ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A2E8S0S4 | MFYGSDPACSFGYRSLCSSAMGGQKTITLTISTLEAARIRSLLEHGDFEFGEAPYALWRARGTDCTATFYTKGKVVLQGAGAQEWAEQIDAGQTLSIVFADPFQDAMDLHPDPKPPRWIGIDETGKGDYFGPLVVTAAAVNRDQVDLLRELGIADSKKIADAKIKKMAADLKACCSYEQIVIGVARYNDLYAKIGNLNRLLGWAHARVLENLLEKEPDCTFALSDQFARDERVVGRYLGERGRSIRYHQRTKGESDPAVAVASIIARAEFLWQMKRLGEKAGFTVPKGAGAGVITAGRRIIEEHGRDALKDFAKLHFSTTDKLGATD | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subcellular Location: Cytoplasm
Sequence Length: 327
Sequence Mass (Da): 35872
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A0A5C3ESK0 | MPDVEEPPLRPEDAVHLLPLEVGPRTYVDIFRAAIREEVAEFLGTAMILLFGAGVQCQVQLYGAGNYATCCLGWAAGVAVGAYIAGPTSGGHINPAVTISLALFRRFPKNKVPKYILAQVLGAMFGACTIYFIYRDTIVILDPNSTSPLFGSNSAAGSFVTHPASSISGFTAWVCEFGATAILVGAIFALTDARNPTGFSVPLGLFILILGIGASFGAQTGYAINPARDFGPRIALTLLGYGGEIWTHDAVYWLRVPWFACLSGGVFGGFVYDFLLNTTDQTVFNNPHIELA | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 292
Sequence Mass (Da): 31095
Location Topology: Multi-pass membrane protein
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F0K3G8 | MSKKIGILNLMHDKIDTQKRFSHVIKEASPETEITYFYPQSHYLNRPRPQNWPAEPLNLKTVAKLNGFIVTGAPIELLPFSEVDYWEELTKLFDLLKAKNIPQLYVCWGAMAALYYFYGIGKHPMPEKIFGIYPQEILAPAPLLSGLITGFLAPHARYAEMNRSEIEQEKALTINAATPDGHLTLVTGPGQQVFLFSHLEYGPQAFSKEYQRELSARGGDDRKIAKPQRYFADEAAMSLPQFTWESSQQHFFKNWLQTIK | Pathway: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-serine: step 1/2.
Function: Transfers an acetyl group from acetyl-CoA to L-serine, forming acetyl-L-serine.
Catalytic Activity: acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
EC: 2.3.1.30
Subcellular Location: Cytoplasm
Sequence Length: 260
Sequence Mass (Da): 29782
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A0A7Z9HWB6 | MQNEASRAMDGSKKGDTCMNGLLHKGWILLVLGVVMTGLSGDEGVQAAKKQRKGDTPPKPVISDNTRAGRSMAMGRNGMVASSHYLATQAGLEILQSGGTAMDAAVAVAAVLGVVEPAMIGIGGDAFFLYYDAKTREVYSYNGSGRSPMGLSREYFAAKQKRRIEGESWEAVTVPGAVDAYAAGLERFGKMSFEEVLAPAIKHATEGYPVHEVVAIVWNSQAGKLGRDEWAKKLKLVDGKAPKAGSIFVDAAYGASLQSIADGGRDAFYKGPIAKEIVRYSHESDGFLTTADFENHTGEWTAPVSTNYRGYDVYQCPPNGQGSAVLSMLNILEGYDLASMEFNSPAYLHFLIEAKKLAYADIGKYFGDPERGDIPVAGLLSKEYAAARRELINPRKAAERVEPGIPQNGDTAYMTVVDKDGNACSFINSLFGPFGTGIVGGSTGIALQNRGNGFTLRKGHFNEYKAGVRPFHTIIPGMVLKGDSLYMSYGLMGGSMQPQGHVQFLLSHIDHGFTIQEVAEIPRFRHQSGLRVLLESGTPESVFKGLKKFGHELKPGSYLSMGGAQAIMIDPESGVYLGASDPRKDGVALGY | PTM: Cleaved by autocatalysis into a large and a small subunit.
Pathway: Sulfur metabolism; glutathione metabolism.
EC: 2.3.2.2
Catalytic Activity: an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Sequence Length: 591
Sequence Mass (Da): 63389
|
V8P177 | MALLSPRVSARAAYLSSFPLGERDQPKRSPGPPRGLSLSLKRRGVKKRQPKGSAARNGPVASDGEQPRDAFPLSGTKEKRKPKRNNISTCKYLAPLQSRQKALRRKAERTRADQKAPEPPASAGPPYGEGGQPFYPRALSSSCSLLTLLQDLEKVQDSRERAAKLFQWLIAPISSQEFFDQYWEKSPLLIHRHNPNYYRDLFSTAEFDSILRNHNVQFGVNLDVTSYEDGKRETHNPVGRAVPAVVWDFYRNGCSLRMLNPQAFSATIWHVLSILQEQFSSMVGANTYLTPAGAQGFAPHYDDIEAFVIQLEGKKHWRVYAPRQQAEMLPQFSSSNFSQMEIGEPILEIVLEAGDLLYFPRGFIHQGDCLPEAHSLHITVSSYQRNSWGDLLEKLLPAALQMAIEEDIEYRQGLPADYLEYMGVINTDADDPRRTVFLQKIRTLLTKLMDYAPVDAAVDQKAKSFLHDCLPPVLTETEKALSVFRHPAQWENGNVQNVDVQLEKTTQICLLRYGIVRLCNEGDATLLYYTTENSRVYHKEEPKCCEIESEYIDGIEFLLSSYPNYISVNALPCGSLNDKIALATFLFEKGLVITKKPLLSGNIKINGL | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 608
Sequence Mass (Da): 68542
|
A0A956CDQ9 | MSAELTTLWARTLLHAARVSGVRDVIASPGSRSTPFVAAALAESGLAVRAVVDERSAAFFAVGQAKITGRPSLLIATSGSAATHYAPAVAEAAATHTPLLVLTADRPPELHDAGANQTMDQSWLFAERAVDLGAPDPRGLPALARRVAQAVLRARGGPVHLNAPVHKPLEPVAIDVALPEPPRLSAPERGVDAAAVRHLAERLRRAERPLILCGTVAPALPFDVALLGRVADRAGAVVVADATGPARFRAGTNIICDKADWLVMSPTWRRTLMPDLVLLVGSAPLATAWESVLEEAELHVVAPQGHPNPTSTAASVSLGPLDAMLRALADALPEAASASSYRSEWQQGQDAVNRALETTPSRGFCEADAVRVAIERMPEDSVLFLGNSLAPREANLHARARERGPRVVAQRGLSGIDGLISGAAGAAAASGAPTLLLLGDVSFLHDVGGLLTAKEVQTPLAIVVLNNGGGRIFEELPVATSGVDLRFWTTPHDLDLSHAAALYGHRFARPESPDALAAAVDDALGTPRATLIEARVTPLSWQKVLERL | Cofactor: Binds 1 thiamine pyrophosphate per subunit.
Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 2/7.
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
EC: 2.2.1.9
Catalytic Activity: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO2
Sequence Length: 548
Sequence Mass (Da): 57367
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A0A4Q5X8V7 | MSDGFSLEGRVLFLSQDPELLKAQLAGGERALGSAALAPLRDRVSTDEITPAWACYYFDATLARYCLVGLAGGAVEAGDVQRGGFEVLVAGESFGYGSSRETAPFSLKAAGIRLIIAASVEKIFLQNCQNLGIYVSTDFGLLPRLLRGERVETRELLLGLDGLARDVVAAGGLFAYNARRLRGGVAAPPPSAPPRAMTLVEKLIAAHVVGDRGELGVRSVAPGESYFVRADLRFSHDYVTAMADSLFRQGFGEDAQVAEPESLVLFRDHLTLLGEALTPRHRELKLYDHALELKRAQERFAERHSVRLFDEVAGPSGPRSYGICHNVVLDELGLPGTVIIGTDSHTCTAGALGALAFGVGSTDMANAFLTRDARLRVPETVKVELVGALLPGVAAKDVMLRLLASPEARAGAFRARVLEFGGPGVASLNLDERATLTNMAVEASAFTGVVPFDARAAAELSARRGVTLSAGACADPGAQYAAVVTLDLSELEPMISLPGDPRNGMPLREAERGGPVRIDIAYGGSCTGSKATDIDAYAAVLGAGLGAGLRVAEGVRLYIQLGSLQIRRYAEERGYLELFERAGAIVLEPACGACIGSGPGISTREDEVTVSAVNRNFPGRSGPGRVYLASPWVVAASALAGHLAAPSEAALPTGAQS | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
EC: 4.2.1.3
Catalytic Activity: citrate = D-threo-isocitrate
Sequence Length: 657
Sequence Mass (Da): 68968
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A0A970MA75 | MSHPVQLRVLEGLTPYDQGLALQRNILQQRQRDACPDTLLLLEHPPVITLGVSAPDSAIVASREALAQQGIAVHQTERGGQATWHGPGQIVGYPIFNLHHRKLGVARYIATLEDMMMRASDLLGVPAMRRTGLTGVYASASPHGKIGAIGVRVSLGVTWHGFAFNACPDLSHYRLIVPCGASDIPVTSVQQQRSQPVDVATARSAVIDAFAETFRVTFASRDIA | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 24161
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A0A956D6H9 | MSVLAVFGGSFDPPHVAHVLVAAWAHATAGADRVLVVPAGAHPFGKKSASF | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 51
Sequence Mass (Da): 5153
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A0A2E4X063 | MQRRCRMRSSRLAPGVLIRARKHSPNLWLNFSRPSMHSLCRTSSMACSPKSDLASTQAQLRVWQQAGERIGFVPTMGALHAGHLSLIQRLKQQCDRVVVSIYVNEKQFGPSEDLATYPRQPEKDQEMARNAGADHVWVARSEEVYPPDFSIALTITGPGQGFEAVDRPLFFGGIATVVARLLGLIRPDIAAFGEKDFQQLAVIRQLVKDLALPVEILGCPLVRDTDGLALSSRNAYLTASHREKALGLPKALARSCEAYADGERDVEQIVKAGREILDSHGLSCAYFCLVDPETLEECSGLLAPKQVPRLLAAVHCNSVRLIDNCALDDPPWR | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
EC: 6.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 333
Sequence Mass (Da): 36763
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A0A9E5AEK3 | MQKLPAMTRIRWPEPPFASGVYAVVDGATLGWTENAESADRLDSIVESAASYAYSALAGGAVAVQLRWKGEAIPAGFRLACARAMSKALGGVIPFIVNDDVEVATHAAAGLHLGQGDGDPLAVRSIVGPAAVLGWSTHRLSEVDAAATLPVSYLGFGPVRWTHSKSNTEPVTGWAALADACARSAQPVVAIGGLSRSDAAIARQAGAHAFAVIGAWLQADGQPLSPQQAQAAIHELAQAWAQAPR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 245
Sequence Mass (Da): 25290
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A0A3B8LEP7 | MHELEVVLVPQLQDNYAYLLICKSTQKAAIVDCPEADKMIEVIESKGVTPVAILNTHHHWDHINGNRDLIARYSKIKVYGHHSDKERIPGMTYPLQEGDIVTFGEVSAKVFFTPGHTNGHISYYFEQTGDLFCGDVMFYGGCGRLFEGTAAQMHTSFQKLGALPHETRVYCGHEYTASNLRFAAKVDPDNAIIQQKLDEVATLRAENKPTIPSTIGVEWQVNPFLRVEQPAIKQSAANTGADSSDPAAVFGAIRELKNNS | Cofactor: Binds 2 Zn(2+) ions per subunit.
