRVNARLTLESES | Function: Inner membrane component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 164
Sequence Mass (Da): 18112
Location Topology: Single-pass membrane protei... |
A0A328SM28 | MAGLSVGILLKYVDLKIEQKSYVTFIAVILVLLAVISPLYADHLTSSQSVGSTNDDMYNTLTWIKANTPENSVLASWWDFGHLFTAVAHRQVVFDGGSQNNMRAYWIGRSLATSNEDLSAGILRMLANSGEDASNVLDSYTGNTTKTVTILNEILPMDRTQANTALTGTYGLDQQQANSVLDKTHPADTKPVYLILSSDMLSKAAWWSYFGTWNFENESSTHYSYYASQSSVENIDGKDFTLGTDNGVVGVSAASNETNGTTMNFAYLDQSKLNKTIDMFTSEDKKRLANELSEGTGNELLKPHKLIMVDNNQLSERIVN... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A537WHD0 | MPLPRPSRTLTRTLLGAGALIALVVLAAACAPHATQDTLKPAGPYAQKIDNLFRPVFWIAVAVFVVVEGMLVYLAVRYRHRKGRREIPPQVHGNQRLEIAWTIVPAILLVGVAIPTVSGIYALAAKPSGRVLEVNVIGHQWWWEFDYPGLDVTTANVLHIPVGEPVYASLCAAGLGYHDQVAPNSCQEQGGYGNVGDDVIHSFWVPRLAGKQDVVPGRTNHLVLQADQPGTYTGQCAEFCGLSHAYMRLEVVAQTPADFDAWVRQQQADAVTPPQGSLAATGLNEFLNGACIGCHAIQGPKVNDQPLTQPGGPNLTHLM | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(... |
A0A538IIC6 | MDDRAAGARARRVPRPHERPQPQLQRRTARAWRRCRARSRGACHGIPTRHLPRRLRPAGPAGGGARRAPPHVRRTDRGLAVGEPRNVDAARRVRAPDRSRTPNRLRLARARGGRRNRARAPSPARATETGGSRVSSNVFELPAHDAEAAREVTAADWARLERNAAEILAALGLDLDTPGTRETPRRFIQALFDATAGYDGDPKLRTLFPSERPEGVEGRHAQIVEGPIGFYALCEHHALPFHGRAYVGYVAGDEILGISKLTRLVRLYARRFTVQERLAEEIADGLFELVGPRGVAVKLEAAHLCTAMRGVEEEGSVTVT... | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 342
Sequence Mass (Da): 37895
|
B5EHT0 | MKIETSRLNPIQHATAALVIGCFEDAKDDLFAACDKELDGYLTSLFESREFTGKSGSSLLLHTMGKLPAQRLLLVGLGKKGDVKGELLRRAAGTAVGALQGVRVASFSSALHLCCQLPKALEAVVAGTLLGSYRFDLYKTKDKEERFQFDSMTLLLGEEKDTGDTRLRIEQAEQLCRGVCLARDLVSHPGNVVTPGYLAQEAQELATRHALECKVYEQDELESLGMNALLGVGKGAAEPPRLIVVRYRGEGAKGRPVVLVGKGITFDSGGISIKPGPGMEEMKTDMAGAAAVLGTLEAAALLQLPVDLVGVIPTAENMPD... | Cofactor: Binds 2 manganese ions per subunit.
