ids
stringlengths 6
10
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stringlengths 16
1.02k
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stringlengths 117
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A0A2H1WZY1 | MHEGWPAVCAPPGAARRPLKVVREMNRLGMIVDLSHVGENTTRAAIKLSRAPVVFTHSSVYSLCNHKRNVPDDIIHSLKENGGIIMVNFFPDFVKCAPNATISDVAGKLSTIVVLTHTLTQK | Catalytic Activity: an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid
EC: 3.4.13.19
Subcellular Location: Membrane
Sequence Length: 122
Sequence Mass (Da): 13327
Location Topology: Lipid-anchor
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A0A5P6VQE4 | MVGLVLVSHSAKIAEGLKDLTSEIAAAHKGIVAAGGMEDGSIGTDAIRISEAIRQANDGDGVVVLADLGSGVMSSETAIELLEDENIKVKLADAPIVEGTIAAAVSAMVGSDLEAVLKAAEDCRGVRKIPE | Function: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone.
EC: 2.7.1.121
Catalytic Activity: dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate
Sequence Length: 131
Sequence Mass (Da): 13250
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A0A671Q8A4 | MLSSLFLLKVFFVFINSSYSSGANAKLRYQITSGNVGGVFDMEPEVGTIFIAQPLDYEQNKLYKLHVLASDGKWEDYATVIVTIVNKNDEAPVFSVNEYYGSMTEELDGSPVFVLQVLPLHSLYCANAKLRYQITSGNVGGVFDMEPEVGTIFIAQPLDYEQNKLYKLHVLASDGKWEDYATVIVTIFIIDEVTGKIYAQITLDREARAVWRFVVLATDEGGEGLTGFTDVIINVWDINDNAPLFACAPDNCNGDVTENSPPGTSVMEMTATDLDDAAVGQNAVLAYKIVGNAALNGANRGADVFSINPATGTVSVAMSGLDREQTDSYILVVEARDGGGMIGTATATIHVTDVNDHVPHFLDRSCSIRIPESSEPNTPIIELAAEDADAGENGQLTFSVVAGDPEQKFYMVSHRQEQRGTLRLKKHLDYERPGEQRFNLTIKVEDMQYSSLLHCTLEVEDCNDHAPVFIPHFLQLPAVREDVAPGTSVASVAATDLDSGLNREITYSIAPESDPYHLFSVDQSGLVTVASELDREKVAQHHLVVLATDHGTAPLTGTATIQMALLDVNDNARLISNYRHCAHLSATNYPPYISSCVERRPIGGIDRRLLGSRDRRPPPTHARRPLASQHCWTWRCPWSSLLLSSPQCRCPDPQFSPGRAPDPDLSPGRAPDPEYSPRRAPSNGRRASGGGTAPFDSLQVFSTEGGGSLAGSLSSFSSAGLEEGTAAGHECLKEWGPRFEKLKALYERAEGSDL | Function: Cadherins are calcium-dependent cell adhesion proteins.
Subcellular Location: Cell membrane
Sequence Length: 754
Sequence Mass (Da): 82169
Location Topology: Single-pass type I membrane protein
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L0EUD9 | MRFSNSFVDDLLARVSISQVIGNYVTWDKKKTNVVRGDYWACCPFHQEKTPSFHCNNNKGYYYCFSCHASGNHISFLSAIKGFSFADAIQQIADIAGVSVPRSDLQTQKSNKTEEETLISIIEMATLFFQNSLQNQSAEYARGYLNQRGINSRSIEIFRLGYAPDNRHALTEYLTERGVPREKIEASGLIVHGSDIPVSYDRFRHRIIFPIFSAAGKVIAFGGRALSKDIAAKYLNSNETILFRKGELLYNFFGARNALKRILPEEISKRKGVQPQSRETVVLVEGYMDVISLHQSGIQNVVSPLGTAITERQLQLLWQLSLHPVVCFDGDEAGFRAASRLIDLALPYLQPEKSLSFIILPNGKDPDSFIREEGKEAFELLIAQALPFVAMLWQRETVGDEAKTPEMKAALETRLQQAIERINHKTLRYHYLQDIRQRLYFLFQKNSSYQHSQKKSQRYHPSADRFSSVKLLASERLQKSKLVQGSKSQQPSLRETVLLLTLINHPQLLVEDYDELLQVTYQNPDLQNLWSCLISEFVVAQSFSHEKLLEKLQERGFTALLQSLDQQIRKVGLWSITSDADLVDARQGYQQALKLYKRSRFLYQQKVELENQIAEATEREEEEQIVSLLNRLNHIQLEIKNIENQDAMVSDSENFL | 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: 656
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): 75134
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A0A9D8KGB0 | MFDSRVLGVDPGITVTGYGVITGGKSPTVVSAGEIKPASRLTMAEKLEAIFRETEEVIEKTSPDAVAVEGIFHAKNVKSVIRLGHARGVILLAAARANLVVYEYSPREVKAAATGYGAAEKAQVEKMIKRILNLPDDVGSHACDALAVALCHLHTFKVTSSKERA | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 165