Pathway: Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 2/2.
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
EC: 3.1.2.6
Catalytic Activity: an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+)
Sequence Length: 260
Sequence Mass (Da): 28834
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A0A7X7CA31 | MYSKSILDEIRDRVSIVSLIGERIPLKKAGRNFKGLCPFHGEKTPSFNVSDDKQIYHCFGCGEGGDIFSFVMKFDGVDFLEAVKYLAGLAGVELPKTKYGFVSAADEEHSKRKKWAFRINEIARDFFAATLKASVGGSAASNYLIKRGISENIWTQHFLGYADNAWESLVEHLRSKGVPLDLASELGLIRKRDSGGYFDFFRERIIFPIISPRGEVLGFGGRDISEQKGDQQVAKYMNSPDSLIYHKSGCVYGLNKAQSSIREDGSAIFVEGYMDLIALSQVGVNNVVAPLGTSLTEGHLRLIQRYTRNIVLVFDGDEAGSRAAIRSLDLFIDAGLMPRVVALPDDEDPDTFVRKYGAEKFREMTASAKSLFEFFVEKVLSETGRDAAGKVNAMGRIIPHLKAMSDPVERGIYSKVAAFQVGVEERDVARSVAAGKISVGREFLPRGAKKKMSAPASCELMLIKGLLMKPARIADVMESVSVEKFSDGWCRDIVSVLFSQTGEKDISVGDILASIDDPEISSQLREMAVAGCGCEEDEIDNLIDDCVNRLKERPAARRLKEINDEIKRAESARDEVKIFELLREKKELISQKHD | 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: 594
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): 65850
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A0A2F0ATE9 | MISLIRDFGRTTRERWVLATLAGIFNGIGFVYFGPASFIANVPLLCALKHSRSYSEAGLLAGWVGFLGGVHIYGIVNYGWFLLLGFSLYTASQMVIYGLLFRGLWRGRGGILDILIVAAIWSLTEWMRTLGPICMPASYVGNIADVDWLRPWLVLSAWIGGIGVSSLVALVQSLIFHGFISSRQSRKSISFATVFLGILGVAGSIQLNAESGGQTVNVIGVQAGLANSQYHAATADPAAQDGVVGTFETLTQRAYKDRADFVVWPETAIRGPVFRDETLQERLFPGKTDPSILLAGLIEHNKEGKRFNVVASVLPGGQVDDIYRKVRLVPGTESHLTPGRSVRAIRAGPNHVGVMICLESVYPDMARRLVETGAEFLVIASNDAGFGFSPITRHMTNRAIVRAMETRRWLIRVGQAGISAIVSPNGVVMDRLGLFEPGLLKGQIKLSQAQTLFVQFGDWWMFLIFVIVGFRGWSVRSKPSIQAPV | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 485
Sequence Mass (Da): 52971
Location Topology: Multi-pass membrane protein
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A0A2E8S3E9 | MTRPSTIIYRWLGRTPYPKGLEIQKATHQQVLDGGPPTILACEHEHVFTMGRRSSSAEILNAGGIPTVEVDRGGRVTYHGPGQAVMYPILSLQDLNLGVQEYVRMLEETSIRSLAEHAIVADRDQVNAGVWVGDEKITAIGVHVGRGVTTHGLALNVQTDLSAYQRIVPCGLAFHGVTSMARLIDNPPSVMNMADQLANQLAVLLECKLVVASDP | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 215
Sequence Mass (Da): 23299
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A0A818WW13 | MHSCRYLAVLIILFLSDNVASLAVHDTIDLNQSKPIEYYNGSLNTCSKIRSNCSSQDGLIIPLWQPQHGISVGDRIARAIVYLLALIYLFIGVAIISDRFMASIEVITSQKREIRKKNPDGTVSITTVAIWNETVSNLTLMALGSSAPEILLSIIEVVGKNFHSGDLGPGTIVGSAAFNLFVIIAICIVAIPSGEVRRIRHQRVFFVTTAWSIFAYIWLWAIVAKISPGYIEVWEGTLTFLFFPLTVISAYFVDTKVGQFMRIRITARKQVSQNDNHKSTSLPINIDNLEEKDMLDGLSKNSIPHITNDTHRNQTASSLTDGVNDQLSGSAGGGLDEAISPDQIDVQQRDEFIDIWRQLRKQYPGHDMHTLNEMASVEMMNRAPKSRAYYRIQATKRLGGGGNIRKKMLEKINEPDKVDETNKPLVLIDATSQITKIYFEPNHYTVLENTGFVKLHVLRTDGNLRNTVYVDYATEDGTATHGDDYESAEGTLIFYPMETHKQIQVKIIDDEIFEEDEHFSVRLSNLKIKDNQGRLTPGAFDKSVQLVEPSTAVVMIIDDDHSGLFVFENDEKTVVESDSLVQITVLRTSGARGRVRIPFITQDETALIERDYLTKEGEVIFENNENQKTISIQIVDRDQYQRNETFLVLLGEPSLIREAGEKDESTMTEQEKSIADLGRPRLGDKNTIRIRIQESKEFKNAVDKALYKANTAILVGTSTWLEQFKQAFCVKEDDDDDDNVVESGDSTQDNEKPATCKDYMLHFVSFFWKFLFAFVPPTSMGGGWACFCVSIFIIGLLTAVIGDLATHFGCTVGLTDTMTAIAFVALGTSLPDTFASKVAAEHDKYADSSIGNVNGSNAVNVFLGIGLPWAMSAWYHYFHNTQFVVEKGSLSFSVTLFCSFAAVGFIMLLVRRLKCFGGGELGGPTKFRVISSLLFLSLWIAYLILSGLENYCHIQL | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 956
Sequence Mass (Da): 106718
Location Topology: Multi-pass membrane protein
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A0A956BI97 | MAFSSIEDALTAIAEGRMVILVDDEDRENEGDLVMAAELVTPAAINFMAKEARGLICLTMTDERLRKLNIPMMVSDNTSPLGTAFTVSIEARTGVTTGISAADRARTIQVAVDDNSTAADLTRPGHIFPLRAMEGGVLVRTGQTEGSVDLCRLAGLKPAGVICEIMSDDGEMARLPELSKFAEQHNLPLVSIADLIQYRLQQDSLVRELTSAPMKSDFGPFELKVFSNSADNLQHYAIIAGEPSPDRPTLVRVQHQCLTSDVFHSTSCTCGSVLRYALQRIAEEGEGVLLYLQDPEHSRLENVLTHMLKQQRGAAAKRLGEEEADPEEVVNRPNPALRKFGIGAQILRKLGVGKMRLISSSPKKIAGLAGYDLEIVEQIVPSNQSEPSDAEGNIVFSDAILKS | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Length: 403
Sequence Mass (Da): 43724
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A0A140GQW5 | MKGKLICIVGGDGVGKTSVIEKVYEILTKKGLVVTKTREPGGVESAEKIRDIILNYNIDGITEALLFAGARRENVVNNIKPALKRGEIVLTDRYLHCSLVYQGIARGLGYEKVLEINRLAIEDCIPDLTIVLDMDTSKAIKRLSDRNDINRLDKETLEFKEKVRNGYLSLANKMSNIVVINSDKKLEDVVEDVMKKITPLI | 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: 201
Sequence Mass (Da): 22457
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A0A1G1WRP6 | MNFLAIDYGLRKIGLSLSEGELAQPLPILIVKNPLDAQRKILSLIDLHKIETIVFGIPHPDSIKAAKFAFDLERLSNVRIVRVDETLTTKMGQKRGQGKKAAEDSIVASILLQEYLDNLKGAEPAI | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 126
Sequence Mass (Da): 13918
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A0A524NSW8 | MSSNGHSGSGPVVEIYDTTLRDGTQMEGMSLSCDDKLRIAGHLDLVGVTFIEGGWPGSNPKDVEFFERAKDVDWKNVTIAAFGSTCRVQLRAEDDKQLQTLLAADTPVCTIFGKAWDMHVTEVLRTTRKENLRMVEESVAFLRQSGRRVIYDAEHFFDGYKSDAEYALETLRAAASGGAERLALCDTNGGSMPWEVEQMLKAVRDALPDAALGIHAHNDGECGVAN | Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3.
EC: 2.3.3.21
Catalytic Activity: acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+)
Sequence Length: 226
Sequence Mass (Da): 24730
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A0A2E6VTZ6 | MLGSKKSIWQRRFGGPMTQAPEKQNIWAIGDVQGCYESLLAILDKINFSPKIDGLWMVGDMVNRGPKSLEVLNFCHEHAQAVDVVLGNHELHLLACWNGIRQPNPKDSLSELLRDEQQKRFEPWLRQQPFYREYENHFLVHAGLSPQSSLSDFKAMLHQAHLQLRDGDLNSTLSELFQGESQLAQSVGCATRVRMVNEMGIPDHGYKGSPQDAPTGLQPWFTHESIDWPENKKIIFGHWAALGLFQNNQVVGLDSGCVWRRSLSAYNVKTGQVVQVNRVSQ | Function: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP.
