ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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A0A0S8ASD6 | MIDWFTVSAQIINFLILVFLLKRFLYGPIIRAMDKREEAIAGRLNEAGQKREQAQKEIERYIEKNEDLDSQRADMLAAAKEAAEQQKKELIDMARKEIDDIKARWREAVSQEKEAFLGNLRNRMAHELYALARKVCSDLADMSLEEHMTAMFLKKMSALEQEELDTIKTKLKDSGEGITVSTSFALPEQKLEAISQTVRRITGLDVPPKFVQSKDILCGIELRAHGYTLGWNLDAYLTSLEKEFGKVIGS | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 250
Sequence Mass (Da): 28544
Location Topology: Single-pass membrane protein
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A0A2E6H0G4 | MTKFILLDIEGTTSSISFVHEKLFPYSFERMEEFIKKNKEVPEVQKILSELSAEQGCGLSLSAAAELFQTWIKEDKKHGLLKQIQGLIWKGGFESGELKGHVYPEVPQNLKSWKEAGIKLGIYSSGSVEAQKLLFKYSEAGDLTSLLSSHFDTKIGHKREVESYENIVLELGVPAEQVLFLSDITEELDAAKKAGMKVTQLFRDEVPGNPAHPYVKNFDELEV | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
EC: 3.1.3.77
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Length: 223
Sequence Mass (Da): 25053
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A0A336MA29 | MIRRFFATFFEYQGNSFEIWPGNTSTTVGTNLFNKSSTLESLSWLYTCAPCFPVNADKISIIQVPSVFYETLVAKSSKAKNRIKLASLYLGTGQLEHNLVTAIHDNLKSNKNLTVDILLDFTRGTRGDINSKTKVLPLLNESENCVLSLYHTPVLRGLTKRLAPPRWNELLGLQHMKIYLFDDTVILSGANLSNDYFTNRQDRYIMIEDKRVADFYSNFLSKVQEFSLKVDKNGNESLHEKWKLSPYESSHKEFSVAAKKLITDYFNDTWEEQNRINYNGQSADTWIFPTIEMGQIGIHHDSHIVKRILASALPQSSLKMATGYFNLTDNYMKALTNECGAECAILMAHPNANGFQGANGPAGSIPKAYTLIAKTYYDTVIAAKQTNRINLFEYERNGWTYHAKGLWYYLPQQRLPSLTVIGSSNFGERSVNRDLEAQVCLVTSSQKLQQQLQTECDHLYSYGTIAQRELAERPIPRWVKAASVIQMFLKGKVLLILSFISSLLIVITETRHNVSRIKRIVNGKRVSQDQAPYIASLQILESSDFVHFCTGTYLGQGFVLTASHCLKYVKMCEIYIQLGQIRLSQGNNKSRYGVENSCRKRYDIYTYNNDIALVKLNMSHNDPLYNMEYAQIPPNYQIYVVDCKIYGFGAVRYGEKHSEYLLTGDVKPIDRNRCTSILGNVITPDYHMGMFCASGDRGVDACSGDSGGGLFCTSPENKNVTLLIGLVSYGMGCGSEAGIRSTDNKADPAKKNKALHETRLPTYRNIKISDR | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
Function: Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP + H(+)
EC: 2.7.8.5
Subcellular Location: Mitochondrion
Sequence Length: 771
Sequence Mass (Da): 87062
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A0A2D4K408 | GINTESEEQKPKRLHPQKSMDDGNLQKCFPKLPVQQASAVYAGKASGCNSTGMKGPNALPLSFKEATLAKKFALKTRSQITKRKRMSLIKEKKAAQTLSAILFAFIITWTPYNIIVLVNTFCNCIPKTFWNLGYWLCYINSTVNPMCYALCNKNFRTTFKMLLLCQCDKRKRRRQQYQQRSSVIFHKRIPRETS | Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Subcellular Location: Cell membrane
Sequence Length: 194
Sequence Mass (Da): 22325
Location Topology: Multi-pass membrane protein
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A0A7X2YY14 | MSRSNDSERNVVDDPRMLSANNNNSVSSTDSVNNPIITNSTNSPGLPDASSIKDTGKDWPLAAAFQFLSRFPVPVEVNFTPGVLRRSAKYYPLVGFAIGAALGLAAVGIAWVLPPMPAAVLILALWIWLTGGLHLDGWMDAADALLSYRSRERMLEIMKDSRVGAMGVIACVLLLLLKMSLLYTLIGYGYAQVGAALLTAAIWSRWFMTYAMQAWPTARQGEGLAGNFRGLKTGSIAVSTAAALLLSAAGLTAITSLEQGNDPGSLMLLYCVAPCISWLAGTLAASRISKRLGGLTGDVYGALNEGIEAAVLLAAVICLG | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
Catalytic Activity: adenosylcob(III)inamide-GDP + alpha-ribazole 5'-phosphate = adenosylcob(III)alamin 5'-phosphate + GMP + H(+)
EC: 2.7.8.26
Subcellular Location: Cell membrane
Sequence Length: 320
Sequence Mass (Da): 33739
Location Topology: Multi-pass membrane protein
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A0A0S8AGK9 | MIKRYPIKRRMRKKFGQHFLFDKNILKKILACSNVTADDMVVEIGPGLGSLTNIIAQRAKKVIAIEFDKKLIDRLKDNVASSPNVEIIRADALKFPYESITGHFKVVANIPYYITTPLLFKLLEYKETIPTMTLLMQKEVAKRVVASPGSSDYGVLSISAQVYTKPVLKFQVSRKAFSPPPDVDSAVVHFEVSPVPRFDIQDVLLFTDIVRTAFSQRRKTIINSLRKFEGIGDALEAAGIHAKLRPENLSIEDFARLSNIMI | Function: Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Catalytic Activity: adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine
EC: 2.1.1.182
Subcellular Location: Cytoplasm
Sequence Length: 262
Sequence Mass (Da): 29537
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A0A2E5JI66 | MRAFYLNNLANAQVGQKLSIEGEGFNHIKVVRLKPSEEILLLTGQGDNYLARLEVLGKKSAIVEVLRYEHKPQLNALTLAIGLVKKDAFDLCLKMAVELGATTIIPLETRYSQRYELNYERANRLLIQALEQSNSAWLPKLLPVTAIESLSQEIVDNCEKYSNLIIMGMANSTLPAKLPELGTSVMGFIGPEGGFSEDEEKLLAKLPNASTIHLPTPILRAPTALAALGGVIFTKQRVLD | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 240
Sequence Mass (Da): 26397
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A0A0S7BYJ5 | MNPAIPEIEIDRSSGFCSGVERAIKIAEDKLLQEEPIYCLGNLVHNEEELERLSSLGMRFIRHDEINGEMKTVFIRAHGEPPETYSILRNNNASVIDATCPVVLRLQHKVKESSRQFRETGSGLVIIYGKPGHPEITGLLGQTEGNAILISKLEETGSIDYNQPLHLYAQTTAGEEEYASLCRRISENSLQLTGRNDLVTVHNTICRQMSQRAPRMRAFAQKHDVIIFVTGSESSNGRYLSGVAREVNPETHVVGSPSDVENWFAGARSIGITGATSTPLWLMDEVAGRIKAIVENNL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
EC: 1.17.7.4
Catalytic Activity: H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 298
Sequence Mass (Da): 32996
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A0A2K2HD23 | MLPRSTIPGRRRSPDSASVVTARPVLPPRCCNSGGHSSRLLLPVVPVAEEPLVLDGAAVERLRLWRARPGEILTFVDPRQTAWRGRLERDGARWRVVPFQPLKRNPAGPLRIDLFQALPQRERFELVLEKATELGAGRLVPYQSERSISLAERDARQKKSHRWPELVLRAARQCRRSELPELYTCCGWNEALDMGSRADLRLMLYEGGCSQQMGEALAVSRAESLALLIGPEGGFSDAEVAEAVRRGFQPVSLGPRLLRTETAAIAAIAVAQACLGDFR | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 279
Sequence Mass (Da): 30916
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A0A3M1KRC8 | MVLPAEVLIIGVVALLVFGPKKLPEIGSSLGKSIKGLKEELENTSSEPEKPDN | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 53
Sequence Mass (Da): 5616
Location Topology: Single-pass membrane protein
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F4KVN0 | MFFKKQCSLFLLLNVLLCATLTQAQDNTPTVGPAQGALIIVGGGKVGPDIWARFIELAGGEGANIVVIPTANEDASIATGVSVEKDLLQRLGVDNVTILHTRDRKQADDPGFVASLRNATGIWFTGGRHWRLADSYLNTLAHREFKALLTRGGVIAGTSAGATIQGSFMVRGDTKGNALMIGDHVEGLDFIHNVTIDQHLLTRNRQFDLVEVIRQRPELLGIGIDESTAIVVQKDTFEVIGNSFVAIYDAKNFSADASKTTGEAASSGPFYFLGKGQRFDLKERRVLRR | Function: Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
EC: 3.4.15.6
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin-2-N-yl)aspartate
Sequence Length: 289
Sequence Mass (Da): 31341
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B3MPF8 | MSTTIFMYAICLAVLSNLLSVSAIRCHDCNSHEDEDCATLVVNTPRAQRDEQFLKECNGKDGLVPFCRKTVIKFEVNNNRRIVRNCGWIPEKVQNACFTADNEGYKQTICTCNGDGCNGASTLLGARQVGYSLIGTVVSLTLATVLRN | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
Subcellular Location: Cell membrane
Sequence Length: 148
Sequence Mass (Da): 16257
Location Topology: Lipid-anchor
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A0A133XW22 | MAGMFITFEGIDGCGKTTQIKRLAHTLRSSGLSLVELREPGGTTISERIRELLLDVRNHDMSDECELLLYEASRAQLTQQVILPALQDGSIVLCDRFFDSTTAYQAGGRGLDEQLVSRANALGCCGVIPTRTLVFDLDPEEAYARATQTTPDRLEAAGLAFQKRVQQRFMGLAQQESDRVKLIDASGTILQVEARVKRELADIFVELADE | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 210
Sequence Mass (Da): 23179
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A0A1F9XY16 | MRGVFITGTDTGIGKTALAACLLRKYGARKDLLYWKPIQTGIPDDDDTRTVRRLSGLPDGNFLDFGIRLKKPLSPHHAAAFEKKTLKPGFLFERLRRLKLKDPVFVVEGAGGLLVPLNGRAMMADFIRRTGLPVVLAARSDLGTINHTLLTLEAARARRIPVAGVVMIGPLNPGNKASIEKYGGTKVLEEIPWLESRTLRAFSVYAERRFDSRGFLGRLF | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