Function: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
EC: 3.4.11.1
Catalytic Activity: Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xa... |
A0A3D9KVW4 | MTMAINKLFFFFFAAMTVLPVIYILFTGNIVRSAFALVVSLLGVAALYVLLQAEVMAVVQLLIYAGGIIVLLLFGIMLTRRLSEEGVFAGHRGVVIGALMALMLFGMLVRLILGSGLEFETAAPVTDQVAHVGIAFLTDHIVAFELVAYLLLVALVGAAFLAKKSDKA | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A8I1S2I9 | MVPETADTAQPAAASSPSAPLAGWRVLVARPAGRGDDLVTLVRDAGGSPLHVPLIATTPVTSAPLRAALDALADGGFSWVALTSAAAVSALQAAARAADRPFRIAPSTRIAAVGTATAAALRGAGLPVHLLPGTAGSAATLAASWPMEPPGLRVLLPCSDRATPTLADALRATGHDVTTVVVYRTEILPVPEPLARDLADGRIDVVLLTSPSTVQALAGTVIAPGTRLVAIGQPTAHAARAAGRVLAAVAVEPSARGMVDALIGLRGAEADMHHATADMRGAATTSTTGMKEL | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A7J4DD30 | MAQPHYQNQFKAVLGAGAWPGTLNIELYGDNLADYRSLRVLSGLDEGERIEGAEPLRIRGFERDGRSFGGATAFKAGITRGGDEWIECAVLIPDLTRHTETAEVISPAFLREALPCEDGDEAVIRLS | Pathway: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (CTP route): step 1/1.
EC: 2.7.1.161
Catalytic Activity: CTP + riboflavin = CDP + FMN + H(+)
Sequence Length: 127
Sequence Mass (Da): 13876
|
A0A538EJA2 | SVSQALFSTVLHARVAHKILDAEAGLERSGRLSQALGTIEQLAKRAQSEMRRFIFEWGPEGIGDGLVPALSRHVASLAEDPIDVRVEGPSEPLPLTRTAETQLFGIGREALANVAKHAHAETACVRVHATTKRVVLEVADDGCGFDPDASRAGHFGLQSMRSRADELGADLHIISAPGRGTVVRVELPAVNGRNGG | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and tr... |
A0A662DF52 | MGSGSVQGRTGSVVARVLNVPNSISFLRLALIPVFVWLVFGAQEHGWAGVLLGVIGATDWIDGFLARKLDQVTEVGKFLDPLADRIAVVVAVVAGLVTGVLPAWFAIALVVREVVIGIGAIHGWRNGVTKLDVRLLGKAATLALYVSVTLFYLGDGFSAAWATWIAYLFGIPGLVMYYWVAVQYLGDMRTAIADRKKGRGSS | Pathway: Lipid metabolism; phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 202
Sequence Mass (Da): 21603
Location Topology: Multi-pass membrane protein
|
A0A4Q1T9J2 | MLITRPLIKCCGFQDVEDIVKLESVDIDFVGFILAPSKRRVPLEKLPTLVEAVPAGKKKVGVFVNPSLTEIRDVMSIAKLDVVQLHGQETPSLCKEIKGEFGVEIIKVVHIDSTESMPLPLGEYGDYIDFLLLDTFDKKMAGGTGKTFRWEVIPAYQQWCVDHHVKLLVAGGITPENVGQLISDWPLGGVDVASGIETEGKKALVKMLQLVERVKEYGGRA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 221
Sequence Mass (Da): 24343
|
A0A6I2WLM9 | MPAKERPDRNLAMELVRVTESAALAAASWVGRGDKIGADGAAVDAMRNVLDTVSMDGIVVIGEGEKDEAPMLYNGERVGNGSKPLADVAVDPIDGTTLTAMGRGNALSVIAVAERGAMFNPGPCVYMEKIAVGPEAANAIDLNVSPTKNLKEVA | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Length: 154
Sequence Mass (Da): 15921
|
A0A1L8CNZ3 | MWASLFTTPFGLTEPLFVPEYWMPPSLLDLAETTGFDIESLIFCFGIGGIASVAYNLITRQVPQEVPHAEKSSPLHKHHYKAIAAPFVAFPFLYLLPWNPIYPSIASLFIGAVANVLCRPDLKRKSWIGGLLFLIYYAVFLAGLEWSAPGYIDRVWNLAALSGWSLGFMPVEELLFAIGFGMYWSGVYEHFTWRK | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 195