EC: 3.6.1.41
Catalytic Activity: H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+)
Sequence Length: 281
Sequence Mass (Da): 31827
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A0A821BGH7 | MILFIIQQYSFRTTGILLYRGYKLHQFIDQCMGNARGSCKGIQMPIHYGSKDLNYITISSTVATQMPQAVGSAYAYKRAANEKCVVCYFGDGATSESDA | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2.4.4
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2
Sequence Length: 99
Sequence Mass (Da): 10979
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A0A7S3GU40 | MEAILKANESMIEATSKVKKQKVQQVSLSHMECVAMRLWDVQKDLRKNYDDAGLSAIEVEVRVGMIVDNYRRWKSRSPGKTAVVVDPRSNPSLRFRAGVDHIFARRLRSKLSDQMFHCAVQPLQIMRCDESDNRWTVNSKGELMMAEKKQALDQINLALIAHEYDIRINVATEIAAPLTDSTDPAVLAATGPPVNRALWVVERRKKRTSYTCKDPHMNKWRIDYTEVDIITKAAGAATPSGKIKKEIEVEFELEHAPMLEWLRERDDQQVINKTKVLAGQLIHLLDYCIPFESEAEKEASLLVVNDTYFDMEINKLDMMVKPDAVQAGRKKSDFIGAMPVNLTRQNFMEVQKTDYFITEKSDGIRYLMYVVPAPRATDPSDCIAVLVDRSKTIFKFRGCETVGKALGVGVILDGELVFNRSLKENVFLVFDALLYRGQPLVDKLFGERLETIRTTILTAFARNLPAVLAQESALNAQRNLPTLPGANPLQLVRKVFVPRREFNTLLSKMRLEEGERVFFDPENRAAAPGAPPTSRRHHKSDGFIFQPNARYVFSKHYELMKWKWAELRSVDLQIEIPMEATSNAAGGDWPIYLKCGGPDGTQINCTKRGDTNVGLGEFDTYRLLADMESPELANRNTQSPPIVEVAYDISIGMWSYLHLRKDKDKPNFIDSVMGVFMEQAESISIEELEYSLSASSHGLENDYEVQIEKMKAKLLVWQRSEVARKNGATMSAPAQRK | Catalytic Activity: a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate
EC: 3.6.1.74
Subcellular Location: Plastid
Sequence Length: 737
Sequence Mass (Da): 83573
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A0A6C0ABF9 | SVGFKAGVKEYKLTYYTPEYEPHPHDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEESQXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLEDLRIPPAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 215
Sequence Mass (Da): 24084
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V8NC26 | EYAPKFYFTCICGSNHLNYFSSSQIIRVLWWYYFSKFIEFMDTFFFILRKNNHQITILHVYHHTTMLNIWWFVMNWVPCGHSYFGATLNSFIHVLMYSYYGLSAIPSMRPYLWWKKYITQGQLVQFVLTIIQTSCGVVWPCRFPMGWLYFQIGYMISLIILFTNFYVQTYNKKAASRRKEYQNGSAAAMNGHTNSFSSFGNNVKQIKQRKD | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 211
Sequence Mass (Da): 25238
Location Topology: Multi-pass membrane protein
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K0ZAG5 | MASSKKPIFGLIGHTLAHSYSPKIHSLLGSYEYRLFEVEPENLESFVKNGEYAGINVTMPYKETVMPMCDELSDAARIIGCVNTIVRKEDGRLYGDNTDYYGFSHLVEFSGVPIEGRKVLVLGAGGASKTVCSVMTDRGAREVAVVSRSLPGAGLNTIEDHYDADIIVNATPVGMYPNCPESLVDIEPFTIAGETRKGYRDGLHAVFDVVYNPARTDILLQAEKHKVPYVNGLPMLVAQAKRASELFQGTRISDETMRSVLESIAFEMRNVILIGMPSGGKSTIGALLSKKLHRPFVDIDNHIPAAAGKSIPEIFSDDGEAVFRRIETDVTGDICKRSGLVIACGGGVVTQPRNYDLLHQNGIVVLLRRPIELLVSDGRPMSIAKGIAALEHERHHLYEAWADIAVENDGTPDDTVKRIIEALDEVSNVVKG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Subcellular Location: Cytoplasm
Sequence Length: 432
Sequence Mass (Da): 47135
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A0A816L0H6 | GGGGGFRGGRGGGGGEFNSSDRGFRGAGGGAGGNCYNWYVLFMMSCILTLLSFVNSNKPGHQARDCPQERKPRDSGSNSFNNSGGRRNNNQGSDDIFDQPGSHTSAHPTERFIPPPAPTTEDGIFGEAVTRGENFGKYHVAHVQCTPPGKLKSIELYEEANFDRQILSNIRRAHFEEPTAIQRYTIPCIRQQDDIMACAQTGSGKTAAFLLPILSNLLSYNADELNENQRPPAPLCLIVSPTRERALQTEREARKFAFETSVIPCSAVGGHDMFTVSDRLRQGCHILSAATGRLKI | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 296
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 32122
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A0A418Q900 | MASGTASGKGETGGVEAFNHAPERQAVSLLEPLFCSAQLAEQVVAARPFATADDAVDEMKELLRDLPEDAILESVNAHPPIGGSVEKGSLSESEQSAALGDQGAGGEGGGEGDGADPLTTIRALNEEYRGRFGYTFLIRAAGLTAGQILANLEQRLTNTPEAEWSEVLGNLAAINELRMRQMLESLGVTGPTLSTHVLDTSTGLPASGVHFELQLIQGVSGGSGTSSDSSASASSASSAIANSANSAEESAGVGSDATVNPGQSVVESGETNADGRFSFADRLGAGVYNLRFDTDSYFAARGIRGLYPWVDVTFRVDDVDLGAGASHLHIPLLLSPYGYSTYRGS | Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
EC: 3.5.2.17
Catalytic Activity: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+)
Sequence Length: 345
Sequence Mass (Da): 35631
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A0A956C1B7 | LDGGASHVGRTVTRLHELRPDILVETLLGDFGGHMDYVDTTVDAAPDVWAHNIEVVRRLQRSIRDVRCSYERSLAVLERVKQRDPSRITKSSIMVGIGERDEEVVETMRDLRAVGVDIVTLGQYLRPTPKHTAVDRFVTPEQFEAYAVAAREMGFAYVASAPLVRSSYKAAEVFVRSVLRPGDPEGAKVELERRLAEAQEAAARISGEDGPRTTSQLAARDGAALLPATSLVRR | Cofactor: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
EC: 2.8.1.8
Subcellular Location: Cytoplasm
Catalytic Activity: [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S](2+) cluster] + 4 H(+) + N(6)-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe(3+) + 2 hydrogen sulfide + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Sequence Length: 234
Sequence Mass (Da): 25804
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A0A0D8JVJ4 | MALLEATAGETGTSAHAGHAAEEGVASYGVNQEFPSRETAYKPCGKPTVRRSPFGGIARHTLGVLLLLIVVFLWTTSNFLASTIFADNTYSKPFFVTYLNTAVFTLPLIPYALRRGFQWWKETRANADVSHQAEDGPLEEESHPFLSSEDEPGIRHDAPGNPSASADGLPRCSKEVCEKLDFRATARLSLQFCLLWFAANYFAYACLQYTTVGSTTILTSTSGVWTLIFGATLGVEKFTARKLFGVIASLTGIIIISRVDLSGSNDENRGSFPYKSPAEIAIGDAMAAFSAILYGVYIIVMKKRVGDESRVSMALFFGLVGLWNTFIMWPGFFILHFTGLEPFAWPDSHLTWTIIRTNAIVSLASDICWAYAMLLTTPLVVTVGLSMTIPLSLIAQIFIHGQYSTVLYWIGAAIVFLSFIFVNHESKTEAE | Function: Involved in the import of GDP-mannose from the cytoplasm into the Golgi lumen.
Subcellular Location: Cytoplasmic vesicle membrane
Sequence Length: 431
Sequence Mass (Da): 47304
Location Topology: Multi-pass membrane protein
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A0A8S2YT80 | MADLQSYSEDSINTFSLASSKKKNIRNSLPVPVNNRITGNIRGPTWWLSLMLLLISVAVGFQLGLVFLCNVKRCITDDLSSEQNGDGFGGGGRSNLSFVSSINLPRVSQKKQLILVAIMTSKDFLTTRAPTVMRTWARNVPGQVIFFSSEGSTTNDSNINLVSLPSVTDTYPPQKKSFLMMKYIYDHYLNKFEWFMRVDDDVYIRTDNLERLLRSIDNRKPYYIGQPGMGTKEEFGKLALGENENFCMGGPGIILSRETLARFTPNIKKCLKNFYTSHEDVELGRCVHKYANTSCTWSYEMQHILYNHPNKTEGYKARNLVSTDILRAVSLHSIKDIRVFTRVHNFALQRRIIELEQRNMLLRRQTKIYDQILNIENQIKLQIKKLFQLIQRTKTDRMQKQLKLLYKQLNMPDR | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 414
Sequence Mass (Da): 47820
Location Topology: Single-pass type II membrane protein
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A0A2K3E7S4 | MVNIPLPFFGGRRARAGTRTSPQEPAADKQELIRLQKEVETLRVANEQLKEQLAARSIRLGEYLYKWSAGGLPLLGALGLGGPAAEWGLRYVLLRGTGLAAYGSAKDTAFSPRDEISVLSCFVAWEGLRAGRFWAFSVFDSGGSLLLDLPRVAERVLKLALPSTYAWLLGFYCLFHLWLNVLAELTRFGDREFYKDWWNAATVGEYWKLWNMPVHKWLLRHVYFPAIRAGSSRFNAILLTFFVSAVFHELLLGVPLHMVRLWAFAGIMFQVPLIMVTEMLRKKLNRDELGNYIFWIAFCVVGQPVCVLLYYHDYVVGIRPALLALRQAAAAVGGAAAAVGEAAAAAAAAGAGVAGTVAAGVGAAAAAAIGGMLGDGGTGAAAAAAGVVAAGNCTLGAVACGVS | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 403
Sequence Mass (Da): 43093
Location Topology: Multi-pass membrane protein
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A0A2E7BUA7 | MLPVLIQIGSLKLHTYGVMVVLGFLVAVNLAQRHGKKVGYDEDLIGDLAFYMMIAGLIGAHILHIIVYWNTGGYADDPLKIIRIWEGGIVFYGGFLGATAYFFYFTKKHDLNLWALGDIYIPSLAIGHAIGRLGCLAAGCCFGTPCDASWGLNFPHERAPVIGGVDENKDGEKDPFASIAYTSIRNQQITKRRFLGQVKGCQELPDADLQKAVKACQDGGECTGIEVKSTSDGANQFLRAIKKCQANKSCDSAEVRDFLRSCPDEKVVVAAAAMPPITQKDLDGEGIEDFSLALHQPEHTMDLHPVQLYEALGELTIFFILVMWRYRKRFHGQIFLMWLILYPILRWVNENFFRGDKSRGEDIIWGLSTSGLISVLVAGTAFIVILLSLRQGRLLGSPVLVPQGLTPSGFEVTDATSDGEASEEMTDLPGDEQSKK | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
EC: 2.5.1.145
Subcellular Location: Cell membrane
Sequence Length: 436
Sequence Mass (Da): 47994
Location Topology: Multi-pass membrane protein
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A0A243KJX2 | MKRNRRLLVSVFSSQEALIGGARIIDCEDPRTSLGNISPIQIMKITETVLSYKTDEKIQISTNIGEEQLLFDKTANGAAIQKFSNEIAGKAAQSALGVAVSMGTVVHPTNIIKIGIDAMNLKLIEEVLREIVLTIRYTDFYSHSQIVPVFFIRDINIWNKRKNNTKVIKQLLELREFYFHNEGTIDLADYYSDAQIARILPADAKTTRVSLNEIYPYSNFGLSNNNRDMLRQVVDLCAKVGVDGLMLDTSIQHKIIRTGLLKHPKNAEDKDSNGTDLPREGILDIEEVKFFCEYCHWAGIESYLAGSIQDYHAEELWKIEELDSIAVRGSVSGVVSDPFGIQKSGDARHERRVQRELVAKLIPPEQR | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
EC: 4.2.3.153
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Length: 367
Sequence Mass (Da): 41380