EC: 6.3.3.3
Subcellular Location: Cytoplasm
Sequence Length: 220
Sequence Mass (Da): 24356
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A0A2H0WRC6 | MLNPKTIRQLSKILGSDRLKKNVSLASYTTFGIGGPAQLFYEAKTNKEITKAIKTVRKLKIPCFILGGGSNTLIADSGFPGLVTKIESQKIKVKNNTISAEAGVPLSKLVKVAQKYSLSGLECCVGIPGTVGGAVVGNAGAKDQWISQSIKSITILNKNGKIISFKKDYCRFGYRNSFFKKDPSKIILKTIFKLKKENPKIIKEKTRQFLEAKSNQPKEKSAGSIFKNPANDSAGRLIDATGLRGKKVGNAQISPQHANFIINLNKAKAGDVLALIKLAQNSVKEKFGVKLELEIKLIGF | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 300
Sequence Mass (Da): 32595
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A0A2G9M3K8 | MLLKNGKVHSVEKGGFIAADLRIKDGLIAEIKPNLLPEQYETVVDCAGKHVIPGLIDAHVHFREPGATHKEDFLSGSKAAAAGGVTTILDMPNNNPPTVFEEQLKEKRELAMKSIVNYGFYLLGCVENKDNLRQKNIAGIKVYLGSSTGNYLTDDLGVFAEILQNSRRPVVVHAENEQLIRHFNHLHGNSQLHHKMRDALCAVTSLAEAITISSYLDRPLHIAHCSTKAEMEFLQKNKTTKVTCEVCPHHLFLTEAFFIQKKNLGKMNPPLRYVEDQEALWTGIRDGVVDMIATDHAPHTKEEKNREFQQAPCGVPGVQTMLPLLLNAVHENKLTLLDVIRLTSTNPARIFYIENRGELKEGYHADICVIDLEREGIISDEAQFSKCGWTPFHGMTIKGWPVMTIVNGQVAFERGRIYEEAKGQEVHFAQNLDLSTMIGGVPFQHPIFNAAGPRCTTEEELELLGASVSSAIMTKSCTLEPRDGNPEPRYHDFSQNSINSNGLCNLGYQRYAETIPGLKQHGKPCIVSVSGLSLADNLVMLKELSAVEEIDLIELNLSCPNVIGKPQVGYDFEQSKEVLKQVSEVCTKPFGVKLPPYFDFAHFQEMADILNQSSVSFVTCVNSLGNGLVIDPETEEAVIKPKGGFGGVGGTSIKPFGLSNVRKFRELLRPEIQVIGVGGITSGKDVFEYILAGADAVQLGTVFMQEDTPAFERIVKELQEIMKQKGYASLEEFKNKLKVK | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 740
Sequence Mass (Da): 81919
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A0A3P7KRJ5 | RRFTYYTVFSIPRSIRAWHAHRTINNRFDHAAYGLQPKHDVFGAHTTQNDELPIRLASGTIVVKPNIEKFTENDVYFTDGSRAENIDYVVLSTGYDITFPIVESGKMIKVNNNQVELYKYMFPIDQPHNTFAVIGLIQPLGSIMPIAEMQARVFFAALSGEATLPSVSEMKRDIMVKREKMRKQYVDSHRHTIQVDYIPFMDELATIIGCRPRFFPLILQDTPLAMATTFGPCAPYIY | Catalytic Activity: (2E)-geranial + H(+) + NADPH + O2 = (1E)-2,6-dimethylhepta-1,5-dien-1-yl formate + H2O + NADP(+)
EC: 1.14.13.8
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 238
Sequence Mass (Da): 27302
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A0A3G8M1J7 | MPTAPQTPQFVDFPIDGLPSKETFTHHDADAPDAQIIAHMANAFFGALPNASLPATGAVTQQSGAPALAGALPAVTPSLTDIPAPSIVTTIAPHAPARAPFGPMDFPPTTIPSVVPTPNVPAPSAPQTLHSSTRPLGLADIPQPGASLGGATSSVPGEMDYSAPTRRLAQEFSLVETDAVARPANNYYFLPTAPAPGPTEPLRYETRAPSTGAGYGHPDPFSPQQTSGAMRGDELVSRHSQGGATQGAYPLHPGEFAQGGDASNYAHSAPHLPGAGGREIPGAVHALYGDGVYAAPRQGRQPEKTVATRHLFDPYRVKRDFPILNQSVNGRQLVWLDNAATTQKPQSVIDRLAHFYEYENSNIHRAAHTLAARATDAYEEAREKVRRFLKAPNVKDIIFVRGATEGINLVAQSWGRRNVREGDEIVVSHLEHHANIVPWQMLCAEKGAKLRVAPVDDRGALILDEYEKLLGPKTRIVAVSQVSNALGTVTPVQEITAIAHRYGACVLVDGAQSVSHMPVDVQSIGCDFFVFSGHKVFGPTGIGVVYGKDAVLEHLDPWQGGGNMIADVTFEKTVYQGPPERFEAGTGNIADAVGLGAALDYVEAIGMEVIARYEHDLLVYATERMTTVPGLTLIGTAAEKASVLSFTLDGHDSQEVGKALDREGIAARAGHHCAQPILRRFGLEATVRPSLAFYNTCADVDALVSALLRLQTSKAY | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
EC: 2.8.1.7
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Length: 716
Sequence Mass (Da): 76143
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A0A8K0HER9 | MSLKNGKVSIDFLIGTVGKWKETYQWIPVFGAFTAIATAILTGANILPTPISSPVESGALTLIKASLMACTIYVPGATFACNSFVNVLFSDVIVLATAAIWLALATYLELPVLTQQSIQGALLGTILVTEGFSYVPLWNKNKNYNFNGGGLLWIFLEWTIAPLLACFCAFLPFSALKVSLLLHENAEKRILMFIPSDCGVSARLLCLFVMYQIVPNITTVYRWETTVAVAAAALLDSFEYDRQTLLRHALAEEYDDQVEEFFIFPQLLASCIFVLLQSAGEVAAVVSPYGAIHDIFSHKTKYSGNGKYMESVHVTWWFRAIGGFGAVMGFFLWGWQLTQCLGGKLTCMSNSRGLASQLSIVAAMIVVNRAKLPVSSVHAFVGSLVGVGIADEPRNVNRKLLLKFICGWVLTIIFCCELTTSQKRGKRPGGGLGGIIPGSLAPCVIHLRDKSCSLPIFHIALTTSSILLWLKAKPTSESMVGRSHGQRTRSTTQQPVDSTLEPQVTMPTTSPGDRHRKDPGPSCASPMETQSEEHTQTASPLETQPQKDVVNPICKKRGDEEGAIPHNEE | Function: Sodium-phosphate symporter.
Subcellular Location: Membrane
Sequence Length: 569
Sequence Mass (Da): 62043
Location Topology: Multi-pass membrane protein
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A0A3P7IQQ3 | MDSSLIYGVSYFSGGLPLLLGIFSIKSTSPWAGPYLKEEYKDLDNLETLTRQMEKDVAMYGFLNLIFFPLIFLYQILYSFFTLSELIKRRPDALGMRRYSNYGRYRVRHFNELTHELNARLNRSHVYANAYLNQFYSTLTEVFAKNIAFVAGAIAGVLAILSAWDEDVLQIEHVLTVISVCGVIMVICHGLISDENLVWQPEVLLAHVTSELHYVPVEWKGQAHTEQVRREFEQFFQLKWMFLLQELSSPILTPFILLFWVRPNCRELVRFFYDNT | Function: Phospholipid scramblase involved in autophagy. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion.
Subcellular Location: Membrane
Sequence Length: 276
Sequence Mass (Da): 32206
Location Topology: Multi-pass membrane protein
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A0A343LFJ8 | MNFMLTLIINTLLASXXXXXXXXXXXXXXXXXXXXPYECGFDPMGSARLPFSMKFFLVAITFLLFDLEIALLLPLPWASQTDKLTNMLFMSLFLISLLIISLAYEWMQKGLEWSE | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 115
Sequence Mass (Da): 13159
Location Topology: Multi-pass membrane protein
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A0A511AE62 | MARFGIEEEFQLLDEDTLVPVPLGSAARAVLPSGAGEVKKEFLTSQVEFSTSPVGTLAAAREELTAFRRELASFARDHGAVAIGSGTPFGVGPEASVVESERYDTVADWLGHIVDSHHVDALHLHVEVPDEEDRVRALNAVRPWMPTLLAVSGNSPFADGHDTGHDSWRTVIMRRLPLSGCPPQFRDMHHYRTEVDRLIAQHVIPDVGSVCWAARLSAQYPTVELRLFDAQLSTDDALLVAALGRALVETAVGADDPVRTGDDIQASLWSAARHGMEATLVHPSNGELVAARDAVGLLVETIAPALKASGDLAFVEDALARVLQTGTGAQRQRAAYAESGIEALRALHRFASDGEVHDAARQQ | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 363
Sequence Mass (Da): 39044
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A0A9D9EV86 | MDRREINIVYTEFGSLNELPDDDRELALKAIEATRNSYAPYSRFNVGAAVRLDDGTVVTGANQENIAYPSGLCAERTAMFYAASEYPDIPMKTIAIAASSGGKLCPEPATPCGACRQVMAEYQSRGGHHISIILVGEEKIWKFSSVDDILPLIFDSLGK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 159
Sequence Mass (Da): 17338
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B3ML97 | MACDETNCDGQISHTFVIFGASGDLSRKKIYPTLWLLYRDDLLAKPIKFCGYARSKLTVENIEGNCRQYMKVQPNEETKYEEFWALNDYVIGSYDNSSGFELLNRQLTLMENKNRANRIFYLALPPSVFEDVTVNIKQNCMSASGWNRVIIEKPFGRDAASSQALSDHLAKLFHEKQIYRIDHYLGKEMVQNLMTIRFGNKILNTTWNRDNIASVLITFKEPFGTQGRGGYFDAFGIIRDVMQNHLLQILSLVAMEKPVSCLPDDIRDEKVKVLKCIKTLTLDDMVLGQYVGNPDGTTDDARNGYLDDPTVKNGSITPTYALGVLKINNERWQGVSFILRCGKALNERKAEVRIQYQDVPGDIFEGSTKRNELVIRVQPGEAMYLKVMTKSPGITFDIEETELDLTYAHRYKDSYLPDAYERLILDVFSGSQMHFVRSDELREAWRIFTPILHKIEQERIQPITYQYGSRGPKQADVKCEQNNFKYSGSYKWPGSKKNS | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Length: 499
Sequence Mass (Da): 57272
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A0A1V0DGS4 | MTIAKRFRWEAAHRLPWHEGPCRNLHGHSYRMTVELTGEPDERGMLLDFQDLKRILKPLVEAWDHAVLVAADDAELLALLAQTDWKRAVLPADTTSENLSAYVAAHLCTEGRAVLQARRVHTVRVRIEETETCYAEVVQAVPPPEAPTPAREARAIVSAVS | 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): 18037
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A0A094I2U7 | PTSSTNFVELKTSLDPSSPRDLQTFERKLLKFWLQSFLLGVPKIIVGFRSANGQLRRLEELETAKIPGIVKKRGGWDGNVAVNFGAGVLSFLKETVVSEGVWRIRRREKSGVVECWKVEEVGHGEILSEEFINWRIKLALGPEGEVNGESEAPSEEQEGGEA | Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (By similarity). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphospho-guanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H(+)
EC: 3.6.1.-
Subcellular Location: Nucleus