Sequence Mass (Da): 17542
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A0A671M5K4 | MLSSKKSDPGSSSSSGGNGGDRAPETLSAPQAGPAGPSGPGIADVKKKERASPSGEPGGPPLLHPPGPGGVDQDSAEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKERKQVIPPPNAFQGAAFQSRLPHDRMTSQEAACFPDIIGGPQHTQKVFLYIRNRTLQLWLDNPKIQLTFEATVQQLEAPYNSDAVLVHRMHSYLERHGFINFGVYKRVKPLPSGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNFLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKDLLNKMVATKEKVKELHQQYKEASEVKPPRDITAEFLLKSKHRDLTALCKEYDELVEMQVKLEERLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTSSGCEVIAVNTRSTTQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTAAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALMAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPAIPGASQPVPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTMPRQATANPNPQPSPSIQ | Function: Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity.
Catalytic Activity: 2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3]
EC: 1.14.99.66
Subcellular Location: Nucleus
Sequence Length: 746
Domain: The SWIRM domain may act as an anchor site for a histone tail.
Sequence Mass (Da): 82766
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D8IC81 | MFIKSNTTDIVKPSIKDEKAIENIKKAAQIAQEAIDLAFEYSLSGTRASKIDKDVEKFIKSKGAYPANLEVPEYGFSTSISIGNEIAHGRPTNKKILVQGDIICIDIGVKYNGYYADCARTMVVKGNQLSSTNKKAYKLIKACKESLEHAIYKLRPNILLSTYGREVEKKVNEYGYSIIKSLTGHGVGYEYHEAPYIYNFYHPNNDVKLEENMVLALELMITEGSDKYIIENDGWTISTADYSFAAHFEHTVLIKKNGVEILGID | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Function: Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.
EC: 3.4.11.18
Catalytic Activity: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
Sequence Length: 265
Sequence Mass (Da): 29727
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A0A968N8D3 | MAAERILAPSPIDLNCDYGETFGGSLVQDDVTLLQYVSSINIACGAHSGDPDVMRRALTQARTHGVAIGAHPGFPDISGFGRRLLHMSPDEVYNSVLAQVGALAALARAEGLTLTHVKGHGALYNHAAHDLPTATAIAQAVATFDPALILVGLSGSAMITAGEQAGVRVAREAFVDRAYEADGSLRSRRLEGAVILDNQHALAQALSIAREGTVITYAGTQIDVPAETLCLHGDTPGARERAAVVRQGLAAAGVVVRRLGV | Function: Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
EC: 3.5.2.9
Catalytic Activity: 5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate + phosphate
Sequence Length: 261
Sequence Mass (Da): 27127
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F2I8U0 | MKLETYQGASVEEAIAAAKEGLQVSDISMEDVKVLQEPKKGFFGFGSQPAIIQVSLADGEPSVDEIVAEVAVEAETVTDPVADTAPATTEVVEEATVVEALDDSQSAASQATSELSSDSQVAHTLDSQSASPSDVSDSAELEPVASQSEPASESVATDYSTTDSQSQDADYEEDEEEEAEDSSYPFDWGVEDVAHYLIDVMEAYLVDVTIDVEDMDDLIIFHINTDKPGLVIGKHGKIINSLETLAQILTHSHVRKRVAVEVNVGDYRERREQTLEKLAERTADQVTVEREDVTLSPLPARERKIIHRCLSKYSHIKTQSQGRDPHRYMVVSYKD | Function: A probable RNA chaperone. Forms a complex with KhpA which binds to cellular RNA and controls its expression. Plays a role in peptidoglycan (PG) homeostasis and cell length regulation.
Subcellular Location: Cytoplasm
Sequence Length: 335
Domain: Has an N-terminal Jag-N domain and 2 RNA-binding domains (KH and R3H).