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A0A074KXZ7 | MGDKIVLIGLPGSGKSTLGKQLSLNLHYPFYDLDELIVDHIGCSIAQFFNEKDELQFRILESTMLNKTLLLDGPLVLSTGGGAPCFYDNIELINTYSTSIYIDVPDKVLVKRLMNNAGGERPMFYKLPESAVKNKILTLKQAREEFYNQAKIKLSGADISTELIVSALGKFKS | 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: 173
Sequence Mass (Da): 19194
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A0A0F8X8P7 | MVASKLRVRFAPIKFHNTPAPNSIDQPEPKQRSRERSRQGCRECRAHRVKCDETYPVCRRCERRGFICRSVPRLTQWQVEVPCMLLALGDIVNKRLMQHWFEKTSQMMAIDPNENSLSFLMTRYFAESPSLLHICQSFSASHESYFPCRGPIIALEERGKALQKFRQDLEISEKSCTEAAFFTTILLACSSYWVEHDVMDFGHAHFVGARTILERLLELRQSASEISQSTQFMVGVYLFWDMATSFLVHSSEQTPLGTPLMADAVQRIGTSYHPMYGYCTEILYLLGIVGRYYRKVLDTGRRDPFLEVELETKLLLWSAPKHSNQPISLLAEAYRKQGLLMISLARAHIPLLDRDLTESEGRSVIVQHARDTLAYLMKVPSTSWSLNFQSIPLIIAGSELTEEEVSLRQWVQERLRVIYSLNRCPAFKPYLAEFLGTALLIVIGDGVVAQCLLSDYQYGTWLSINLAWASAVCLSCYLSDPSPTINPAVTLCLAIVRPSAGQWKRIPAKLAAQFLGGFVGAAIVYINYRSAIHAWDPEYTIPGGSILSPRGHHSAGIFSTYPAAVFESNWEAAFSEMLGAAVLMFGSLSISDPGNAHRFPAPQMSLFVLLLMIGAALGWQTGYAINPARDFGPRLFSAIIYGREVFTAANYYFLVPLFAPIVGCIIGATTYDAMLFEGDGSWIADTLDKAEGRGSLRLEE | Catalytic Activity: H2O(in) = H2O(out)
Subcellular Location: Membrane
Sequence Length: 700
Sequence Mass (Da): 78482
Location Topology: Multi-pass membrane protein
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A0A1A9R1B1 | MPILTTRWSNVGRVMQLALEGVAGATLFALMLLTNADVVGRYFFNLPILGTVELTQQMLAAVVFLSLPVACWREEHVSVDLLDAVFPARWIWLRQMIVNLIIAVALWVIATRVWALGVRAFEWGDVTEFLRIPDGYLIYLIAIMLFLSALLTLGRAVSYLLEGVGVIKCGGPVSQGDKHD | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 180
Sequence Mass (Da): 19958
Location Topology: Multi-pass membrane protein
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A0A3D1QX30 | MKRFASWPGHAWIALPVRVYLAAIFLLACYHKILDPHAFALDVATYQILPLALVNLMAIVLPWIELATGVMLLVGLRTRPAALLIAGMMVVFTMALSIALAKGLDMSCGCFASQGADEDPISWTTLVRDAVWLAMAAYVLFFDKRPLGLDRLLERRGPPVAAQPNP | 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): 18173
Location Topology: Multi-pass membrane protein
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A0A2N2DNP1 | LADKVLGVDHYTVLETLKGKELEHIEYEQLMPFHSVEQKAFYVTCGDYVTIDDGTGIVHTAPAFGEDDYNTGRRYGLPVLQPVDEEGKYVGTPWAGRFVMEEGLDVDIIKWLAAEGKLYDKEKMDHNYPHCWRCSTPLIYYAKPSWYIEMTKLKDQLVANNDEVNWFPDFIGEKRFGNWLENVNDWAISRNRYWGTPINIWRCEDCDALESIGSRKELADKAIEDIDDTIELHRPYVDEVHIKCDKCGSVMNRIPEVMDCWFDSGAMPFAQWHYPFEHADDFDADRFPADFICEGIDQTRGWFYSLIAIATFIKGKAPYRNVLVNDLILDKEGKKMSKTKGNTVDPFDLFDKYGADATRWYLLYASPAWSPTKFDEEGLIEVVSKFFGTIKNVYNFFVLYANSDGIDPRNFIARQKNDKACLEFTTEREFALDPEFPVDHSPAERRGTAFGQSAGFDCEHRPELDRWILSKYNRLIREVTEEMDRYDHMKSVRKIQEFVTEDLSNWFIRRARRRFWGEALTDDKKSVYATTYEILCGVARLAAPFAPFLMDEMYIALTGEESVHLAYFPESDASQIDENVETRMDLVRTLVGLGRGVREKERLKVRQPLTGILVDGKYEALISDMTDLIMEELNIKGVVFEKNLDTFMDFSLKPNFKVAGPVLGSLLKPFGAAVAALDPKETVAILERDGQIELNISDSANAAGQTLIIEKDLIDVKISAKEGFAVAMEDNVFVILDTTLTDELVSEGLAREFVSKIQQMRKQKDFDMSDRIRIYYKADDAVAKAMEDHGDHIKTETLALELHEREGLTEYDLNGHKTGLDVERI | Function: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile).
EC: 6.1.1.5
Catalytic Activity: ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Sequence Length: 825
Sequence Mass (Da): 94637
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A0A816CNG7 | MRVXLRYLWYKRSVSDEDDELENNKALDNHIEKKILSLDINASHSIEQTNNTNLKSTSIPSWINDQVYGDKVILFSPTVYNVQQMDPDARWHQEPIVDVIFFHGLAGSAFKTWRQESAHTEDIKPIEKSTVTVAQTEEENDELLEISEETNWDTARMTSPVPPPSMPKMNQDEPSLCWPKDWLSEDISTSHIRMLAVDYESTVSEWQMRSMPRHIIRRSMHDRAKEIAEQLKQAGVGKRPIIWVAHSMGGLLTKYILTDEDNEEIRSNTRACVFFSVPHFGAELASFGIRHAFIVRPTVEIEELQPKSKNLLNLHEKFLEILKKHDNIKILSFGENEKTTFSLRYQTVIVPAESSQINIGKFFILNKNHIYVCKPNSKNTIEYQELLDVIQTIYYQRKNELKSQQMQLTEDILNNLYSFSSPIEDDVQ | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 428
Sequence Mass (Da): 49681
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Q67R89 | MPAGRLPGRKAATAAPEAPPIRLGYIDYLNCLPVYFGIEQGAVELDVTVQKGPPSALNRAFREGRLDVTPVSSIEYARHAADCVIIPGLSISADGRVASILLFHRRPLEELDGRPVALTASSATSVVLTRIILELRYGVRPAYRVAPPDLDAMLAEHDAALLIGDDALLAAQAYPEIPHVDLGAEWKAFTGHPMVYALWVARRELAEADPAALRRVVRVFHASQEYAWDRRPEMVAEAVARRGLPPDVVDDYFDLIRHEFGPRYRRGLVAFYEYARRLGELDAVPPLRVWGEE | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis.
Function: Catalyzes the dehydration of chorismate into 3-[(1-carboxyvinyl)oxy]benzoate, a step in the biosynthesis of menaquinone (MK, vitamin K2).
EC: 4.2.1.151
Catalytic Activity: chorismate = 3-[(1-carboxyvinyl)-oxy]benzoate + H2O
Sequence Length: 293
Sequence Mass (Da): 32434
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A0A7Y3GCW7 | MNVAVSRRYRFAAAHVLRSDALSDEENRRVYGKCSNLHGHDYGFEVEVTGPVDPISGQIIAPERLDGLVERHVLGPLAHSDLSQHPWFAERVSTAENVARVIHEQLESPIAGEGRARLASIRVQETRRNGFEYGGEAER | 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: 139
Sequence Mass (Da): 15513
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V8N499 | APPWAKDLLGALNDRLQQLIQAVSFTPETLVEALADRVPLGQPGAEWKRPFKSSFGYEITFSLLNPDPKAHDVHWDIEGALQRFVKPLLEKLSPLAEFSVDSQVGEARGREGVGGSQTLCPVQADGPYFSPHPRSSTTQRWESRPALTLLPPATP | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 155
Sequence Mass (Da): 17008
Location Topology: Multi-pass membrane protein
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V8N5C5 | MTLNDPKLTMEIDATGEKSDKTQKTTGKCCQQMLRALSSVTGDMKLFGDWLKEKPVALQSVDWLLRGISQVMFVNNPLSGIILLIGFLVQSPWLTLMCCTGVVVSTLTAVILSQERSTIAAGLHGYNGVLVGMLMAVFSDKCEYYWWLLLPVILMSMTCPIFTSALGSLFSKWDLPVFTLPFNLALSLFLGATGHYNSFFPTTLIEATTSLPNNSWSDVQVSMFGLPIGTWPFCLSSLTFLLLTTTNEAIFKLPLSKVTYPEANRAYYVERKKPRSESICDKV | Catalytic Activity: urea(in) = urea(out)
Subcellular Location: Cell membrane
Sequence Length: 283
Sequence Mass (Da): 31389
Location Topology: Multi-pass membrane protein
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A0A0T6BC82 | LVLVFVVYNRRREAHIKYPGPDDDVRENIINYDDEGGGEDDMTAFDITPLQIPIGGPLPELAPPKIGFNIMGLGGEPNVGIFIEEHKKRADSDPNAPPFDDLRNYAYEGGGSTAGSLSSLASGTDDEVQEYDYLGAWGPRFDKLANMYGTGEETELEDE | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 159
Sequence Mass (Da): 17413
Location Topology: Single-pass type I membrane protein
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A0A094CM57 | MKSIALLALAGAASAHYTFPALISGGTTTGAWEYVRDWTGSYTYNPVQDVSSLDIRCNVDGSTNTASTLDVTAGSKIGFSATPDIYHPGPVLAYLAKVPSGQTAATWDGSGSVWFKIYEDGPTGLGTQLAWPSDAATSVSFTIPSATPDGEYLVRVEHIALHSASASGGAQFYISCGQINVTGGGSGTPGPLVAFPGAYSASDPGILIGIYYPVWGERRIFRPELGDARRRAAGHGESSTHNPPTLRLYGRLRAYMLQTNKTSSKASFTPNLPGMHESQLCIRCGISRASSTLQPRAQTNPVNYNNMRSAILIVSALFSLAAGAAIDSDVLTKHENVGRATCSWIGHAPMCKPGNCPAGTQACAQDFCGDGACCFTGFKVKCCTVNPNVPSCT | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 393
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 41167
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A0A8J7M279 | MFFSNGHPSIRSKLASLVLVCVVPFWFIAALISFNVYLYQVEQASREMLVAARQMSQTVDRELVSVISALSALGTSPSVARGDFEEVRHQALDLLRLYPDADIIVADASGQQLLNSFRPLGTPLPKRNNPEQVRQVFATAKPVVSNLFQGAVTKRLLISIDVPILRDGRVVYDLSMTFPAARLSALLARQKLPESWYASIIDRNQVVIARTIGADRFVGRRTSLRFTQTAFGASEGNVRMKNIEGIDSVSAFNRVAASDWLIAVGVPRATLMADIYRWVAWVALAAVLISLTAGALAWGIGRRIAQDLQSLVQPALAIGRGESLTLGSAGYLQETFEVAQALTQASELLQRREAERDRAETELSQALVNLQKETAERIRAIEDLREQEQVMIKQSRQAALGEMIGNIAHQWRQPLNSLGLIVQGLPLYHEAGLITRDLMDQCVHDAMAHINHMSQTIEDFRNFFKPEKDMVDFDVNQAIRQALSLVEGNFSSQAVEVSLDLTPGRTVRGYPNEFAQVLLILLLNARDEMIRRQVVPGRVTIRTFADGGHCGITVSDNAGGISGDIIDRIFEPYFSTKGVQGTGIGLYMAKNIIEKNMNGRLTVRNSGPGAEFTIEV | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 616
Sequence Mass (Da): 67985
Location Topology: Multi-pass membrane protein
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A0A7S3H9H9 | MLLLPTCAYLLTRRATFTALLFALMNSSLAFFLASFQVHEKSVLLMLAPAAPLLLLDQKYFCFVQLLGCFTMFPLLVKDKLRVPYLACCGLYLALTCLLDGPATDSTEASDGAKKQTMEKLYAKLAYTTGDIARQMGWLGELLAIEPVKSVLIGLSAFGMIVLHLLEIFVPAPQRLPDLYAALFSIFGAANLCVIYLVGVCWLWWLPSADAQSRKLKSENVAVTQKD | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 227
Sequence Mass (Da): 25040
Location Topology: Multi-pass membrane protein
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A0A7S3HRX0 | MRIISVLSVLVGFTSLFQAIVVRESNDDKRDGSTKAMTVEFRLFQFQYLGVYLTIMLADWLQGTNMFTLYSSYGVNVGTLFLTGFLSSAVFGTFLGIYVDTYGRKLGCIIFCLLEIVINLLEHIPNMNLLLAGRILGGMSTSLLFTAFESWMVSEHRKRGFEESWLASTFSISSWGNGFGAILAGFLAQVAADVAGDI | Function: Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum.