Sequence Length: 162
Sequence Mass (Da): 18023
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A0A6H5IW07 | MLIDNNSFNTATAARMQTMANEPQVVEHFFGVYLLYCKNPKYKGRTYIGYTVDPRRRINQHNAGQKFGGAWRTSNRGPWEMVLIIHGFPNSTSALRVIYLIYQLITTYTLAFYFLFVVLFIVRHHQFEWAWQHPQLSRRLKHVGKKRARQKTFDYLLEVCSAMLNCGPWNKLPLTVRWLDDEFGQKYSTHLTSPLHMPITYGKVTSRKKKTTTTTTTSNDKAKEAVLAVLGTRDDGSSRDCIKPDCGLVAHLVCLAKLFCKESGDILPVEGSCPICATDALWGDLIRKKIGCNLHIDADVDESGSSSSSEEDDDYQSDD | Function: Catalytic subunit of a heterodimeric structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 319
Sequence Mass (Da): 36244
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A0A831SP07 | MFNPLDILRDPENLQPVLLSLQTAVAALICHLILGVALGYALSRKKLPLRVLLDGLVTLPLIFPPVATGFILLMILGRYGIVGKHLAAQGMDIVFSPAGVYIAAVISGLPLIVKPVQSAIENSAESLKEASFVLGKSELDTFVCIILPTIRRVIIAGLMLSVGRSFGEVGITLMLGGNISNRTETISLAIYNSVFEGNTEKALVLSGLLAVFSLLVFYGMNKLNGNRTTLQ | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 231
Sequence Mass (Da): 24672
Location Topology: Multi-pass membrane protein
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A0A4Q4UQU9 | MGVEDESLVPVVNLLAPSLVIKRQSSPFGAAPIYKHPDIINLYCVWRDFHTTTTKYLQNSTRQWVDFMAAGVMDQVSAVPLLCQTDPAGRKYEDTASDSLTVGFIDRGLDHSQIYSPTFCWQLREEMWKTVLPALIEGHWNEFKGFNRAFCTDADSNLGKGCLRLLMEALARDKNAIAAAGTVFAQLEPGFGWSSWDLHQRFQYTFSQFVRRRAEGHIGKVTCLPGCVTMIAVRKEMAGAIQKTWHVRPIHFPALIIVPLHHSSPPPQRVTSTNASSSQQGTDRRVTYSMLSQGHNLSTFFVPKAVSEAVAPQPLERYLSQRQRWGSNSYFNGYFYLGGENMSLIIRVAAASDTARQTFVYCRVLNTIFFISSLVWSRREPDILLALIAGQLPLACLGCVRRHCRVNAADSSEPEFESEDGGKKRSQSAESTDDTRPVNAETSAEEVGVCFLSKQDYPPQGKGRESLLAHFGVPEFVASRTCFELNGFFGHRVAYDGGDRRTGPVDGWTGHVDGDGVPVTSCTTWFRCLFKMIQKIPTGASEDGLEYCSTGKGYQWYETTVFSHWKSEARCQVLCVDVPFDFAEELKKALESRTAPLNFGDPFAMHVDVWDRIVVYYDISVWRVRDPVRMLEKDPTRRRDVFRPTHDHMRHAIHVSEILESAVSTAMEMQRCRAEIYKDLPRDLLGKTYEQQANEYAAFQVSVVRNLKLRSESNQARLGQEINYAFNNLALQDNNFIKSITLFTMIFLPATFISGVFSTTFFSYGQRQWEVSDQLWIYWAIIIPVTIAVILLWHLWLYKRDAILKLLQKIGAWCRNVPRKPAKHLMKRWERRGGSKDAEAGLS | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Subcellular Location: Cell membrane
Sequence Length: 843
Sequence Mass (Da): 95638
Location Topology: Multi-pass membrane protein
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A0A4W4EI36 | MPRTHTQQSKMADSKVKQELLDATTTSLKINSSEITTLIRQALEAKKFAYCPYSKFRVGAALLTHDGTVFTGCNVENACYNLGICAERTAISKAVSEGFRDFKAIAIASDLREQFISPCGGCRQFMREFGASWDVYLSKPDGSYMEMTVEELLPESFGPEDLKMKREHSIPKDVEPATK | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: 2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+)
Sequence Length: 179
Sequence Mass (Da): 19948
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D3EP72 | MKNQLPIFAKIWEQEINWKPTEKHLDQWEELYQEIILINNQVNLTRIVKPEEFWEKHLWDSIAGVVGLPFFQYSRKMKVIDIGTGGGFPGLPINIVFPIWDFTLLDSRRKKIEVVNFLLKILELENSWALTGRAEKIAHDSRFRGKYDIALIRAVGESSTCSEYILPFLNIGGIGVLYRGNWSIQEEQLLKVALKRLGGKLILVKESKTPLTKSVRHFVYVQKTHLTPKCFPRDIGVPKSNPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 28082
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E0S5V2 | MENIVIIGSGPAAYNAALYTMRGNPLLFEGGYIGNNGPGGQLTTTTSVDNYPGFPGGIEGPELTQLMKEHAVSRGLRVVKETVSDVRKEDEWFVVSSEKGEKKARIVIVATGASARRLFVPGTGDDEFWQKGVSSCAVCDGFIYVNKVTCVIGGGDAAMEEGLYLSNIAKKVYIIHRRNEFRARSDMIEKARNTENIEIMTPYVLERAEGTNKIKEIVVRNTETGETKTIPMDGVFFGIGHDPNTSFLKSVNVDLDSNGYIVVKDDACTSVPGLFAAGDVCDRKYRQAVTAAASGAICGIKAMEFLDKNK | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.9
Catalytic Activity: [thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH
Sequence Length: 310
Sequence Mass (Da): 33571
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A0A0J1FL26 | MLWVALLVGVQVLLLGTVIILENKDPGKTVTWLFILSLLPILGFLLYILFSQKQRNKLFRNKAQRTNRLKQRINEYDPIPKNEYSTFSPDNNLDLKLANLLMYSGYARLKMHNKVDVLVNGREKFAALLQSLENAAHHIHLSYYIFKDDEIGADVLKILSHKVSEGVEVRVLLDGVGSLFLAGNFMTTMRQAGIQAQWYFPLRFPFLTPRLNLRYHRKIVIIDGYVGYMGGLNIGDEYLSRDPKLGFWRDTHLKLFGESVHTLQSIFLNDWNTVTHQEIRGENYFPKVEIPDILPIQIGASGPDSNWASILQGFFVAITMAKRSIKIETPYFIPDESLIMGLKTAALSGIDVQIIIQGVPEHKVTYWAMNSYLEELLEAGVKIYKYMKGILHAKVLLIDETLASVGSANMDVRSFSLDFEISAFMYDQKLTMLLVKDFENDLSESRSINLEAFQTRPYSERLKESFARLFSPLL | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
EC: 2.7.8.-
Subcellular Location: Cell membrane
Sequence Length: 474
Sequence Mass (Da): 54215
Location Topology: Multi-pass membrane protein
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A0A1V0DB92 | MTYLTFLLVFLIPPIVLLAVTQPRPLAGVGGWRGRWSIPLVCVIAMLYTTPWDNYLVYRQVWWYGADRVLATIGYVPVEEYLFFLLQPIMTGLLLYQFLARSPHVERLGPARGTAMAGTVFYVVLTAVGCWLLLAGGDQGLYMGLILAWAGPPLAGLWYYGAPIYHAHRRSFAGAVTLATFYLWVADRTAINLGIWDISDRFSFDIDPLGLPVEEATFFLVTNLLVVQGTLLFLFGHLLPSRTSRLPS | Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
Sequence Length: 248
Sequence Mass (Da): 27734
Location Topology: Multi-pass membrane protein
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A0A425XNK0 | MQKVSNRLVPGYRLGLSITFVGLLLIVVIPFCSLLVQGLDVGFKKFWLQATNDRVLASYAVSLKGALLAALINALLGLILAWVLTFYQFPGRQLLDYLLDLPFALPTAVAGIALAYLFSNKGWLGRLAAPMHVQISYTFSGIVIAMVFVTIPFVVREVQPVLEQLDSTYQEAALTLGARPWTVFRKIIFPEILPALISGFGLAFARSIGEYGSIIFIAGNQPFKTEITPLMIMFQLEAHSYTGATVIALVMLVFSFCFIFAIHALQRHVQRQKG | Function: Part of the ABC transporter complex (TC 3.A.1.6.1) involved in sulfate/thiosulfate import.
Subcellular Location: Membrane
Sequence Length: 274
Sequence Mass (Da): 30260
Location Topology: Multi-pass membrane protein
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A0A257HQH2 | MTDPLWTSTAAALAVSGKAQGQWAVNGISIDSRAVEPGDLFVALKAERDGHSFVRSALAAGAGAALVVDPTCADAGAPLLVVPDTLLALENLGTQARRRNVIATRVAITGSVGKTTVKEMTATALAATAKTHRSVKSYNNHWGVPLTLARMPGDARFGVFEIGMNHGGEISRLSPQVRPHIAAITMVAPVHIEHFADETGIADAKAEIFLGLDAGGTALIPGENRHAARLAARARDRDGISILTFGMQPGFDSHVVGIDEIDHGRRVTADIMGQQLSWIIQEPGAHWVHNGLCALTLAVLAGGDGQAAAAALSQFGAIDGRGVSRPISLATGGFFVLVDEAYNANPASMAEAITTLSGRAGLRRIAAVGDMLELGVNENAYHAAVAEDVIRAGIDLVFCAGPRMKHLWDALPEAQRGAYAASAAELAPVLAQAVQAGDVVMVKGSNGSKMAEVVRALQALEAPAGES | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 467
Sequence Mass (Da): 48341
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A0A3A1Y5N8 | MTELNKHSFLVELGTEELPPSDLKNISAGFTDALVLALHKANVAYDEIESFATPRRIAVYIKGLNSVANSQLVEKRGPAKAACFNEDGSLSKAAQGWLKANNLEFSQVSFLETDKGAWLYYSFEQPGASSEEILPQAVAEALAGIPISKGMRWGNHDFTFIRPVHTFTMLLDDKVLEGTAFGVKSDRKIYGHRFLGTKEFTLNHADEYQSRLLAEGSVVASFAERRKMIVNNVKKLASQYNGYVNLEDDLVDEITSLVEYPNVLIANFEKEFLKVPKEALIHTMEGDQRYFPLFADNKFTQLLPHFIFVSNVTPKDPSLIIAGNEKVIRPRLSDAKFFYEQDLKKPLEDLLPRLKMVVFQNQLGTVYNKTLRLEKLALVLAEKLKGNTTFAQRAARLAKCDLMTNMVFEFTDTQGIMGMYYAQAAGEEKEVARALFEQYLPRFSGDQLPTTLTGSILSLADKLDTLVGIFGINQPPKGAKDPFALRRAAISILRILTENGFNLSLGSLVQATIEVYGDKLTVPADKLKEDILSFVNGRVKALYEEQGYAIDEIQSVQNLNIDNPYDFFLRLKAVHDFKSNLACEDLAAANKRVNNFLSKSDFDNNAKVDETLFETDEEVNLFQDLLVLEERCLPLYRAQEYMKILSELASVREDINAFFDNVVVNAENELVKANRYALLNKLQLLFSLVADISTLNY | Catalytic Activity: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
EC: 6.1.1.14
Subcellular Location: Cytoplasm
Sequence Length: 697
Sequence Mass (Da): 78384