Sequence Mass (Da): 22031
Location Topology: Multi-pass membrane protein
|
A0A7W1N8S6 | AMAGAMTATKGKFPPGDAHTERDADQPLTKTDRAAAYPTPDGKLTFDKLSSVFASGNRTRDDQPNHIRVQTQVPRELAEMWVRLCPAQVYEVGEADGDGTVEVKLAPSNCVQCGAITAKGGRLTPPEGGSGPEYTLT | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 137
Sequence Mass (Da): 14530
|
A0A538AC19 | MILATLLGSPLTPLEDVLRHVLEWLHGTAGLPWAWSIVALTVIVRLLMVPLAVKQIHSMQAMQAHMPEMKAIQ | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispa... |
A0A350MUM0 | MRSVAIVPHLEKKEAVSLMRELMEWFFERHVEIRLPAEDASVLGHPELGFPEERVTEEVDFIVVLGGDGTILRTVRLLKGRDVPILGVNLGRFGFLTEVEVSQLHFALSRILDGKFCLEKRMMLECEVFSGNEVVSRQLALNEVVLGGGGRQRLLEFDVYINGEPFSRYASDGLIIATPTGSTAYSLSAGGPLVSPSTRLIILVPVCPHTLFGRSLVLTETDEIRVSCPGSKNSAVMVSVDGVILFEKPFDFVRVSASSHTTNLIKVDGRNFYSLLKEKLRIWDSF | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A7W1KV70 | SEAWSPEGIAQQAIAALRGELGDDAVVIGDLCLDEYTDHGHCGVLDERHEVDNDATLERYRRVALVQAEAGADMVGPSGMMDGQVAAIRSALDDAGRGDVAIMAYAAKFASAFYGPFREAAEGAPRFGDRAGYQQDPANGDEAMREIFADIDEGADIVMVKPATPYLDIVHRAKVETGFPVAAYEVSGEYAMLKTAAANGWIDERRAVLETLTSIRRAGADMILTYHAKDAAGWLREEH | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 239
Sequence Mass (Da): 25736
|
A0A3N5JZV7 | MRAVARPLSVTGMSIAADNAGVVAARSLTCSISSLSRADVLYAGGKGANLGELTAAGMPVPDGFVVGAPTYAQFVDETGLRERIASRLADLDVDDTAALEAAAREIRAMVETEAVPDQIRSAIADA | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 126
Sequence Mass (Da): 12892
|
A0A353FV84 | MLNNPAARKVAAVIIDPPAKLLVRMKVSPDAVTLTGTIGGSLSMLILIPQGEFIWAFVLGVFFGLSDLLDGTMARMTGKSGPWGNFLDATLDRITDGAVFAALVLWGMNQDNYWIVGGALLALVSGQVVSYAKARAEAVGATANVGIAERAERLILTGIAVLLTGFGVPYVLAIALWIIGIAGVVTVFQRMIEVRRQLRSAT | Cofactor: Contains a di-nuclear catalytic Mg(2+) center.
Pathway: Lipid metabolism.
Function: Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphat... |
S7RUA3 | MDYAKGKTGIAGKGKKDAGDHKVRVTCPSSHTGAHDLFLKFWSTQPVPQLGDEVPAEDGPIEPSRPGEEVRQEPYPLPKEFQWSIVDLNDPNQLKEVYELLSLNYVEDKDATFRFQYTAEFLQWALQPPGYHKEWHVGVRVASNKKLVGFISGVPITLRIRSNIVKASEINYLCVHKKLRSKRLTPVLIKEVTRQCHLKGIFQAIYTVGMLLPTPVSTCRYYHRSLNIPKLVDTKFTYVPRNQTLARMIRLQKVPSSTHLALREMTESDIEQVADLYDRYMKRFDMVPLMTVEEIRHQFLSGLGRGDMVKGRREGQVIWS... | Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins.
EC: 2.3.1.97
Catalytic Activity: N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]
Sequence Length: 458
Sequence Mass (Da): 52039
|
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