Subcellular Location: Cell membrane
Sequence Length: 198
Sequence Mass (Da): 21853
Location Topology: Multi-pass membrane protein
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A0A5C3EU06 | MLPPASSPGELDGHGLAILLLLNFHCRVHLPETSREARRALMLLLMDLIYQAVPPTASLDEFLGHVRSALACEPEQAEVVCEYLNRTVSWPLEILEVTDGLTKLFNESKTDLTMYLAWPAELSRILAPYETLGMDESPEVFVDRRSFFGLYFRRQKLVFDSLDLEARGRLRDVAFEWKEGLLPPHASNDALHEAEGTEDSRMTAYKQFQRAMLTGDYSTAKDSMQKSFDYFAPGSDHELHQHTLLHLASFHYQTGGLDAARAALEEAVSLARSADDLECVAMCESLMRRLQGEGTSRRSMEDKSPGVQRQLSSQDALWRAETDAGKGDELVEVLQQLVRSAQPPRANVKATKSSVDISLHLIDDASRRFGNDAARPDAVVGHLWQDLGQGKVANVYLGRAARARGEVAAAQREGRIKARCEKASKLARRGRYEHGLGLLLRPSTYEALSAAEYRAWTEAVWGILWLRARRRREAKTLSRLAQLDPSSHHVLRDADIEDLVETPKTLQELLPSLGPRGAGASEKKPASEANFQRRLALSSRQKIELLLDKAQMLMDAKQPARAQSPALTAIAMARAQAHEPLERAGIVTLSRIAGISYQLPIQALASLEEVLPLTLADEDLEVRAMAQWTYAECLLGQTKSAGDPSTITEALDWLDRAERDTETISLIHVQRKVLYFMARVLHQLDRAEERDRVADKLAAVERDCLRASEAVCTESLAVVDDVLDVVNLVGAHVASGGAAAIRLSMG | Pathway: Protein modification; protein ubiquitination.
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Subcellular Location: Cytoplasm
Sequence Length: 746
Sequence Mass (Da): 82682
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A0A818ZH04 | MRAIKFENDLYQDIVQEDFLDSYRNLTYKAVMALKWISIYCPQASYILKTDDDMIVNTFMLLKHLKFRDSYQLKQNKSIFCRVYESMNVIRNKKIKWYLSEKEYPPKKFPSFCSGSAFILSNDLAETIYNTSLYVPFLWIDDVYITGLVAQAVNVTFKQFKSLYTVNDKLLKSIIPIPFTLDMASCKNIIHLGLILLVDFVGLCTGRLIRTKVVILGGGMAGVMVARTLSEKGISDFLIIEAESVLGGRMKETTFDKYTIELGANWIEGIRNHETGEENPIWTMAKKYNLTSTATDTDDLLTYDQNGQFNYSDVVDQAFAHFKQVLDDATKREASNLEDLSFAEGQRLRGWIPKTPYENVADWWAFDFEFADKPTASSMIRTAANEKATHGQWLEDDQFVTDQRGYAFLVREEAKRIATNKNILYNSTITTIEYSNSSVNITLKNGLIIWADYAICTFSVGVLQHNDVHFIPAFPAWKQESIFSFKMATYTKIFLQFPHKFWSNAQFFLYADPYRRGYYPQWQSLSEIGFFPESNILVVTVVADQALIVEAQSKNQTLIEIMNVLRSMYGKNIPEPNNFYYYRWTLDPLYRGSYSNWPTGTSLCQHNNLGRSIGRLHFAGEAYSQEYYGFLHGAYLEGLKTGKKVADYVLNKTFRTDNRDYSCKQHSSREQKRIILSLLSKLKSGKNSKVSKVEFLQSIHNFHDSKR | EC: 1.4.3.-
Subcellular Location: Membrane
Sequence Length: 707
Sequence Mass (Da): 81571
Location Topology: Single-pass type II membrane protein
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A0A0L0V660 | MLTRNIGRLQSAGLMNKQAPRHLNQIVARPNRLHQQQTKSIHVENSVGNTLPFKFRGPETSKVGVAMKVASFFFVGFFTPFAIARYQMKKSGAWP | 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.
Subcellular Location: Membrane
Sequence Length: 95
Sequence Mass (Da): 10716
Location Topology: Single-pass membrane protein
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A0A955VAB1 | PLMSVTNAVSGIIIVGGILEGARGGELHASIVLGLVAALIATINIAGGFLVTQRMLRMFRRD | Function: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane.
EC: 7.1.1.1
Catalytic Activity: H(+)(in) + NAD(+) + NADPH = H(+)(out) + NADH + NADP(+)
Sequence Length: 62
Sequence Mass (Da): 6432
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A0A4Q3K0E1 | MSTTKSGVYELVQTVRFESARRLPRTPPSHPCHNVYGLAFYLDIHVEGRLDPATGWVFDFAEIDRAMKPLRDRIDHHYLNDIEGLDNPTSEVLVTWIWDHLKPALPGLTQLILKENDVSRVIYRG | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.-.-.-
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 125
Sequence Mass (Da): 14410
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A0A4Y5ULE7 | GEEDQYIAYVAYPLDLFEEGSVTNXFTSIVGNVFGFKALRALRLEDLRIPTSYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVF | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 165
Sequence Mass (Da): 18645
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A0A2H6K8I1 | MYGRNPGLGGYTLCLALFWVLAIISIGAAVADDGVEEYTFWDDDVVVDIDTERSINFLSCACYGLSELREVALRAGAPGIEDTPDGLGERLLRSRGNWQILSATRHVILPTQPVHVSHLMVLKCLRQEGCNDFLFILPFHEAMQTNGITAIDGDSKSTLQVKLIRDIARVKNDCVHVLPDDQYQSFKDDATCRDSCYPAVYQVQLEETIQPEATTKVRVEYYLGKPYSPWQSRLKLGEQQRVAFGITTLLPSAYHSISQKTRFIVMSELNIDVESLHVYATLTEIAENIFLCGPFEKVELLSSGEPMVLTIDCNDSLEYIPELHKRISVPMCPFSGHIQIAEHYVVYNDASPVEGHFSLETLREIDRNEDNHRGGGNFVTYMDALFPQQASKLRYFDDIGNNARAYLIDKNASHNYKSVHVGDIWLAAQLCAAASEVPAAGRMEDIVHGAVPPAEMHTEIKKGIRIYENR | 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: 470
Sequence Mass (Da): 52664
Location Topology: Single-pass type I membrane protein
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A0A838SP43 | LATQRQLFVVGAQLATHTDHWAQLDDEVSRVTPAMVDRLEEGIDELVEQHPLPGEFVVPGQQPAGAAIDLARTIIRRAERGTVAMRRTGLLPDDLIVRYLNRLSDYLFVLARCVEQGEYVPTRER | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate
Sequence Length: 125
Sequence Mass (Da): 14089
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A0A0H3B966 | MLKRNVPLLITIAVFILGYAFCLSQFPSFSSSRVWCDLLTDNAFLGIVAVGMTFVILSGGIDLSVGSVIAFTGVLLAKLIGTYGIHPVYAFAIVLVMGAMFGALMGWIIDSLKLPAFIITLAGMFFIRGMSFIVSEESLPINHPIYETLANYAWRVPGGGRFTLLAFIMLMVVAFGILLAHHTRFGHNVYAIGGNSVSAGLMGVPVRRTTIKIYMLSSTLAALSGIVFSLYTSAGYALAASGVELDAIAAVVIGGTLLAGGIGTVFGTLFGVLIQGLIQSYITFDGTLSSWWTKIVIGILLFSFIVIQKAMSAFYLNRRSRPQSSPLTPV | Function: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 330
Sequence Mass (Da): 35250
Location Topology: Multi-pass membrane protein
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V8PHK8 | MNFCHFCSMCLEAKSKHLKKQSKMPPIAMEQELSLSSDSEESVIADQELQEAFAKGSLKPGLNIVLEGRPKAFNNVDGLKRCLSEFQRNLSWVERLDITSPLETNVTGAASKNTVEKDSVDPEDDFKREMNFYHQAQASVLEALPRLHHFKIPTRRPDDYFAEMAKSDQQMQKIREKLKSKKEAMEKSEKAKQLRALRKYGKQVQIDVLQKRQKEKSTMLNAVKKYQKGESLPSHLSILEKEPNAKRRYKNQKFGFGGRKKGSKWNTKESYNDVSSFRASKAHNKGTGKAGKRGAKAPQSSHVPADFSAPTWEVQPIIVPVDTDLMRPAEDSELDGRIRCTVAVEHLGAAAAPNRRLLRDAWVTLGRNEFRELVLQVAGPGRLQNFPLRQNEMRLFTRFVKDGKSSIRLGPAGSDCVQLLLSNCPPDRLRRFVQTLRVKFEATQQGRRPVAERTRLLSSLPRTFDTVSPVQARDLQQANARGALANVTATPTKGQALRCGSRKRPMESVDGRQMTEEKQVKKPWLMGSRATLSQEQSRVLNAVLSGKNVFFTGSAGTGKSYLLKKIVASFPPNGTYVTASTGVAACQIGGITLHAFAGIGSGKAPLHQCLELAQRPGVRQQWLNCRCLIIDEISMVEGELFDKLEAVARDVRKCQDPFGGIQLIICGDFLQLPPVAKDHRQPKFCFQAKSWRKCIHLNMELTEVRRQTDKEFISLLNAVRLGRCTEEVTRLLTQTVMQKVERNGILATRLCTHKDDVEFTNTMQLQQLSGQLRSFKAVDSDPMLAKTLDAQCPVKSMIELKEGAQVMLTKNLDVSQGLVNGARGVVIGFETEGKGWFLTGTLWMISSWGMSLDCAEVSLARVFESGQAYVALSRARSLASLRVLDFEAKVVIANPCALQFYKELKRDQFLDQASLHSYIHADKENEIVKGAFTA | Function: Required for the processing of the 27S pre-rRNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 934
Sequence Mass (Da): 104517
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A0A3Q0EVT1 | MSALFNFHSFLTVILLGICACTYFKMQFPAILDQKTGFRGFFWKAARIGASILYRSFMRKLQIYEMRVCTYDFIGALDTNLFHHIVNYFFFVVETKWSFCH | Function: Involved in the early part of the secretory pathway.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 101
Sequence Mass (Da): 11993
Location Topology: Single-pass type I membrane protein
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A0A7S3GQU1 | IKVAAQNVSASAEGAFTGEISPGQLKDSRIEWTLIGHSERRSKFGETDAITATKIEQCQKASISVIFCIGELLEEREAGKTDEVNKRQLDAVYSQIEDWKKIVIAYEPVWAIG | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Length: 113
Sequence Mass (Da): 12498
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A0A094D7R0 | MRSFVTINSIIALACVGTELVASIAVKAPGNAARDTTPQYPYDPNTTPYCTQWWDTQGLFTCQELVEVYSLSMADFIRWNPSITPQCDNFIESGESYCVEAAGEPPATTVAPPTTTALPTKTTTSPISTPPTSTTTTGPPPTTTIIDGTSYPLPPAPTVLGSTPKCKKWYVVSSGDTCLTIAAKSNVMKTQINLWNTYINIACSNIWATYAICVSSPIAEDYWSSVGCLTDSTTSRALANRITLDSEKSIMTPKACSDACAAAGYRLAGVEYGSQCWCDNAIRNNHALTSSGCTMSCPGASSIMCGGSDRLNLYRLDKYKDMGCYNDISTARTLEKQIIIADQNNILTREICQDACEKVGYYFSGVEYAHQCWCGYSVWGSVAGSGCSSACPGNAAQTCGGSDRINVMMRPQSRSIGCYSDDVNNRTLRYQVAIANEATLMTPDLCRNTCLTKGFIYSGVEYGHQCFCDDELYGSGAPTTGCTMACPGGGAAVCGGSSKINIYSLRRKEGTAPRKVPRQSNVKPLYNRKVVAWIPQPPGGMSRILSSRQADELHKSIVAYLSANNLPNAVSALRTELGLEEETFDAATVKKYETLLEKKWTSVIRLQKKASPSSGYPSTRLCLFRIMDLESRVATLQSELDSATPSSLSKRSQDPTSWLPSKPSRYTLESHQFEISCIAFHPLYSTIASGDQGSTIKIWDWELGELERTIKGHTKAITGIDFGGPKGHTLLASCSSDLTIKLWDPADAYKNIRTLSGHDHTVSAVRFMPSGNLLVSASRDTTLRMWDVTTGYCVKTIRGHLEWVRDVCPSPDGSSILSTGDDRTVRLWNVSGSVAENKLTLLGHENFIECCVFAPPSSYQYLSTLAGLQKPPPLTSTSEFMATGSRDKTIKLWDTRGRCFKTLIGHDNWVRALVFHPGGKYLVSVSDDKSLRCWDLSQDGKCVKELSSLHDHFISCLAWAPSIVKDKDKPSANGEAGGSAQDVQIRCVIATGSVDMALKIFAR | Function: Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for nuclear migration during vegetative growth as well as development. Required for retrograde early endosome (EE) transport from the hyphal tip. Required for localization of dynein to the mitotic spindle poles. Recruits additional proteins to the dynein complex at SPBs.