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A0A1V3P5K9 | MDERALADLFVAPISACIADSDMFSAPLFSEEEAYIRKAIPARRREFSAGRAAARKALAKAGADVGPIVAELDRSPRWPDSFCGSITHCEGFCSAVVARSVDADGVGFDAEEAKPLGSDLYHLVCRPNDLEHFHPLPRIDGVDWPKLAFSAKESFYKCYYPSTRSFLGFRDVSVIFSVTAENSKEGTFLIILENKVKPMPRPSTDFVGRWFVHGERVYTGVTLPRA | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Catalytic Activity: apo-[aryl-carrier protein] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[aryl-carrier protein]
Sequence Length: 226
Sequence Mass (Da): 24970
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A0A317CJE3 | MSRLFRSGMVISIMTLMSRVLGLVRDAVYANYFVMGSAMDAFLVAFRIPNLMRRLSAEGAFSLAFIPVLTEYKEKKSKEELKDLIDHVAGLMGLILFIVSLIAVIASPLLMMVFAPGFEAKPDAEPELAAYLLKITAPYMLFISLAAFFSSILNAFGNFAVPAFTPVLLNVVMISAAIWWAPAFEEPVEALAWGVFIGGIVQAGFQLPFLQRLGLVPHFSLKKGHEGVKRIMKLMGPALLGSSAAQLNITINTMIASTLTAGSISWLYFSDRFVEFPLALIGVAIGTVILPKLSGDHANAEGKAFSGTLDWAMRLSLLVSIPATVGLIVLAVPILATVIDNGVNGWRDVEMASLSLMTYALGLPAFIMVKVLAPGFYSRQDTRTPVRIGLIAIVANIVCNIAIVLPWYKLGFIGPHAGLALSTAISGFVNATLLFIGLRKQGMIAATAGWPLYLMKIVIASLCMAAVVWYVNPADSWWQDSGVFGKIAALGGLVLSAMLTYLLAILAMGIRPRQLLRV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 518
Sequence Mass (Da): 55849
Location Topology: Multi-pass membrane protein
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A0A4W4EVC8 | MGKQQFRETDVAKKISHICFGVKSAEQMRQQAHLQVVSKSLYSQDSSHTPLAYGVLDHRMGTSEKDRPCESCGKNLADCLGHYGYLDLELPCFHIGYFKAIIGILQMICKTCSSIMLSKEERQGFLDHLRRPGLPYLHKRGLKKKISDKCRKRSVCLHCNAFNGPVKKCGLLKIVHEKYKTTKKVVDPVVSDFLQSFDLAIEHNKEMEALLSRAQENLNPLVVLNLFRRIPSEDIPLLLMNPEAGKPADLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRMSGAKTQMIIEDWDFLQLQCALYINSELSGIPLNMAPKKWTRGFVQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDEVAVPVHVAKILTYPEKVNKANIELMRKLVKNGPDVHPGANFIQQRHMQMKRFLKYGNREKMAQELKPGDMVERHMIDGDIVLFNRQPSLHKLSIMAHIVNHRLHSGGER | 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: 488
Sequence Mass (Da): 55521
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A0A4W4FHK2 | MSSSACACCCFRKAIAKSGIQHLTAQSSASMPNKCEANQEIPQKVDWTENAQFGQHVWFETSLSGDFCYVGEIYCFAKLLQKSLPRYKCAACKIAVHTVCMEQLEKVKYFIAVFTDLGFSLQINFRCKPSFRDPGMRNVREASTVRHHWVHRRRQDGKCRQCGKGFQQKFSFHSKDIVAISCSWCKQAYHNKVTCFMLQQIEETCSLGAHAAVIVPPTWIIRVRRQQASLKSSKRRKKASLKSKGSKKGPEDGKWKSFIVKPIPSPLMKPLLVFVNPKSGGNQGAKIIRSLMWYLNPRQVFDLTQGGPKEGLEMYCKVPNLRILVCGGDGTVGWILSVLDELRLNPQPAVAVLPLGTGNDLARTLNWGGGYTDEPVSKILSHVEDGNIVQLDRWNLSVEPNLEASEEEKDEQQTDKLPIDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRLRNKMFYAGTAFSDFLMRSSKDLSKHIKVVCDGMDLTSKCPLLYCAGTMPWGNPSEHHDFGPQRHDDGCIEVIGFTMTSLATLQVGGHGERLHQCRQVTLTTFKPIPVQVDGEPCRLAPSVICISLRNQANMVQKTKRRISIPQLNDQQPISEQLQIRVSCISMHDYETLHYDKDQLKEASIHLGFITVPGDSDLETCRLHVEKLHEVHLNRLPLVQSLYFVTLQTLKHCLLFHSKILCLSCCWLQEHLNYVTEISQDELFILDPEMVTKETVGTSPGMPGTTDVVEECSNGSDKFAFPVYSPTPRSLDRYNWNSGHGALKRATCYRIGRTEQFCCSLAVCVSQLPINHCSPAVLQLVAQHKAGASLGLCDEMGCTLLHYAVDMGNKDMVRYILDNAPPSILDAVEKETGETALHKAAALCQRTICGYLVEAGASLVKADLQGDSAKVRAERAHDRPLADYLENQQHRQMIQRDDHETAV | Pathway: Lipid metabolism; glycerolipid metabolism.
EC: 2.7.1.107
Catalytic Activity: 1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+)
Sequence Length: 932
Sequence Mass (Da): 104572
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A0A8E6B1W4 | MLTLQLPDGSTRQVNPGTRPREIAEGIGKRLAQAAIAAKVNGAIVDLEREIEASDQPITFQLLTDKDRESLDVLRHSCAHVMARAVMRLFPGTQLAFGPTIENGFYYDIDSPTPITEADFPKIEAEMKAIVKQAEPFERFERSIPEGRGLVADLKQRLKVEHIDEELKKYPSISFYRQGEFIDLCRGPHIPHAGKIGAFKLLSIAGAYWKNDASRKQLQRLYGTAFFTQKELDAYLLQIEEAKKRDHRLLGKQLKLFTISQQAGQGLILWMPKGATVRHLLETFIREELVKRGYSPVYTPHIGNLNLYRTSGHFPYYADAQFPPIYFNPVVQTVDTWYTLLEKGKLLPEREESFLKLVEALSRGEFPEGADDYPRYTWSQISLDMRTLLLDYREAKDEEAKKHSLKNWMSGQEGYLLKPMNCPHHIQIYKAGPKSYRDLPIKLAEFGTVYRFEQSGELGGMTRVRGFTQDDAHLFVTPEQVEAELRSELELVLFILRTLNLTDYRVRVSVRDPASSKYVGAPELWDKAEKTLLDIVKSTDLNYVIGVGEAAFYGPKIDFIVRDCIGREWQLGTVQLDYNLPNRFDLEYIGADNQRHRPVMLHRAPFGSMERFTGILIEHFAGSFPLWLAPEQARIVTVSDKFIDYARGIETQLKAAGIRVTGDYRPEKIGSKIRDGSLEKIPYLLIIGEKEQNSNTVSLRDESIPDIKQRDIGALAVADLLSRFKSEIEEKRVRNVSTATAGLTDGAAKFGE | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC: 6.1.1.3
Subcellular Location: Cytoplasm
Sequence Length: 752
Sequence Mass (Da): 85454
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A0A4W4E6B3 | MITLHILSGMSARHFLFLCVLCALYVSLCSGACAEVDSDTQAVAGQNFKLGCISCKMRGEVEASATVDWYFRAKGETDFAHIYSYDDESPTIIDERFKERVNWTGSRKTNDLQDASIYLLNVTFNDSGVYRCFFSRTLSYQYYEYQTTVSKLVHLTVVAKATRGVASIVSEVMMYVSIIGLQLWLLVEMVYCYRKIAAAGDEALRASAAEYLAIASESKDNCTGVQVAE | Function: Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with NFASC may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons.
Subcellular Location: Membrane
Sequence Length: 229
Sequence Mass (Da): 25526
Location Topology: Single-pass type I membrane protein
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F6G4B5 | MFSFWKKRKAEPQPAAEPAPPAAAPEAVQAPVPAPVASPTPAPAPAPVAVPDTPAAPAALDMQADDIETVPTPPVMEQARKGWMSRLRSGLSKTSKNLTTLFVGVKVDEALFEELETALLMADAGVDATEYLLDELRRRVKAQRIETAESVKTALRDLLVELLHPLEKTMVLGRDQPMVIMIAGVNGAGKTTSIGKLCKHFQTYGQSVLLAAGDTFRAAAREQLVIWGQRNNVTVVAQESGDPAAVIFDAVNAARARGIDIVMADTAGRLPTQMHLMEELKKVRRVIGKAMVTAPHETLLVIDANTGQNALAQVKAFDDALGLTGLIVTKLDGTAKGGILAAIARQRPVPVYFIGVGEQVEDLQPFSAREFADALLG | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.
Subcellular Location: Cell inner membrane
Sequence Length: 377
Sequence Mass (Da): 40168
Location Topology: Peripheral membrane protein
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A0A1F9XV41 | MTSHGVADSIREKLDIVDVVQDYIPSLRRTGRNYKAVCPFHNEKTPSFTVSQDKQMFYCFGCNEGGDMFTFVMKIEGLTFVETLKKLSHKAGIPWAETEYHQLSAKEKERLDLKKVLTAAAEFYKKLLFSSNGEKVRLYLGGRKINKATVEHFGLGFAPGEPSLTAELERQKFSKELIVTAGLAGVRDNGSVTDYFRNRVMFPIRNSTGDVIAFGGRALDDGQQPKYLNSPETPLFSKRRTLYGIHEALPQIRKEGRILILEGYMDVIAAHQHGVTFAVAPLGTALSAEHAAFIKRYSKDTILMFDADEAGINASVRASDIFMEAGMYVKVADLGESLDPDEYLNEYGREAFDSKLAQAADPLEFRISALLRDRPDAMASQDKAKLIETLLDTVVKQSDEILKSEWVKTLATRFDVTQESVLRQLKKKSVYAPAPRRDAPGHGAGAPALPEVPAIELGFIHLLVKDPGLIACVKDLTEADFQNPVSKRIFSAVKDLAGEDPAKTIPRLVELLPEYAGIIMKLSVEEMGPDMNTTQNAAKAAETLRKLSLERKRKELKSRMGSLTQAEMAEYIALMGLKKGLKVKTDTE | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 588
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence Mass (Da): 65264
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A0A1F3SMZ0 | MTTKSKTKFQSQHKSDMLHPLYSYKKNKLFYSGINLSDLPTSLPTPFYLYSLSAVTNNVAAFQQAFANAGIHDLLICYALKANPNPHILSHVSQLAAGADIVSKGELSEAMKANIPSERIVFSGVGKTKEEILEALNAGQNGIRAFNVESIEELDLIASCAQECNKIAQVAFRLNPSIKAPTHHLISTGNKSHKFGLLPKDILETLPHFKTKSLYRKHLKLVGLSVHIGSQLLTFRASKNAFRALASLALTVSDFLGRPLEFLDVGGGLGIAYHHHTMTLSPFHAYAQSVKSGVAAYLDRYPCQIVCEPGRSLVGNAGVFITRVVRVKKSGPYTFLVVDGGMNDFARPALYQAHHEIYPFIKRSGAAVKANVVGPVCETSDCFAEGRTFSPVLVGDYLAIADTGAYGHSMASFYNLRSLPAELIMDAEKKQAYLYRSVPTQFKSSTFEVTSSRAPKESSLA | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
EC: 4.1.1.20
Catalytic Activity: H(+) + meso-2,6-diaminoheptanedioate = CO2 + L-lysine
Sequence Length: 461
Sequence Mass (Da): 50294
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A0A238U6X3 | MMNFIKTKIPDLMIIEPKVFGDQRGYFFESFNVKQFEEHIFKVDFVQDNESRSSKGVLRGLHFQKPPYEQAKLVRCVKGSVLDVAVDIRRGSPTFGAYEAVELSEDNKRQLFVQEDLLMALLFCPKVQYFLIKLIIGMLLNLIVV | Pathway: Carbohydrate biosynthesis; dTDP-L-rhamnose biosynthesis.
Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Length: 145
Sequence Mass (Da): 16795
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A0A8K0GXM5 | MKVIGKELFKVLRERRDTNFESFISEKVTAISGDVSLENLGVQDVQLREALWKHIDIVINFAATTRFDERYDAALDTNTLGVLHVLGFAQRCVKLEMLVHVSTAYVCGEREGLIKEDTVFHMGKTLKATSILDFKEEQKLVAEKLKELRDQNASEDTITTTMRDLGLKKAKLYGWSNVYVFTKAMGETCLVDSKEKFPSIIIRPTVITSTYKEPFAGWIEGLRTLDTLVVGYAKGKVKCFLGDTMSILDLIPGDMVIDLMIVAMVAHANDHQSFKTIIYHIGSSLRNPINISNIRKFSFQYFTRKPLKNNKGEPIKNIGKLLFLSNAAVFHTYMLIRFILPLKIQKLGNIISCQYFPDVYTENNRKLKLMMRWIELYKPYTLFKGIFDDENSGKLRETLRGSSKETLEGFNFDPKCIDWEDYVMNIHIRGIERFGARYGKENLMREVVYYAMEKRNLASICFCYALRCEQLHCRESKSKVQEESTIWSPPPEGWIKANIHASRNDEGLPLILVICISWDLPKTLADRLILEQLQAALYDVALSTNTLGALLVLSIAKRCINLKMLVHVSTGWIEGLRTIDSAIASFAKGKMKCFLGNRKQIVDLVNMEIKLSIYTYADSRSLTNKNRKIVKVGKPIALINNMPTLKLYIAIRYKLTLKDPKC | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 662
Sequence Mass (Da): 75625
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A0A1F8L2J0 | MALPSRPPPPASGVVLAGGRARRFGRDKLAEPIGGGPLLHRPIAVLAALCSEVIVAIAPGSAAPALPESGELLWVVRDPIPDGGPLAGLVAGLREAREPLVLVVGGDMPDLRPALLEGLLRRADETGAGAVALAEREVVRSLPAVVRSSALPVAERRLGSADRSLVGCFRSLGLVVIPEMEWRAWDAAGDSLRDVDSPEDLPAPER | 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: Cytoplasm
Sequence Length: 206
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 21387
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A0A336MN17 | MLQAYRSIAVFICSNVKHRDRRRHIRTTWGRVLRPKPIFILGLSTDNEVDNEMALEEAHLYQDVIIENFHESYQNLTLKTLFALKHFLRLTPNETYFLKIDDDVFLNTYQLDHIMEKYQTTPGIIGHLESQRYAHRDKESKWFTPRWMLSKEALPNFINGPAYLISGSLVKKIYEKALETPLITLEDVFLTGLVSNELLNIPLYNNIGFEDYYSIDSIFNRDCFYRSVFTIHRMTLMEQIYELWDKLKENHEPCWDI | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 257
Sequence Mass (Da): 30622
Location Topology: Single-pass type II membrane protein
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A0A0P9A948 | MSWRYASPSRLETSEQTTGRQLQRVLHYSMAPSRALPGLRRAECAIHDVDCDEVYPGIYIGDAAAAKNKTYLRLMGITHVLNAAEGCRYGQVDTGHSYYRDMPSIRYMGFPMIDAPTTDISRYFYVASKFIDSAISSGGKILVHCLVGMSRSATCVLAYLMICRKMSAVDAIRTVRMRRDIRPNDGFLQQLADLDMELKRKNLYPY | Function: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues, with a preference for phosphotyrosine as a substrate.
EC: 3.1.3.16
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Length: 206
Sequence Mass (Da): 23313
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A0A3P7IXC6 | MGLIRFFKENTITVRSDRLLDKERIYHLDLYNSFSTYSTTLGNLLLLMGSDEHSSRQRELIVDLLPPTSVRSEPHSLPRSVHQILSDDEFNEEQRKAVFSALLCKDYTLIEGFPGSGKTTTIVALLRCLLEMKCSVLLTANTHSALDNVLAKLRKHVEPEKLLRLGKFSSGCSAVSDLTLESKIRSGEGDKYILARNILKNTVCSTLHLKAFTPRVFC | Function: Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 218
Sequence Mass (Da): 24544
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A0A3P7LJ71 | MFLLFNENQPDIVKSGDVVRLFHADQQTFLTLDSVPKTCPPQDVVFLRMTNRPSAADATSSRALWEVQVVQKDAYRGGAAKWREYYRFKHLATDMYLTVIPATSPVKPASNGRRASLMHMKXXXXLDSVPKTCPPQDVVFLRMTNRPSAADATSSRALWEVQENAYFRTKAELLAPPSLYADGPESTEECATSMYFLVPVKSDFPEADKRLLFCLDPGTMPKVGQLYIAKCILINKDVPTKSYVRLQHEATNTWVHATNASEKQNLYYSSKNEKGWVRVICENSRVDKETFALLPVSPNEVRDLDFANDACRALRNFIRHIKSGDPVTKESINKNEKGWVRVICENSRVDKETFALLPVSPNEVYLRNFDPIPKW | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 375
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.
Sequence Mass (Da): 42589
Location Topology: Multi-pass membrane protein
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A0A3P7KYQ9 | MIVVKSYKIELLKQVGKGGEVKLKVEYRLTQLLKPLPEKITQRENQYVVYHGNAHYAAPYAVEQEKTIVKLGSGKTLSVTQVSPTTQENERVVYGPYKNQPAFNKKHIKIHYENNAPFVVATVVERTIEISHWGNIAVEEYIELVHKGAELKGPFSRIDHQLDRRGRRQPALLHFTVSCSSFM | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 183
Sequence Mass (Da): 20928
Location Topology: Single-pass type I membrane protein
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A0A3P7L1C9 | MFVGEDKEKVTKIVRGSMQELAEVYDPILSDDPRIVMQNGKILQDGSTAAIYHRLNL | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 57
Sequence Mass (Da): 6434
Location Topology: Peripheral membrane protein
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A0A3P7LEN6 | MSDARLPCEVRASFTRLMLHLHVVRGSPLSAIRHARLWADIPEEVVVQSYKTTSVEGYSDGGRARVGDQFANDVLNTVESYLDSLRDRHPSGPVLKEDAASVCTNKLTHEMVTLAKALAQFGYYTFDNLLTLTENLLNIKNAPVLARTVSHGMTMIHRVTQSMIGGRSMTLDGPSKSTEKSSIEDTVKTKESRQLLVKTKLIVAEILQVRYLYCLGARLR | Function: Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 220
Domain: The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.
Sequence Mass (Da): 24490
Location Topology: Multi-pass membrane protein
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Q919T0 | SGLPVGGNEMKAKLANVVRKMMTNSQDTELSFTITGDNTKWNENQNPRVFLAMITYITRNQPEWFRNVLSIAPIMFSNKMARLGKGYMFESKSMKLRTQIPAEMLATIDLKYFNESTRQKIEKIRPLLIEGTASLSPGMMMGMFNMLSTVLGVSILNLGQKRYTKTTYWWDGLQSSDDFAL | Function: RNA-dependent RNA polymerase which is responsible for replication and transcription of virus RNA segments. The transcription of viral mRNAs occurs by a unique mechanism called cap-snatching. 5' methylated caps of cellular mRNAs are cleaved after 10-13 nucleotides by PA. In turn, these short capped RNAs are used as primers by PB1 for transcription of viral mRNAs. During virus replication, PB1 initiates RNA synthesis and copy vRNA into complementary RNA (cRNA) which in turn serves as a template for the production of more vRNAs.
EC: 2.7.7.48
Subcellular Location: Cytoplasm
Sequence Length: 181
Sequence Mass (Da): 20613
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A0A5K7YMI5 | MILYLIGYRCTGKTTVGRALARRLGWPFTDTDQMIAATAGNSIARIVDRHGWPYFRQKERQALASVSEMDHQVVATGGGIVLDDRNVAIMKTSGRVTWLKAGRKTIEMRMLADDATAGNRPSLTGQGLMEEIESVLSERRPLYEKAADLALATDHEKIETLCDRIVAEFKISELRD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 176
Sequence Mass (Da): 19611
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A0A924S0V5 | MRTLPPLRRRLALATLVVVGAASLAACGFHRRVAQSLSYERIALSGFGDRSTMADEIRRALPSSAHIAPSVLESQVVIEAIEDTQKTTVEASTAFGQVRELELHVKLRYRVLDPNGLELLPLADLERFRDMTFDEKDALAKDTELKALYRDMQSDMAYQLVRVLSAVGNPTGPAAHVQAARAASAALAPASAASAVSAVEWAASQAAGR | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 209
Sequence Mass (Da): 22438
Location Topology: Lipid-anchor
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A0A7S1CU31 | MALRSAVCAALVDRKDFIEPFIGSGIEEYVCEMQKPSTWGGEPELSMASIVLLCKIVVFEPVIEAKVISLSKTSEYCLVEDAKDDDLESIHVLFSGGMHYDALITMP | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 107
Sequence Mass (Da): 11773
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A0A069CXX4 | MGIINQVREKQPLVLNLANTVTQQRVADVISYVGGSPLMTTASNELAELMQIASALVINIGTLNDELLPLYIEAGKLANQLNKPVILDPVAVTLPYRGEIVTALLKEIKVNIIRGNAAEIAWFANQTVAGKGIDALDNQINEAIVLDAAQKTGAIIVQSGPTDLIADGQQVIKITAHSDLFKINVGTGDMLSALIGTFSAVSADYFAAAVEATELFANSGVKAAQIVEQKPANFINALLDCLYEAN | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole: step 1/1.
Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
EC: 2.7.1.50
Catalytic Activity: 5-(2-hydroxyethyl)-4-methylthiazole + ATP = 4-methyl-5-(2-phosphooxyethyl)-thiazole + ADP + H(+)
Sequence Length: 246
Sequence Mass (Da): 26040
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A0A8J6NBD5 | MFDFLKNVTYQIISPIASARSRYETFKDLLKNDQKAHELLATLEEVYYQNKKVDINYATRLYSQLSQAVSTMVACLGKMSPGESTNLRAYYRKIDFFCRFALAPPEIDTSPPFILPITKIYPDDSLTGGKGFNFCILKNTLGLPGPHGFIISTSAYNYFIKESGLRHTIDEILAEIDIHSTESLHNSSKQIIDLIGNTALPDSLKKELNQAFKELRNQCSTDITLAVRSSAVGEDSKISFAGQYLSILDADGGNLLESYKQVTASKFSPRALYYRISNGLHDYSTAMAVLVLEMVDASVSGVITTKDSFDKGDDVVCIHSLQGRGEDLVSGKRSPDTTIIQKEKPFKILQQIPSRPGDAFTLTEDQAKQLAQWAIRIESHYGVPQEIEWCIDQNGSPLILQTRFLRVQKKPEQTEIDTSSYRELFRGGELAARGSAAGKIYLLNDFNRLSEVPKGAILVTRSTLPSLATIAHNLAGVIADAGSAADHFASVAREFNIPTLVKTNIGTELFTSGQQVTLWTDQTTVFDGVVETLITQYSEDEKEKETPFLKSMSIVISLISPLRMVNPADPSFVPESCRSLHDIIRFVHEKGMMSMFGLALHKPLRKGGSKLLESNIPLQLYLLNVGGGLSPESDSQKTIAIEDVLCRPLLALWKGLAHTGVTWQDRSHFDWGAYDDLVMAGGVVNAKSIAFASYAVISQDYLNLNMRFGYHFAILDALCSPDNGEGYITLRFAGGGGDIEGKLLRLAMISEILSRLNFTVTRKSDLLDARFSDRNTDKILETLDMLGRLLGATRIMDMILTNEEMAAGAVEEFMNGKYTFSKE | 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: 823
Sequence Mass (Da): 91150
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A0A1F9XRM6 | MPKFIDYYSILGVPKSASEAEIKSAYRKLAMKHHPDRNPGNRESENKFKEINEANEVLSDPKKRQTYDQLGDDWRQGRNFTTPPGGGPRGGGFESRPRGGGGQGFEQFGDFSDFFRSIFGGMGGASYGRSGGEDDFESFTRGVGQSTPGDMESELHLSLSDVIRGGQQRLTFSYKSICPECGGKGRQKARACAPCKGTGHSLETREIRVNLPKVLRDGTRIRLTGQGRRSPSGRNGDLYLSIYITPHTDFKIEGDDLETRIHVMPWDAALGAEISIPAPDGPVKIKLPAGSGAGRRLRIAGKGLPKKDGSRGDLYAILTIDIPPSPTPRQLDLFRKLKEVS | Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Subcellular Location: Cytoplasm
Sequence Length: 341
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Sequence Mass (Da): 37285
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A0A3P7LBI4 | MLVIGKLAPRWNVPIIAHMSGDDALSDRSVFPTLGSVALTSASEMARATLAFLQLNNWDELNDHYPWEATNVDKQEVKAAFENVIIITAHGYDKKFFDEFQTKFSQATGMLSSHYATLNYMSLYDALFLYGLALRDAYEEIGGYDVHHNGSFIWSKMTNRQFIGATGQVLMNNKAIRVPSYATYHTTNGTLRIVVELEAKHAERSLCEKNSDQCSEXXXXNFKRSLARQRECSVVINITFPKSELKLLKELKLTENENLNKFYGICFNQQNEFIVLWVYCNRGSLEDILFNEELKLGRNFQVAFAKDVVKNCLVDSNWTVKLTNFGTESIISEKLYHNEIKLIVDEGEDEADRLADRKYVQQAPEIIRELVTRKTLPPGSQPADIYSLGMSIITFKSKILCRGKGSLVDQMMKMMEEYTSNLENMVRDRTALLEEAQKQADRLLNSMLPKSIAEDLKVGKPVLPQLYQCATVLFSDIRGFTRISSTSTPLQVVTFLNDMFSGFDAIIAKHDAYKVETIGDAYMIVSGVPTENGNNHVQHIADIALKMRSFVCNFKLAHRPDEVMMVRIGFHSGSVAAGVVGLAAPRYCLFGDTVNMASRMESTGVANKIQISEQAHDLLHCFFQQFIVVERGKIEVKVKKRFCLLTYS | Catalytic Activity: GTP = 3',5'-cyclic GMP + diphosphate
Subcellular Location: Membrane
Sequence Length: 648
Sequence Mass (Da): 73240
Location Topology: Single-pass type I membrane protein
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D8LMP5 | MLPQTMINDCESNDPNSLDNNNQDAGAAATATDNAVNAAHPRTKRKNPEKVDDKARCPICQDLLPEENRGIVKCGHVFCLKCVLQWVKKQQNSCPTCRAKVCHIKKTLSLAEALEKNANRKPLTKAQLKRTKRKSTIGKPFPKPDITTEKIRVHKKVSREQIRQNAMAPHPQAPGGFLHAQEQAEAAAEAAQAVPDAQPDQVEAIVDQQVAIAVFSSSPPPPPATPQVPSPLPPSSPRSLATDLEDRRVAIEADRRALLESTSAFRGHRSVGGGSYVGGAGGARSIGDSGGGVGDRVGEASLDVRVENNSGGGGGGGGGAVGGRGWRSTVNIGNSSSGVSSDGGGDGSGNSDADNSNSRNNAGVRTGGAAEAAAQESSSNRDVQGAATSSGGDNLDHDDDDDDGTGDGVGNITTLGHLLSVLGSRRIRVSPNGGIGGIDDGGGGGGIAAAAPSSVPCSPLLPSYSRRSNNNKSISNSSHGVGNPATDPETRSAAQAAMAVSRAASRYTSLVPEQALAVQGLAALESSPTLRQLRAVARLVVGGSASAGMAGAPALASVSRRRQPQDGLGQESRQDRDDEAGVFGRRDGGKSNGEERGNLLPRIDNDDNRSDNISSRGGGNGSEEEPCVEPASRRTAVGERDVSHTEERDEFAFPGRNDNDTTAGGTTGSASPILSDSSATVACGSSTSIPESFAHTSGNDAAPSGSINDGANTAVAGAEDACGGDADGAGVAGSDHAGGGISVSANGAAGPGGVAINSGRVHSSPLSSNNNNNNNNTCSYLTWLESRSDFNHWPSPSSDDDDNAASD | Pathway: Protein modification; protein ubiquitination.
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: 807
Sequence Mass (Da): 82124
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A0A1G4AYZ1 | MELFSLLALLSIAVTHCSAAFDPTSKNNVVVYYGQGPNQRDLIYQCQQPEIDVIVLSFVYLFPAQANGYPGTNFGNRCGGQVYPGPGFNGVNDPSENELQSNCPTLNAQIPVCQQQYGKKILLSLGGGVTSYQLTGKNEGELLATYLWHMFGPKDPNWTGPRPFDYNGQAVEVDGFDMDIEHPSTDNSQGYIALVTLLRSFYATASKQYYLTGAPQCIVPDANMAAMISAAKFDMIFVQFYNTPSCSAATWVSSNPSYTPGQTYQQAGFTFDAWVQWLSNTPSRDAKVFITLPASPDAANAGNYITPQQANNLISAYYCRPSFGGVAVWEATRGDNNPYNGKSFQATMKVWLQGAAADPRLASCQAPTTTTTPAPAPSSPPPNTPNPSTQPTTPAQPNPGAPGACGSGIGSCGSGYCCSAYGYCGTSSAYCGTGCQPGFGTCSGGGSSSGGSSGGSSGGSSGGSSGGSSGGGGSSSGGGGGSGLPVATDGSCGAGIATCRGNGAYQCCSRNGFCGNSDLYCGAGCQPSYGICS | Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
EC: 3.2.1.14
Subcellular Location: Secreted
Sequence Length: 533
Sequence Mass (Da): 54841
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A0A418JJ38 | MERDKNNHLSHTLNIKWNRDIILAIILGVLGSSVALAMFFLSGYMITESALGAPLFALMGLIVTVKLFGFMRAVTRYYERLFSHRATFTMLRDVRVYFYQALIPIVPNVFRQFKTSDLLGRMVSQIEALQNIYLRVYYPPIVMSLTGGLTICVLLYFSVWHALTLLIVMSLSLWLIPWLSAKRATVIKKDIDDTYQKLMHRYFDYILGYDELMRFNQNQSYEGRLLRTEEALSNAEYQEQMFHIVYQYVLNIISMIAIWGSVCLIIIQVNAGTFDPVYATSIVLMLLTLFEQHVMMSQVAYYKSETDEATHQLNDVMSVAQLDEGKDRIEVEQIEMRASLFCLKNVYHQFPTQQRATLKGVHLNIKKGDHIAILGTSGSGKTTLLNILLGLYPISKGHMTIGGKPHFHRTHWLTQVNPLLQDAQFFDGTVKDNLLSSCNEVDCLNALRKVGLDHIPLSREVTLNKNALSGGEFQRLAIARLWLKQAPVWILDEPTKGIDAKRVVHIMQQIHDTAETLIVATHNLDILRDFDAVYKIEEGILTRVDPESLTVNA | Function: May be involved in multidrug export. Transmembrane domains (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Location: Membrane
Sequence Length: 553
Sequence Mass (Da): 63155
Location Topology: Multi-pass membrane protein
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A0A6N8U8T8 | MERAILHCDLNNFYCSVELVKHPRLKGKPVVVAGDITKRHGIILAKSYEAKAYGITTGDALYEAYEKCPDLIAVDAHFEDYLYYSQRVKAIYERYSDQIESYGIDECWIDVTGSLSYFGCDANILADRIRKQVFEELGLTISVGVSWNKVFAKLGSDYQKPYATTVISKDNYQQLVWRLPAQDLLFVGRSSAEKLYRQGIYTIGDIARNEASLMKQLLGKAGEMLWAFARGMDVSKVALSDYMREIKSVGNSITTVRDIYTEEEAKLVFYVLCESVAERLKRQGLEGRTICIYLRSWDLHSFTRQVTLDDPTDICEEIMEQVMMLLHRHYAFKEPLRSIGLQVTQLKTKQRPVQLTLIGDQKRRSRSRTIDQVMAAVRERYGHASIKRCSMLLEPELTAFDPLHEHIIHPEIFIR | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 415
Sequence Mass (Da): 47727
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A0A8E8PWL1 | IISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLMMNPAWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVNSTNGSSISLL | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 207
Sequence Mass (Da): 22947
Location Topology: Multi-pass membrane protein
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A0A3N9TCD7 | MLNPILTGLYNLLILIVSPIYLTVLIRKMSSLPNAQHRWLEYIGLGKIESESTRPIWIHAVSVGESMGIIPLIREIKKSHPAKCIIVTTTTSTGAQIIMSQLKDDVTHYFMPFDIPWCVRRFVTKINPETFIIMETELWPNTLSIVNSLSIPITVINARMSEKSCKSYQKLGSFFRRVLNKIDHIVCQNTSDRERFERLGMDTSKLSVSGSLKFDIKIDDAAIEKGVNIRSEFGDRPIWIAASTHQGEDEQLLTVHQQILKQLPNALLILVPRHPERFDSVFKLCTESFDTVRRTGKLPVKSSSQVYLADTMGELIALFAASDVCFMAGSLIGDKVGGHNPLEPAAVGLPVITGPSYYNFKDIYRCLFELGIAFEKSIPTEIAKTVCSHLENKNKLGDIKIKAKTFVEHNRGALHFTSSAILQYSNDTVDTAE | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 433
Sequence Mass (Da): 48541
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A0A834KET6 | MILGWYSVLLATLLAFLIYIAFFWKINWIRDLRCENKIKYRKMEKLPPVYPNGWFALLESSQLKVGQVKHVSALGENFAVFRTEKGIVNILDAYCPHLGANMGEGGRVKGECLECPFHKWLFYGNDGRCIDIPYANKVPNVAKTKAWRSCEVNKIIFVWYHAESAKPDWQPHPHEKISNGTWRFQGRNEFIVNCHIQDIAENGADLAHLSAVHGPALFLSEDVMRFVRHRWSNAGWTPHSSESNDDSSKTPTEKNIPEEETMWEDDLTKKTSTTKTTINGDSKNMLNGRTTMTTTATATIANGQQNSYNGEKHRASMTLRHSLLLLDRFDILELNVKVEQIGPGYVELFIETTFGNMFILQTVTPIEPLLQRICHIIFSPPLLAPYASIVFLGECLMFERDVAIWNHKRFETRPILVREDKTIAAYRKWYSQFYSTNSPTYQTAMKSLQW | Pathway: Hormone biosynthesis.
EC: 1.14.19.21
Catalytic Activity: cholesterol + H(+) + NADH + O2 = 7-dehydrocholesterol + 2 H2O + NAD(+)
Sequence Length: 450
Sequence Mass (Da): 51750
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D7FRS5 | MKYAWLALCLVCGCWAAQGSRGKGAAGTELIITEQPVVAIWAHPSNSSLPDCGGDCDFVKAAYVNWLANAGARSLPIRYDATPEELRPILDQVNGLLLPGGHPLLPEGVRWALKYAKELNDDGDFFPVWGTCLGWEWMAQTFAGDYPVVTDDFDAENFTQPLGLLADAGESRMLSGVPTSLLEKAKVKPLATNAHHKGVSPGDLVESGLDTMFRVMAINADRQGVRTYVSVAEAIDYPMYGLQWHPEKSQFDWGLDPDGTPHYVINHSKDAVELSQVLATFFASETRRNGHSFTSISDWEPGMFHNRDVTASGPINGQMYGFHLSESGRTKSALAPTKDLRRQRHSQQFGRGVSMEGGRAQPPLQQSSSNRHRPLLRET | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 379
Sequence Mass (Da): 41626
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A0A1F8R7G5 | MRVALSFGLFQAFMTLVGWLAGRTVIGFISPYDHWLAFLLLAFVGGRMVWESFRDKDPGGKRTDITRWGLLLALSVATSLDALAVGLSFAFLKVNISLASLIIGLVALAVTGIGFALGKKLGAVVGKRAEVVGGAILIVIGLRILLENIL | Function: Probably functions as a manganese efflux pump.