Subcellular Location: Cytoplasm
Sequence Length: 1003
Domain: Dimerization mediated by the LisH domain may be required to activate dynein.
Sequence Mass (Da): 108972
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A0A2E0AFK6 | MLEGIVVSCQARPDNPLHGPLFMSAMAVSAVQGGATAIRANGVKDIRSIKAHVKVPIIGINKIFSDKSEIYITPSKKSASDVARAGASIIGIDATIRKRVFEPLTDIIKYIKKDLNCLILADVSNLDEAMQAENLGADFIATTLSGYTSTSPKTKNEPDLDLVATLVNNCKRPIIAEGRYENSQQISSAFELGAAAVVVGTAITNPREITRKFVNQVKDR | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
EC: 5.1.3.9
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine 6-phosphate
Sequence Length: 220
Sequence Mass (Da): 23626
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A0A1T5J315 | MTRRPLVAVSLKAYLGAADTERWLTEVAEVATSAATTPAGDVELAVLPSFPLLPAAARLLARTSARWGAQDVAPGAQGAQTGEVTAALLAELGCRLAVVGHAERRSAFHEDGDVVRAKVARLVEAGVTPLLCVGEEEQTSPTEAAAVAADQLEDALRGSGAPDVVVGYEPVWAIGAPRPAPAAHVVTVARALRERLDALGVEGRVLYGGAAGPGTLTALAGAVDGVFLGRFAHDVAALRDVLDEAAAARPADSAVRP | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 257
Sequence Mass (Da): 26196
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A0A5E4PH44 | MDDILIGRRACARRDDYHYMKFSIYSSRIRQMIIFVLSAIVLPCGMAYGSAASGSGMTLSKTTFARLPGWERDNQAEALLAFRQSCAEIVNRNPESYKAALQEHVSTQTWQAVCKAAAALHQADNRTAREFFESWFVPFHVRDREDSTGLFTGYYMPVIHARLQADKRYTVPVHALPDDWVKIDLGAFYPDMAGKTLVGQVKDHLLYPYPERRAIIKGALAGKARVLAWADNPVDVYFAQVQGSSLVELPDRQRFIIGYAGDNGHRYTSIGKILIAKREISREAVSMQSIRAWIMRHPDQAENLMNQNASYVFFKKLDYSQPLGTEKIPLTPRRSLAVDQRYLPLGAPVWLSTSVPAYDGKHASKPFQRLLVTQDTGGAIKGIVRGDVYWGSGDQAAYIAGHMNSPGQYWILLPRTQA | Function: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
EC: 4.2.2.n1
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Sequence Length: 418
Sequence Mass (Da): 46985
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A0A5E4PJM7 | MFKRVFLFIATNILVIGTISILVSALGLHSYLTSRGIDYTKLALFCGIWGMGGAFISLFMSKFIAKTAMGVVIINPNNATREEHYLLEIIYSLANKAGLKTMPEVGIYHSPELNAFATGPTRNNALVAVSSGLLSSMNRDEVEAVLGHEISHIANGDMVTMTLIQGVVNAFALFLSRIIAYVISITMARGDDKEGDISYMAYSVLTLVFDILFTLLGSILVAAFSRWREYRADAGGSKLAGRNKMIAALMRLQTASGIEDDRAPVLAALKISRQSGWLDIFSTHPPLEKRIARLQEAR | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Cell membrane
Sequence Length: 298
Sequence Mass (Da): 32569
Location Topology: Multi-pass membrane protein
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W4TS56 | MPPTVTGTVLDGIISGVLEDLHERQLMVTSDNLREATELVAPAIDPIPRLTAPGLSVISEIKRSSPSNGQLAAIHDPAALADQYRSGGAAAISVLTEERRFQGSLADLDAVRAKVEIPVLRKDFVVAEYQVLEARAHGADLILLIVAALSDDDLQRLYDLAIELGMTPLVEVHTPEEVSRATALVPVWWV | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 190
Sequence Mass (Da): 20458
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A0A955VKN1 | MPIEYSLQLAKEYFHFSASHFTIFGAESREWMHGHNYYLTLSLFGDRLEDGCLVDIERLRPEVRQLCEELDHQILLPAESPHLRVDQIGDVVQVSYGASEFRFPLSDVTLLPVNNITMENLAHHFATAIWERLAAPALSAIEVHLEETRGQRAGVRISK | 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: 159
Sequence Mass (Da): 18187
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A0A7S3MHA0 | QEAGLGVVFCIGELLEEREAGRTVEVCQQQLGQVLPKVRNWQKFAVVYEPIWAMGTGVAATREQAQEAHHAVREIVRETSGAEAAEALRILYGGAVNVRSCEGFVSQPDIDGFLGL | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 5.3.1.1
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
Sequence Length: 116
Sequence Mass (Da): 12611
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A0A815N5L5 | MLQVEQNLLTGRNQSLSDRIFSQQTGVEIQRHSRSNGELKQQHEVLLSTLLLEQQLHSTATNQHKQFVKEESLLKLCDELRPNLILTTGGTGISPDDTTPEVLYRDIDDDIQMSEFALQKNVPLELADLGLLATVGRQTIHVYDKLCVVVLSTDNGEIRDSNKIMLMRVLKCTTCYLLSAWHYR | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
EC: 2.10.1.1
Catalytic Activity: ATP + H(+) + molybdopterin = adenylyl-molybdopterin + diphosphate
Sequence Length: 184
Sequence Mass (Da): 20920
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A0A094DEV4 | MDANGEFDVNSLSQRDKQELQQFIQNETQKSKLQQSVHNLTDICWTKCVTGSIKSGKLDKSEESCARNCVDRFLDANFLVIKQLEGMRGQ | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 90
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 10255
Location Topology: Peripheral membrane protein
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A0A819L0X5 | MFYHAYDSYLKYAYPYDELRPITCDGYDTWGSYSLSLVDAIDTLATLGNSTEFSRVYTIIQSLDIERDINVSVFETNIRVIGGLLSAHLLAKRMNVSVNSTWPCTGPLLDLAVALANKLLPAFDTETGIPYGTINLVWGVPIGETNITCTAGGGTFLIEFGTISRLTGDPKYERAALKALRALWSKRSSINLIGNHINIQTGEWTANDCTIGTGVDSYFEYLVKGALLFRHPELMDMMNEYIKAIDAHMSDGSGWFVFANYQQGRKTMPLFASLDAFYPGLLTLLGKLDRARETLYAYHTMWRKYGSMPEFYNLAQQECMQGREGYPLRPEHIESIMYLSKATDDDTLLFMAADIFDSIESCCKTSCGYTSLKNVKDHQLDNRMESFFLAETIKYLYLIFDENNFLHANGEYATEHRTASGSCFLDTGYVYNTEAHPIDIGSLDCCTSSPFDETSSDAFENDSLTKEQIRWLGNILLNQDKQELHGISFTMIWQFIKRHRRKLFLISLLSGGGYAVFRFINGKLTTMLDDQDKMMAEWKKQLYYEHNRDTSLRTSTDIFAQVVLNINRRFQCENILTRLSTISDATEKRELWEQLRVECFARLFTLAYSSSFVLALTELVVSALSGRLYSQSQLQHASIREHNITTTAGGISATSKSSHAESTHDQSSLLSRDIQLACLDVIRYTTDAGMNNLIEDVRKATQSILSRISLQQMLDINDIIWYCSEIRHQIEKKRYQSVNNHHPLLKYVRSTALPARSSQPTTTSGYSFSNAVTTASSLLTKRTHSPSSVFSVQQQFEIECIEMIESDTFQRVLIQIIDQSFSNIYDEFAREMAKSSAATVNSSENQLHDPTTIIEVQIPFAKVIPISNNIYSKLSSHHEQLMLHFQSLACRPELHEYTKCAYDLFSNESLQPATRAAYSFLPLASSSTLQSSLSSFLQSLMSS | Function: Involved in peroxisome biosynthesis and integrity. Assembles membrane vesicles before the matrix proteins are translocated. As a docking factor for PEX19, is necessary for the import of peroxisomal membrane proteins in the peroxisomes.
EC: 3.2.1.-
Subcellular Location: Peroxisome membrane
Sequence Length: 943
Sequence Mass (Da): 106700
Location Topology: Multi-pass membrane protein
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A0A8S3CY09 | QYDPNYWESAQVLLNSSSFNLRDDIGYWRQYGFGMLGIYKSDLGQIGNWNVEISGWGKEDVEIYDKLVQCPTLNVFRTID | EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 80
Sequence Mass (Da): 9331
Location Topology: Single-pass type II membrane protein
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A0A956E2J4 | MSAAQQMKAHQLVVRVGELRVGQADDVIVTYGLGSGVALVLYDPALRIGGVLHAMLSGPGSSDSPGKFVDAGADALLKEFYSAGTVRSRLVAVVAGGASPGGAFIQTGSRNLTVLKKVLWKHGISPRANDVGGKSVRTVTLECDSGRCVTSSRDSRLVLMP | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 161
Sequence Mass (Da): 16662
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R5NE55 | MKGYIINPDKEYAEKIIQGIYKRQGHCPCRVNVDETTLCPCDEFVQKKICRCKLYIKEKSIDI | Function: Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
EC: 1.8.7.2
Catalytic Activity: [thioredoxin]-disulfide + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [thioredoxin]-dithiol + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Length: 63
Sequence Mass (Da): 7411
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A0A7K5Z0W4 | SREALRVQERSEQLAQELREVTHNRASLRQRLHHLRQYLHVLREGQRFTSQPAPLGSPLRPRAHSDCEPIVDPSLQQHVERKVNFVTGVIHPWRVSAFERLLWCACRGYLVASFVEMPEPMEDLVTGENVTWVIFLISYWGEQIGQKIRKISDCFHCHVYPYPESEASREDTMSGLQSQIHDLGVVLEETEQYLAQVLDKVVAELPGWRVQVQKMKAIYLILNQCSFDVTEKCLIAEVWCPVRDLTQVQDALRQGSYQSGSNVECFVQRIPTSESPPTLIRTNKFTAGFQGIVDAYGVASYQEVNPAPYAIVTFPFIFAIMFGDVGHGLLMFLFALWMVLYENSPSLRQATNEIWLTFFGGRYLILLMGAFSIYTGFIYNECFGKATVIFPSAWSVATMANHSSWSSAYLATHPTLTLDPNVTGVFRGPYPFGIDPVSVPWRGGDRVGTLSGVTQSLTHPCQIWSLATNHLNFLNSFKMKMSVVLGIVHMGFGVLLGVFNHLHFQQRHRLVLELVPELIFLLALFGYLVFLIFYKWVKFSAADSRLAPSILIHFIDMFLFTANADNPPLYPAQVPVQTVLVVLALASVPVLLLGTPLYRCCRRRAPGGPAVRLGPEEPLLEGQEAGNSVNANKEDVESGGHSPDAEHADLAEIFMHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVMRNGFVRMSYAGGAVLAPVFAAFAVLTVAILLVMEGLSAFLHALRLHW | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 744
Sequence Mass (Da): 83443
Location Topology: Multi-pass membrane protein
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A0A7S3HS43 | MSLLGPFVKISRALKERGLKGALTQIYLIGDLKFGELKGTDKFGNKYFENQDLPFGQHRWVEYKNIHNYDSTMIQPEWHGWMHHVYDETPNDPVAVPDYLPTSTISHAIYNTHVGRVDPAAAANDREQIDTTQYRRRGYKIGSLMTGPDEEDHYYKQPGHPLSKDSEKGRYK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 172
Sequence Mass (Da): 19855
Location Topology: Peripheral membrane protein
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A0A2R6CA70 | MVNGFTQRKGTTTIGIKASDGVVLAADRRATAGYTVANKHVKKILTVTSYCAITIAGTVGEAFNLADRVRSEAYMYELRNNVRMGVKSIANYASLLINSKKFSVFPVQIIIGGYDSSPELFMIDFFGSLSAEDYVATGSGMHTALGSALNRLKPNLSLAEAIPIAIRSISAAMEWDTATGEGVDVVYADREGVKRMEEDEVAEYITGGHI | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Catalytic Activity: Cleavage of peptide bonds with very broad specificity.
EC: 3.4.25.1
Subcellular Location: Cytoplasm
Sequence Length: 210
Sequence Mass (Da): 22587
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A0A0L0VDU7 | MAIILVPTRELSAQVTLAISSLCKGLGNENAIEIINLAGSDPKRSRRKHAQTEQSYTSNPPDIIVSTPARLLDRLRTTPIDMSGLLYLVLDEADLILSYGHSFDDIKAILSGSGSTVTQSWRFPTFFQSFLMSATMTSEVAELKSLVLRNPEVLYVKESINELSNLTQFSIKVPNEQDKFLLIYVIFRLKLIKGKGLVFVNSTDKSYQLKLFLEKFGIRSGVLNSELPFNSRYHAVEEFNKGIFDYLIATDESENNLPAGKNSSKPTPLPADPNLISTQPPTADNVVSTEEVVTNPKKRKNGDDGNGQSQDKPTDYGVSRGIDFVNVACVINFDLPLLTQSYTHRIGRTARAGRTGIGLSFVLSNPKSDPSLNRTNKNLQETYIRETEVWKKIENEQIK | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 399
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 44409
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A0A6B9VS41 | MINMSFWLLPPSLMLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMKVNNLSFDQMSLFIWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV | 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: 147
Sequence Mass (Da): 15837
Location Topology: Multi-pass membrane protein
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A0A977MKP3 | MSLQWTIIATFLYAEIAFVLLLTLPIASPSRWNKFFKSKFLAYISGQASIYFLVLIGVLILCLLDAIREMQKYSSIEASDHQHLDAEMQGNMRLFRAQRNFYISGISLFLLIVIRRLIQMISELAALLAQSEASFRQAQSATVAA | 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: 145
Sequence Mass (Da): 16425
Location Topology: Multi-pass membrane protein
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A0A8S3K9C4 | MKIFEHHYVVEREETRISPPLFSLHFIFLRIVELGATLGIRPGDFFGPVSAAHCLKQALQAAVELNQVPDTLRIYISQDAIIYREDVMNLCTAPFNLIKQKLNRSIDT | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine
EC: 3.4.22.-
Subcellular Location: Cytoplasm
Sequence Length: 108
Sequence Mass (Da): 12354
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A0A0T6B0L2 | IYELKTKFASIKEIVELSSKQNDADIPNIYNFISKWYSDIENYAPADVCIDDHIALIMFSSGTTGLPKGVMLTHRNFNTRRAITLEPSCIYEPKTKVTLGVLPFFHLFGLNTVITGLVHGRMVVVIEKFDPILYLSCLEKYKIETISAAPAIVQLLAKSPLVDRFNLSHVKDLVVGSAPLSRTLEEAVKRRLPIKYVRQGYSMTEGTATFVTVPPNTERLGSCGKLYPTVIGVVKDIETGENLGPLKSGELCFKGNIIMKGYYRNEEATREAFTRDGYLKTGDIGYYDHDGYFYVIDRIKELIKYKGYQVAPAELESILIAHPKIRDVAVVGIPNVDAGELPMALVALQPNADVSENDVKTYLNRYVSAHKSLHGGVKFVGEIPRNSLGKINRKEIKALAANITKSKL | Catalytic Activity: ATP + firefly D-luciferin + O2 = AMP + CO2 + diphosphate + firefly oxyluciferin + hnu
EC: 1.13.12.7
Subcellular Location: Peroxisome
Sequence Length: 408
Sequence Mass (Da): 45409
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A0A956KS36 | LENPTSERIAAWIWRELAPQLPGLSRLVLHETHSSYVIYTGPER | 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: 44
Sequence Mass (Da): 5088
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V8NLL1 | MQCIIPCFNSVNECSSWALSSFLYALRSSCSFCYWCGLLYFSQPPAPLKKAQRHSEDGKGFIDALQPVLVSRNDPDSRKHTIHEITKRATSEEQWPQVMIFPEGTCTNRSCLITFKQGAFIPGVPVQPVVIRYPNKLDTVTWTWQGYSFKQALVLTLCQVFTKIEVEFLPVHAPSEAEKKDPVLFANRVRNKMASVLDVPITDHTYEDCRLMISAGQLTLPMEAGLVEFTKISKKLNLKWDSIREQLDQFSRIASMSKGGRIGIEEFANYLKLPISDVLQELFTLFDREEEEEEEXGGGGGGGGGGGAGAFLKNLTGGGGGTGGALIQGLGGLLSGGGGGGGSGGGGGGGTSGGGGGSKATNVLGLLGGLVNIISEAAAQYKPEPPPAPRSHFANVEANESEELLQFRRLFAQLAGDDMEVCATELMNILNKVMARHQDLQSESFSLDTCRSMVAVMDSDATGKLDFYQFRYLWNNIKKWQCSFKEYAGPAGRIEMRNLPAAFKAAGFNLHEQLYALMIRRYADEDGSMDFNNFISCLVRLDGMFRAFKSLDRRGDGKVQMNIEEWLQLTMQASKRQERYMEAEKNGDGTIDFREYVIGLSVLCNPANTEQTIQMAFQLFDIDEDGSITEDEFALILRSSLGLPDLDVSNLFKEIDADKSNKLSYEEFKDFAEKHPEYAKLFTTYLELQRCQLFTEAEFASGEVTPTTTSCPSSYETIPVPRNKVCPLVTEDEHSNISDKKED | Pathway: Lipid metabolism; phospholipid metabolism.
Function: May be involved in the cellular control mechanism of the secretion of toxins from the gland into the venom.
Subcellular Location: Cytoplasm
Sequence Length: 743
Sequence Mass (Da): 82114
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A0A2D5QRX7 | MSTEPQQVSFTSPNQRLQYGQPIMLIDKRRRETYTVLQPEKVMNLNGNVIKHDDLVGLANGDRTESAKGNPFKVFKATLQQHILNMNRFATIIYPKDIASILMQGDIGPNLRVVEGGLGSGALAMSMLRAIGSQGQLTTYEINEAAVKCSTRNIKVFLGEVPHHIVKQKDIYEGIEEKDIDRVVLDVPEPWHVVPHAADSLADGGLLIAYIPTVIQVHELVKALRAHPAMYTTWSLEILERPWYVTEESIRPDHRMTGHTGFLVFSRRSARWAPEDGASKDSTKMEKTN | Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA.