Subcellular Location: Cell membrane
Sequence Length: 150
Sequence Mass (Da): 15956
Location Topology: Multi-pass membrane protein
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O03495 | LALAASVLILFLTPLLHTSKQRTMTFRPLSQLLFWTLVANLLILTWVGSQPVEHPFIIIGQIASLTYFTILLVLFPLTSVLEN | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 83
Sequence Mass (Da): 9319
Location Topology: Multi-pass membrane protein
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A0A8K0GZU0 | MQVCHKCARWTCNKRCRSKGMVSINREDKINFIKDELSKESLDNILLTLETHPCGVEMEGASVCRFTNICVFCGSSPGKDKEFLKAVHTLDRMLAEKKVHLVFEGGSLGLMEVVSLAAHIGGSNVLGLLNVNKFFNGLLSFLDHAVEQNFISYSAQQILISASTADELIDKLQRFIHVPDPVMAQLDWLERTVAELRTRTGRWNEELLRDLFEQHSAQEILKLEWPCVPRQDKVLWMGNALGVVESAEHVFRDYHVIGAITFRSKWGIDWDCFNNYDIYILINFSLDPKRGINDIIRVVHVFESAVEEYDKLLQLKQNFDNFIKKQQLPFPNIMPPIVAEMKALEWASNLALKENWMKANWFSDSQLVVKEINMEFVLEKQKLERAC | Function: Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
EC: 3.2.2.n1
Catalytic Activity: 9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin
Sequence Length: 387
Sequence Mass (Da): 44523
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A0A141QD47 | IFGSWAGMIGTSLSLLIRAELGNPGSLIGNDQIYNVIVTAHAFIMIFFMVMPIVIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLSLLLMSSMVESGAGTGWTVYPPLSANIAHGGSSVDLAIFSLHLAGISSILGAVNFISTIINMRSIGITFDRMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNL | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 195
Sequence Mass (Da): 20811
Location Topology: Multi-pass membrane protein
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A0A2D4JXZ0 | VEDTAVVEKTKEEIIAKLQGRYGCCRFLRDGYRTPKEDPSRLYYEPAELKLFENIECEWPLFWTYLIIDGLFSGNAEQVQEYREALEGVLVKGTNGLRLVPELYCVPLEEVEEEYSHPHTVERLPVGKLPLMWAQSLYILGCLMAEVSFDPALALSCLELSVGGKGHRQPPPREA | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 175
Sequence Mass (Da): 19933
Location Topology: Lipid-anchor
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A0A7W5LHD0 | MKAVASLAFSIASATSLCVGGASVASHMVAQPNRAALRVEEEPDLWTAEPRPVDLSKQRYQRLPPLLSSYAEDQLRNQLRTAKTVTSRPSTDEARTLVDSTTRHTEWCTARYRSYNAKTDTYLSFSGEERPCISSPSDEAVSPFAASRPSDDHVAWCSTRYASYRLEDDTYQPYSGSRTKCISRIARPAPEQVTASGY | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 198
Sequence Mass (Da): 21937
Location Topology: Single-pass membrane protein
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A0A399JEX5 | MGSGKSSVGRELSRALNLPFVDLDEELVSRHGPIPALFAARGEAAFRELESAALAAVLAGPAVVLATGGGAVLAEANRAALAEHTVIRLTISPETAARRLAGDATRPLLAGDHPEEAWARIARERAPHYQAVASHTVAADADGPQTVARTVLTAMRTEPEEHSS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
EC: 2.7.1.71
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 164
Sequence Mass (Da): 17068
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A0A4Q4UZI5 | MDWAFANGLLNWSGQGEEIQAKAIHPSLDYDALQSRHFQLLKASESVETIIDAAMVHSFDKSGTYSFVVEGPIPLAVAPSTKLSGPPAYVKSNAVSMHVEAREASFQGRRSIEGRTNLDFAGCNGTKHEVITAALSNCNKLALAAAADARDPTSARFVEYFKSNSSATRREVVERLEAAAAECSTTDSGPSRLFCYDYYEACETDDGPLVAYTLWTFDTMVMCPLFYERPPLPTGCHRQCHATTVIHETTHCGGVYSPMTNDFAYGYEEIMALKPDWALLNADTYSLYANGHKAQDNKLEAAAVDI | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine.
EC: 3.4.24.39
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.
Subcellular Location: Secreted
Sequence Length: 306
Sequence Mass (Da): 33494
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D7FVJ5 | MSGNEAPRSKSIEEQTRADSRRRRQERKKAQLGALKTGVWDRCLYRVPGKGRYCAQHRSKHSASFCGTHMGETAEKGKRVPCPVDPNHTVFEQQLSSHVKICNLALQQARMVAQPYYSEGINSGPPLLPGEEEEEKNKEKEEEDRGDVAVVAAVAAAAALDDAFVVDLLSRVEAAHRDLVGEIPTEVLDPPEVQALHRGLVGPAGGDNGHGENGPSVLHVEMGAGKGTLGQSIATAFPGSDVTMVERSSVRRKAENRLEGVSTRARIDIRDLNMGGLPSLTAEGDDRPVVAVAKHLCGVATDLALRAMLTLPPRPESRDADDGGHVGNGDPTAAPAAATTRVGGVAIATCCHHVCNWRDYVGRDFLTQQGFSARDFEAMRRISAWISLEPDAGARKNNRYPDDRHPGVTSSPSFCRKTPGETASVAARSRRPAAETRKLEPVLEPGGGDCPRPGEREAYGWSGGGPGEAREGTWTEQLCGEREDSLERARETNRGHSSSPPWHTTPAPTFMTASTPSSLHSPTSDNANANTSIGDGSDVLDANTSIGNGSEVLAPLTPSEKAVAARGCKRLLDRGRRAFIEERLGLRSEIVHFVGSDVTPENALLLGFRAEEGP | Function: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
EC: 2.1.1.225
Catalytic Activity: adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 614
Sequence Mass (Da): 65792
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G9CI92 | FGYLGLVFATFAIVRIRCVVWAHHMLTVGMDLKSTVFFIPAPMIIGVPTVIKVFSWLFMLSCNNVFKTDHILWRAVAYQLLLLTGGVPGILSPASI | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 96
Sequence Mass (Da): 10653
Location Topology: Multi-pass membrane protein
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A0A2D4L073 | KKLYPNMAMKLKVSPSSVPSLSISPETLSLTPSVDIQAFAILPDSSLAPLFVIEATSPVSAKIDVNSTRIFGNLKLGRLKFSLKHSDVGIFSVQLLESLINVLTASILIPQMNARLAEGFPLPLLDHLELSNPVLQAHQDFLVFASDVRYG | Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular Location: Secreted
Sequence Length: 151
Domain: The N- and C-terminal barrels adopt an identical fold despite having only 13% of conserved residues.
Sequence Mass (Da): 16383
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A0A4R6U7G9 | MQHSAKPQSHRVIFHIDLNSFFASVEMLLRPELKKHPVAVARTSSQRLGIVVTSNYLARQQGVKTTMPVWKAKQHCRDLVIVPPHFDEYRAYSRRFFSLLRTYTDAVEPASIDEAYLDVSDWRGDYVALAKTIQDELLDKVGLPCSIGIAPNKFLAKMASDLKKPLGISVLRKRDWPRLFYDKPIEVIHGIGEKMGEKLRQAGYDNVQQLAEANPAKMAELFGPKSIRLIDKAQGVDDRMVDPERAEKRKSVGVSSTFDADLRTLSSCERELKKLAAKLSERLSDKQLAGFSLTVQIKYASFETTSKTTSFLSPLSSETDIVEQAAALFTLLWNKDSVRLLGLSIGKLVSDQQQSTQLNLFTFEREISQYEQRRKREEEKE | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 381
Sequence Mass (Da): 43256
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A0A336MZ97 | MLNQVAVEALYSATYVENYLDAVENLPDEIQRYITRIREIDVKHRSYLRDVDIFYEQWANCPTNELESTNATKRNRAMTRIQQSLIAAQELGDEKLQIVQQLTDLIETKTRQLDQNFKNLDYASGHNSSRDTREDTPPQEEAIDPDEPTYCLCDQISFGEMILCDNDLCPIEWFHFSCVGLATKPKGKWYCPNCRGDRPNVMKPKAQFLKELERYNKEKEEKT | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 223
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 26069
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E6SKT9 | MDRWVLHCDLDAFFAAVEQLDRPELRGRPVIVGGDPASRGVVATCSYEARAFGVRSAMPLAQARRLCPHAVFLPVRRERYEAVSRQVMAILARESPVLEPVSIDEAYLEVRGDGVAAARRLREAVRREVGLAMTVGVGPNRLVAKMACQRAKPDGLLAVAPAEVEAWLAPQPVEALPGLGPVTAARLRQAGIATLGQLAAADPVVLHRLLKGRAAELQARARGWDPRPVGLVAPARSLSEERTFPQDRRAQDVLPVLAELCEELGGRLRRQGYEATQITLKVRYADFTTVTRSRTLPRPACADGELFAAARELLARHVPPERWLRLVGVAAGGLIHQHDPQQLALWPGDSRSRRLAQAVDQVRGRFGRHAIGLAARWLPGAATGTGQGARRAPASRPVARARYPAAGGAGRDGAGTGPERGPAAGRMRGLAPTDAAPGAGVGTAPRTRPGGPRRAGSSPAGEPAGGGRP | 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' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 469
Sequence Mass (Da): 49794
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B4RHL5 | MQRSMGRVRREWRDQLSRYGAALALVAASTAVAEALYRLTATTRLSMVFLAGVLLAAFLLGSGPAYFAAAVAFLVYNFYLVEPRFTIELTTPEELLTLLVFLAVAMLTGNLTGRVRDEAARAEARARATTALFDATREFSASSDEGLIRQRLAEHLAATAGGEGFVRDAGRLQMAPAGLRREDIPGGLPGAAEPAGGWTLRRLEVEGQALGTAGWRAPPDRRLSRDEHDLLELMCDAGAAAIARARLAAGKAEAEARARTEDLRNALLSSISHDLRTPLAAILASATSLREFGDSFDPGVRRDLAATIQEETERLDAVVANLLSMTRLQAGALAIQKAPFNVPEVVRRTVERRDRAHRRFTLTSITPRLPEGLGDPILFEQALGNVVENALRHTPEDTLVLVSMRLEDDRIVVDVCDRGPGVGEADLERIFDRFYRAGGARQTPGTGLGLSIARGLMEAMDGAIEARNDPAAGGLVVSLSLESAA | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 485
Sequence Mass (Da): 52173
Location Topology: Multi-pass membrane protein
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A0A559M4K4 | MIPSDWRFWSPSGALFPGGPYTWHIIDWDQRRWISVTGSEEALPDDEDAINILSKHIDHLDLDVFEIKVSDDGELLSTSSNLKDDATWAIHYPRYNVSSTPSMEKDTLTRSLLEEVDRLGPEVDLVRYADESGISKLVVFKYAMIEQHLRRMWKELHIIKSLPQHPFIVPLDRIVLDDTEPRILGFTTPYVPGGTFADNQTRPFRFKWLQQLTSVVDDLNLKFNITHQDISPRNLLVDPVTENIQLFDFDRAAKIGSQGEDRRRNDVDGVIFTIYEILTLDDHFRTIPFDQQDVKNVEEIETWDVKAPVEAGTGGVEAFRKFLQEWAQGRRAKPLELFSEASSPLDWPEYPPDTPIPYVSYPDSDNEDGAEPITFPGGARTRTDARRNGQHVVCWERPPSISKFEIETARKGKRASNDGDISNDREKRSKAS | Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. BUD32 has ATPase activity in the context of the EKC/KEOPS complex and likely plays a supporting role to the catalytic subunit KAE1. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Chromosome