EC: 2.1.1.220
Catalytic Activity: adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 289
Sequence Mass (Da): 32408
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A0A8S3IAC7 | LPDLGPLIVPPKDHLLSGYYKISRHYGYSLNYVLNTLNYEAIIITEDDLEVSPDFLDYFQALYPLLKYDKTLWCISAWNDNGIDKKIDRQANLLHRTDFFPGLGWLLTRTVWNEIKDDWPQAFWDDWMRKPEQRRDRACIRPEVSRTGISPEVIIS | 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 Activity: N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP
Sequence Length: 156
Sequence Mass (Da): 18433
Location Topology: Single-pass type II membrane protein
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A0A059EN25 | MVKKIKNHKNQISLIKPKSSQILESNPLRRTILTILMILLFMYIIVSDKMYLFVLIFLVQSFVFKEVIGVAAFRRKVSFLTKYLSFHFFFAANLFLLHKNITSFLRKFLPEITRFYTFFAFSFYVLGFCLFTFNLKRKRIRDQFIIFAVTHVTVFYLSKAVQLA | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 164
Sequence Mass (Da): 19555
Location Topology: Multi-pass membrane protein
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A0A1S3W023 | MGGTRPLSQSIFFFVLHLFAWSRFLLANETTHECLSTPIKNIGVVLDLDSLMGKQQKVAMEIAVQELNSFSCSKLELNIQNSNGISATAISSALNLTQNKQVLALIGTITHNEATIASELNDTIKNIPILSLTSPIANMEMLSPQLPHFIQFGNDIKIHMQCISAIVGEFRWRKVTAIYELNNKFSFDPGMLLDLSYSLRLVGSEIDNHLAFPSLSYLSDPKSTIENGLKKLKRKSNRVFLILQSSLEMANILFEKAKQMGLMEKDSVWVIPDGVASLLDSVNSTVISNMQGVIGFKTHFIETSEKFRRFKFKFRRRFALEFTEEDNISPSVFALQSYDATWVVAQATRNSQWKFNLEQLSRTNLSNNRKLQQPPIFSIINVIGKSYRELGLWSPELGLTKNLVIEQLPEIMKTHGASTKVLSTIYWPGGLQFVPKGWTHSTEEKTLQIAVPANGVFHQFVNVTYDQNTNNTSVTGFSIDVFKAAINTLPYDLKYTFVPFNGSYDEMVEKVYNKTLDAAVGDTAIMAYRYHLVDFSQPYLESGLNMVVLEQSKKSKKAWMFLDAFTKEMWLMMTTLHIFVGLVIWLIERQVNAELKGLGSMLWFLVTVIFYAHREPIRSPLARTVMAPWLFVILIATSTFTASLTSMMTFSQLVPSVLDIQTLQKRNSPVGCNGNSFIVKYLTEVLKFKPENIRKIYSVSDYPKAFQNKYIEAAFLSTPHTKVFLAKYSCRGLIKAGNTFKLGGIGFVFPKGSNLATDISEALLKVIESGEIEELEKEMLGGNASCSTLESKMKDGSSTGFQPFLGLFCICAVVSILALLYNMICVFMNDVETFTNYIHVTLTPLRRIYIWTSASFTWICSTLQWGSIKSVITTTITANAEETTINSQQSAMVVEVTDIVLASHSS | Function: Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Location: Membrane
Sequence Length: 906
Sequence Mass (Da): 101697
Location Topology: Multi-pass membrane protein
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A0A0T6AXD2 | MKLHEAEDIYDVILPIYILSKILGLAPFTIAKKILKPHFNPLTLVHILLVIGGMCYNAYLVETLEQQQKMVALALKCELYLGTLMTFTVLTLAIINQKLLIECVEKIDEIDMNMKNINIKINYKNSRRFVSVQIIFITCVFLLKVVLQFFMHSAARLSMYTAFNVFDYINTIMLFQYVDLLLLIRQRFIWMNRRLRQLNNYTDYFEKLTIPLTPIVSDTDTKKYPIRTKLDSELILNNLAAIYVKLCQLSRLVNRTYGIQILVTVGSRFVMITTQLINTYNIIGDPRFDSPIRYTLTFIYLFLHSSKIFMIASLSENTAAKVGCYNFC | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 328
Sequence Mass (Da): 38147
Location Topology: Multi-pass membrane protein
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A6WDE7 | MSTSTSTSGGTGGSTGGTRAAVPEQPRASQDVLTVDGVSSDEGHAALRASVRRLGELLGASLTRHEGAELLDLVERVRALAREADDGAELARLLSGVDDRTAIVLARAFTAYFQLANASEQLHRGLELSKQPGGGLSATLGRVREALESGDLDRDTAQQILGRLQLRPVFTAHPTESSRRSILDLLLRITGIVEASEDPAQRATDAERGQRRLAELVDLLWQTDELRVLRPRPADEARSALHYLRNLTSTVLPDLLEDLAVGLDELGLDLPVDAQPLRFGSWVGGDRDGNPNVTPEVTMEVLGLQHDAALDVLTAVTRDLLTELAASTQVVGFSPELLASLAADAEALPEVHAARVHLNGEEPYRFKLSYVLARLEGTRTRLHTGAEHVPGRDYAGVGEFTADLLLIQDSLRRNDGQMVADGAVARALRVVRAVGFGLATLDVREHAGRHHEALAAIYDRLGELITPYAALDRSARTKLLSKEMTGHRPLIGAAVRTLTGTPAQVVQLFTTIRTALDRFGEETIETYIVSMTQGIDDLFAVVVLAREVGLVDLAETPGANDVARIGFAPLFETVTELEAAEELLEGLLSDPSYRRVVAARGDVQEIMLGYSDSSKDAGIAASRWQIHRAQRALRDVAARHGVTLRLFHGRGGSVGRGGGPTGEAILAQPYGTLDGPIKVTEQGEVISDKYVQPRLARHNLEVALSAALEASTLHRTSLQPGEVLDGWDTTMGLVAAKGQEAYRALVGDPGLVPFFLAATPVEELGNLNIGSRPSRRPGGTGGLEDLRAIPWVFGWTQSRINVPGWFGVGSGLRAAREAGRGEDLRAMFAGWSFFRSFVSNVQMTLAKTDLGIAAHYVEELVAPDQRGAFDVIRAEHARTLEEVLLLTEQDELLQSAPVLRRTLELRDAYLAPLHALQVSLLGRARASGDAVDPALRRALLLTINGIAAGMRNTG | Function: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
EC: 4.1.1.31
Catalytic Activity: oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate
Sequence Length: 954
Sequence Mass (Da): 102535
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A0A1F2Z1Q1 | MKNILFIIVALFLSVPVAFAQVAQKPETTAKQAIILDFETGEVLYDKNSDEKMPTSSMSKVLTTIVAYDAIREGKIKWEDELPVSQRAWQEGGSASGGSTMFLNLNSTVKVSDLIKGIVIQSGNDACIVIAEGIAGTEENFADLMNRKAKEIGMDNSHFMNSSGLPDPNHYSTARDLAKMAVYLIREYPEDYKFYSEKEFVYNNIKQGNRNPLLYKTIGADGIKTGHTEVGGYGMIGSAVAAGRRIVMVINGTESMQARADEAEKLMKWAEVSFKNIDLVKKEAVIGKAPVVLGLARDVSIVASKDLKATVSAFDKEPATMVANYKVPLTAPVKKGDPIGELVATLGNGTKLTSPLVAGEDVEEASFFSRLSEKFMLMVVGAPKYQ | 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-alanine.
Sequence Length: 386
Sequence Mass (Da): 41944
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A0A356SYT0 | MLEQLPDEIPVVSAVISQELQAPLGHLAILCATRGTPNMGLREALSTPALSALEGQLVRLDVAAQEHAIRPATRDEAERSWAARRPSQALTPQIDRGHRALQDVCDARIGDAPRIGAKAAQLGEVCAMGLPTPGGFAVPFFHYLRHLSRHHLADGLDAMLADDTFRSDPRARAENLAQLRAVIERSAVDPALLRDLRRRIAAFPGEPRVIFRSSTNAEDLPGFTGAGLYRSIVVSGGASEAEIADALRRVWASVWLSGAYEERDWYRIDHREVAMGVLIQPFVDGAVANGVAITANPFYEARPGYFINAQALGGSVTGAGGDEIPEQHLIYTYADDGPELELVSRSTRGDGALLLGEPELMQLHDALRRLDFALTPYWSGRANSVDVEFLVAGADRRVVILQARPFCVRYTEGQRARHHAERGACPPRAYPPARP | 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: 435
Sequence Mass (Da): 47370
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A0A956SVP5 | MTERGFKLWRWATVFFANVPNLILVVWLFFWVTRTGRAQAPAAPWCNLGLFALFAGIHSAMSTPRYKRWFTARWPAAFERAVFTIVAGVTLLALMALWRPMPRALWEIEGPAGWALDALYWIAFAGAASVSTVFDQAAFAGTRQLSAHYKGKALPAPEFHVRGWFRWSRNPMYFFMIVLMWSASTMTTGRLLFAAVSTAYFIIGARFEERRHLRELGETYAKYQRGVSMFVPLPNRYAPDDAGGTA | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.334
Subcellular Location: Membrane
Sequence Length: 246
Sequence Mass (Da): 27952
Location Topology: Multi-pass membrane protein
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A0A949JR97 | MVRRRAREAKSPTSAEHLARWIFDRWAGEFPELTVVRVSETPKTWAVYQPE | 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: 51
Sequence Mass (Da): 6043
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A0A0T6AY68 | MEKNVSRKLRINAKEAMRIAERLYTQGLISYPRTETNIFPKELSLQPLVEQQTNDDRWGNFAQRVLNEGGPNPRQGRKSDQAHPPIHPTKYSNSLTGNEQKVYEFIVRHFLACVHKDALGHETIVHVDVADEKFQAKGLMILERNYLDVYIYEKWNAKEIHNYRNADTFMPTVLEMVESCTSPPKLLTEADLIALMEKHGIGTDATHAEHIDTIKSREYVGLQQNMYFIPGTLGMGLVEGYDRIGLEISLAKPKLRAEFENDLKLICEGRKNPDVVRREQIEKYRAMFQTVTTKIRCLDETLANRLEDQPEAYAEPLINQEEFRSVLKCPKCDSDMILKDRKNGEGKYLSCVMYPGCKNAVWFSINVESIEVLDETCPNCGPNVKKLKMKFKHNVFPGYPNPNVLCIGGCDEIVLSTLDININTVRKQLNNNERPTNLNTSNPWTSTSSNLRNNSLNNRNVPHSRDSGFSSSFDDNQNRNRDRYRGSSNQKKDNRSFLNSSAPSTLMPPPSTSNGSFTASSSLDNESNDNEIMCTCNQPAVLLTVRKEGPNTGRKFYKCRSGTDGGGCNFFLWAPDNEDPNPNNSRNNGAMPQRQTAPQCNCGLQAQLRTVQKDGPNKGKQFYSCPKPMGEGCNFFKWADNINDDNSNNWGGGGGNSHRNWRNKNRKGGGKTKTNNQTNRPAPYKNKVRAKRKCGICGQEGHTRSNCPN | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 709
Sequence Mass (Da): 80099
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I4EKX2 | MTGRERSSPRGRIWLMKSVNEGNLDLLDPVFEEEMSLCLNCRACEAVCPSGVKYGEILEASRAQIETHRAASPRAKLIRAFAFNVVFSDIRRFRLLSHGLRLYQRTGLRSLVQRSGVLRLLKLEEAEKMMPELSDRFVVGNGTTIPAQGEWRGRVALFVGCVMSTAYADVHRSTARVLARNGFDVSIISGQQCCGALHVHAGEPTGGRRLARKNIDAFENPYIDAIIINAAGCGAALKEYGHLLKDDPAYAARAAAFSAKVKDAIEFLADRGLSAKPGPLPMTVTYQEPCHLAHAQRITKQPRALLRAIPELKLVEMPESSLCCGSAGIYNLLQPNMASQLLNRKLDNALSTPATAIVSANPGCMLQLSAGLKARGHAWQVIHLMDLLDRAYEAADRS | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
EC: 1.1.99.14
Catalytic Activity: (R)-lactate + A = AH2 + pyruvate
Sequence Length: 398
Sequence Mass (Da): 43532
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A0A8S3J160 | VVVTIINYRSQYEYTNIPIKLPKLIDVNDTAPKSSPERFWGTYRSNLYFGLKHRSARSLSGGLMWFDYSKLQQTPDRFLRHWCDQNDRLKYGWNYHDGETFGVEQINDDNLQLNVQWLKQISGEHGGDWTTRISVTPQVCSKT | Function: Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor.
Catalytic Activity: H2O + N(4)-(alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] = beta-D-glucose + N(4)-(alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein]
EC: 3.2.1.106
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 143
Sequence Mass (Da): 16791
Location Topology: Single-pass type II membrane protein
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A0A7K5Z5Z9 | QGVPKPFTEVIKANIGDAHAMGQKPITFLRQVTALCLYPELLTSPSIPEDAKDRARRLLAACGGQSVGSYSASPGIQLVREDVARFLQRRDGVPAHPENIFLATGASDAIVSILKLLVWGEGPSRTGVLIPIPQYPLYSAAIAELQAAQVGYYLDEERCWALDVAELRRALAEGRRHCCPRVLCIINPGNPTGQVQSRQCIEDVIKFAYEEKLFLMADEVYQDNVYAEGSVFHSFKKVLMEMGPPYAEAVELASFHSVSKGFMGECGLRGGYMEVVNMDPEVKQQLAKLVSVRLCPPVIGQIVLDAVVAPPQPGD | Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
EC: 2.6.1.2
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Length: 315
Sequence Mass (Da): 34366
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A0A2I8B6U7 | LSSNIYHNGFSMDLTIFSLHIAGMSSILGSINFISTIINMHHFKLSLDKIPLLIWSILLTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILFQHLF | 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: 104
Sequence Mass (Da): 11491
Location Topology: Multi-pass membrane protein
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