Sequence Length: 432
Sequence Mass (Da): 49510
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A0A3P7LP80 | MIALALFGDQPKNSKVIEKLGISVTLKKSEINEERVTVAIWEVLENKRYSSTVKRLSEMARKQPVSPKEVLMKWTECLADFKTLDNLRQLE | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 91
Sequence Mass (Da): 10492
Location Topology: Single-pass membrane protein
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A0A3P7IHU4 | MLWRTLCADSVKYTYPVAACDYFDKIILIWRTQSQSVNRRLFGSVTVKSDFEDYSAILQTALELVSAVSFDPKCEVRKLIPKDALFSQKCYEVSYYEDELVVVFIPVQLDLCNNKKTAHIPFPYKLSCQVLSEFRQVEIVCLRLILSVPTCVADTDCRWLLNTVFPALHKWLQFIDPHKTVRKTNNLLDLEEYSHRYKRIKEEYGRKLVESWTEKTDPKKFVYEDCGIAAYLLELWRKRGRFPRKFADLGCGNGLLVHLLNKEGVSGIGIDIRKRKIWSEQFSESSLIEQVVDPSQKETSIPSDVDYLIGNHTDELTPWMPIMAARPGDSGSQYDSFLKFVKEVCVRLGFVVEEDRLSIPSTKRLCFVCNIPPQGLVPNVEEVIQELTGSSSKGFLARPKVEQIRNCLNVPAEIRLDLINRFFDKILYSSNEERDGWRCGGAIELSELATMLTDEEKQLMKQQCGGLQTFLRNQHQVFKVRSNICRSFLLLCFEVRVIYFFCYLAVFKLLHFHILVCSKRASLTVCK | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 527
Sequence Mass (Da): 60875
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A0A4V1XD99 | MVSLVWGASLARSAVDLNGAQVVAPVIEDDPSPITDNNAGVAATGAPVENPKKWEELLDASLDIVPACAVTGKELQEKLALSASGSGGKGSGGEVAILLEGMRKFFNAEDNYDENFLFAYYRQTVASVYIGGGLGKPTIGSAMETLAARLQTGGSIPGRTVAQLCNGGRQPERVFGVFIDITGDLAGVQKTAWDWSQGNCAADRELVSAGVLPSIKHIQVVAGDSYAFLAFKYGINGADFTKYNLKKDLCSTFMPGDYVCYSAGDPYTEPKPNPPKAGPDGTCTTHLIANRDSCAALAKKYGLTISQIKRFNKGKTWAWTECTAMLSGYNMCLSEGTAPLPPPQQGTECGPLVPGTKPPNNKSILLADLNPYPLKACCNNWGFYSPFAAHCEIHAPKDGGPDSKLPGFQRTYVSNCGTEIKQNSGPPAAFERIGYYKSWNLERDCLWLKAKNVNNDLSYTQAIIDNRKKFATNLAQFVKNKGLDGVDIDWEYPGAPDILIGGQPIGKPGDGVAYLRFLITLKSKLQNKSVSIAAPVSYWYLKAFPIDKIAAVIDYIVYITYDLYGQWDYGNVNAFDSCPSGKYIRSHAGYISNAEINKIIRRGDGARTFHDGGSNTDIMLYQGDYVSYMTLTTKNTRRADFKGLNFAGSIDWAIDLQAFISDNFESASGNGAPGKEGCVMGRDESVNSGYLCAFSCKYDFCPDSLCSCRVTGPIEPPPPEVKGMDDIIAWDELNLDLNRLCRTRAG | Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
EC: 3.2.1.14
Subcellular Location: Secreted
Sequence Length: 746
Sequence Mass (Da): 80656
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A0A0R3L5Q6 | MKAWRYVGKLLSMRDGEADQFSQAVDNATAVLRQALQQEHDRAEALATELANARRAMEQIPAAVDGRPGVSLPAWANSYALVKPAQTAVQPDVARENGKSAIKPGEPARVEHKPRGGYGCQHFRTYDPASGTYMGYDGRRHSCP | Function: Has immunoglobulin-binding and hemagglutination properties, and can bind to mannose. Essential for virulence. May be involved in LPS biosynthesis or polysaccharide transport.
Subcellular Location: Cell membrane
Sequence Length: 144
Sequence Mass (Da): 15736
Location Topology: Single-pass membrane protein
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D3ENP3 | MIKTRKNYLRTFLNIIFISSLVLTGCSEISSKFNSSDSKREINSTQQMHQIDVNNYTPRLDSTAVVEMSINDSSIIIEINGREAPITAGNFIDLVERGFYNGLVFHRVIKDPTPFVAQGGDPDGTGMGGFVDPKTKQRRYIPLEIKLENDEKPIYNQSLGIQGSASPKSVVLKHKRGSVAMARSAMPDSASSQFYVALSDLDFLNGDYAVFGTVIEGMKIVDNIKEGDRISSMHVISGLENFKK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 244
Sequence Mass (Da): 26992
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A0A8K0MPP3 | MKEGGMDAIKLEGGSPARINAVKAIVEAGIVVVGHVGLTPEPINSVGGFIPQGKNAASAIKLVETALALHEAGCFVVILECVLPHMAVATTSALRIPTIGIELGLFAMVKCKSYLRKNTIDCLKTLIPLPL | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 1/2.
EC: 2.1.2.11
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 Length: 131
Sequence Mass (Da): 13626
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A0A8K0GY66 | MAKPRYSRLPSRKTSSSTLVLTLLVMFTFALIILLALGILSVPSSSGDFAKANDLTSIARNSVDRCTKDECEYLIELAKPKMQKSTVVDSETGKSKDSRFVLCISSLFIFELWNILARGRDKIIRNIEKKLADFTFLPVENGEGLQVLHYEVGQKYEPHYDYFLDDFNTVNGGQRMATVLMYLSDVEEGGETVFPAAKGILALFLGGMSCLNVAKGTFCQT | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 221
Sequence Mass (Da): 24548
Location Topology: Single-pass type II membrane protein
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A0A3P7IK59 | MCLLLREENIMGEYFDHILDLLVQLKNGHVNGIRVRMGRVHQLLNTSCIEHIDFATSDDVEFDIDVLEETDGNNQILSRLSLRDGIEDDTTVEEDVRVLKDDDLYEIIKKEDMEKPRQLAFALAAMWSRRHPDTPLDGSSIRERMERLYRRVCQLRLWWLVRYCAGRLRKVMNSLAPAITNMLVRGKQVTIGVRGVHEEVIRRPISPGELTNLLFACCPQDEPQVAVMQQELIIACSDLVRISEFSAISIYLHFPTQMGHSPTAFDGVLTIRLSWLADAITLLLNYVRTTGSLSRSGGKLVTPATPTTTGIPEVKVNDENISHVNEDALPDDDLIAFGNLCGFGI | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 345
Sequence Mass (Da): 38955
Location Topology: Lipid-anchor
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A0A2T0ZW87 | MTGLTDQNEITSVVSTHVLETPDFPSEGVLFRDFTPLFCDGSAFARVVDLIAEQVTAKGGVDLVAGIEARGFLLCAAIGYKLGAGVVPIRKAGKLPAPTVTESYALEYAEATIEIGPHAVNKGDRVLLVDDVLATGGTMVAAATLMRKLGAEVVDSWVLLEIEALGGAKAMQAADLTFNTAMTV | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from adenine: step 1/1.
Function: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
Catalytic Activity: AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine
EC: 2.4.2.7
Subcellular Location: Cytoplasm
Sequence Length: 184
Sequence Mass (Da): 19182
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G8PBX7 | MKHYIKLFSTILLLGLILAGCMSNDNQSKDKMGTIKTGIARSTVFALVSSAENSTTDYTKQYSYIEDIGDGRGYTGGIIGFTSGTGDMLAVVKKYTHLRPRNNILAKYLLALKKVNGSASHKGLGKNFIVAWKKAADDSRFIKAQDAILNEQYMQPALKYSKKDHLGQLGQYIYYDALVVHGPGTPKEKNTFQGIRHQALKYAKSPSEGGSQHAYLLAFLRARKPIMREEQAHHDLSRLNTQRQFIEDKNYSLKLPLKWKMYGDTYSLTKKQAADFLQKTQ | Function: Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.
Catalytic Activity: Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan.
EC: 3.2.1.132
Subcellular Location: Secreted
Sequence Length: 281
Sequence Mass (Da): 31612
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A0A2P1J271 | FIFGAWAGMVGTSLSILIRAELGHPGALIGNDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLSLLLTSSLVENGAGTGWTVYPPLSANISHAGASVDLAIFSLHLAGISSILGAVNFITTIINMRSNGITFDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTD | 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-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 193
Sequence Mass (Da): 20624
Location Topology: Multi-pass membrane protein
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A0A336M7X6 | MESNKLKSIKEFYNGKIILVTGGTGFLGKTLIEKLLWSCDGVEKIILLLRSKKGKSVEDRIASLKREVAFQRIHEKKPSVLDKIIGIEADLSAGSLKFESENGDFVSNELRNVNLIFHCAASVRFDDPLKKAILINVCATKALLDFAKTLQHLEVFMHVSTAYSNCDRFEIDEKLYPASVDWRYAIKISEQFDEEILDALFYKFSNNMANTYVFTKKIAEHMVDDYKNALPIVIYRPSIVTSAEVEPLPGFIDNFNGPLGLLVATSMGVNRTSWQSHKAAINATPVDMCIKGIIIAAMRCPESWKETKDIQIYNAASIKTPTYLHMIKKGKRFIVKDAPLNIFIWRPGGRITQCYYEFYLRFMLTQVLPAIGADVVLKLLNRKPFFLKLQRALMTVQKNLHFFMNNTWEISNHNFLHLNEFVPASELIDFEIKEVYPEYIEYGTLSLMGARRFLLNWPDEDLKKARRNYRIAVLIDSILKYTILSGIFWYFYRKYFFSGREIFLTGGTGFIGKAVIEKLLRSCPDLSKIYILIRPKRGKTLNERLNTLKSDILFRKLLHANPHAFEKVIGIKGDVTCENLGISPPDITRLENVSIMIHSSASVRFDDELKDAILTNVRSTYEMVRIGLTLKKLDAFIHISTAFCNSDYKVIEEKIYPEHGDWKKAIKLALNMDRDILNSLTMKLTDFLPNTYLYTKGLAENICNDFKEHLPIVIYRPAIVTGCEVEPIPGFVDNFNGIVGLAVASGTGIQRSLYCLRDAELFCTPVDTSVRGIISSTWRKVLCEPKHDLSIYNCSNGTTSITEIMSVSYKFIEKVPLLNTVWTPTDIATTSLCWDYICAVFLHFLPALLIDFIATHFMNQKPILLRVQRKIRHAQLALRYFIINKWIIRNDNYASLSSCLKDCDKKSFDTSSDAIENRKQYIIDQILYCRRYLLNQPDDTIPAAKAHYWRLYVLDKLLKIGFVILALYGMFKLLKFLDVIKI | Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols.
EC: 1.2.1.84
Catalytic Activity: a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH = a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Sequence Length: 982
Sequence Mass (Da): 112626
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Subsets and Splits