Sequence Mass (Da): 36692
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C4V7D0 | MKEVKAATDLELLVNKIDSTGYICRLKQSVKTCKICNIKHFISHDWFTDLEKEFKDDYFETLCTKLHGKVFFPKVENIFTFTYFFPLADTKVVILGQDPYHNLNQAMGLAFSVPNNVKIPPSLKNIFQELKNDILDFVIPKHGNLEAWAKQGVLLLNDVLTVEQHKPGSHSDLGWKIFTKAILSKINETCQNVVFIFWGNYARSKSKYVNKHKHLVLEAAHPSPFSAYKFFGCKHFSKTNEYLVKNGKSPINWNL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular Location: Mitochondrion
Sequence Length: 255
Sequence Mass (Da): 29375
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F9Z9V2 | MKIKTGIGIDVHRLEAGREFWLGGIKIGHEKGCVAHSDGDVLIHAICDALLGATGLGDIGQHFPDTCPAYKGIDSKLLLQKTKALIDHRGYAISNIDSVVCLQRPKIRPFIDDMRHCLAEILELDVDDLSIKATTTEQLGFEGREEGVSAYATVLVYKL | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
EC: 4.6.1.12
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP
Sequence Length: 159
Sequence Mass (Da): 17369
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A0A1Y5TY12 | MLRHCLHLFFGMFFLPLLLAASPPAGADIPDETYEALGLTRDAPPKDLYGALIKRYYDPGKGHGKGAFGELWQPTPFTRYLDPKTLYVAPDMDFEATREECVECHSTVTPGWVHSWQKSVHGDLDEIRGLPAGDSRAYKKELIDQVEANLHSMGVLPEGQNLDDVGCIDCHMRVGALKGNHKADLKMPDAADCGQCHVQQFAERESERDTLTWPQEQWPAGRPSHALSWQANVETAIWAGMEQREVADGCSLCHTMQNTCNSCHTRHEFSAAEARKPETCSTCHNGVDHNEFEAFSMSKHGVVYATQGHDWDWQQPLSTAFGAGGQTGPTCQTCHMEYEGEYGHNLVRKVRWGFEPKPEIAENLGHEWFQDRKESWVTTCSNCHSPSFARAYLDMMDEGTKQGIELVKEARGVMNRLYEDKLLVGQTTNRPAPPKPDADSPGAFAGLFFSSGNFPTAIDYEFAEMWEQHVMKHFKGLAHVHPGGFTYSEGWSRLIRSLARIKDADTQLREKAALLQRVEMLESGGDKRGLLDLDTPVKRAAAGGAGVALAGFGLALLLLPAIRRRRRD | Cofactor: Binds 8 heme c groups per subunit. One specific heme c group is called heme P460.
Function: Catalyzes the oxidation of hydroxylamine to nitrite. The electrons released in the reaction are partitioned to ammonium monooxygenase and to the respiratory chain. The immediate acceptor of electrons from HAO is cytochrome c-554.
EC: 1.7.2.6
Catalytic Activity: 3 Fe(III)-[cytochrome c] + hydroxylamine = 3 Fe(II)-[cytochrome c] + 3 H(+) + nitric oxide
Subcellular Location: Periplasm
Sequence Length: 568
Sequence Mass (Da): 63297
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R6C9F2 | MRNEEKPGRAWLEIDTGRIRENYRSLCASAPDGCDIMAVVKADAYGHGAGRVAKLLQEEGCRYYAVATLEEAISLRSAGILGDILILGYTMPRDAFLLQHYDLIQTIVDEKHGQELAKSGSTVRAHLAVDTGMNRLGIPAKEEETILRLLKLPGIRIEGIYSHMSVADSRQKEDIVFTNGQIAEFTGLKKRLGRMGYGHLYYHCQSSYGFLYYPVPGMRFARVGIALYGCTSNSAEESYPVALKPALSLKARISCVRMVAPGEFVSYGRTYKAVEDRKIAAVTMGYADGLPRNLSGQGYAFIKGRKAPIIGRICMDQLMLDVTGVAHVQEGDIVTFIGREGENSILAVEIAELAGTITNELVSRLGSRLTKIYIG | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 375
Sequence Mass (Da): 41154
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R6CC44 | MISISEYPVPVLTGDFSHKTIHVKVPGSKSITNRALLLAMLSDGKSHLTGAQFSEDSSHFLQCLSDLSFDVASSPETGEVSVHGLSGRLPVKKASLYVGSAGTAARFLSAVLGVSEGEFFLDASEQMKKRPMAPLLSALQSVGCDISFAEKEGFFPFTLHARGFQNTDLTIDIDKSSQFLSALLIAAPLAKEDVKIKVAGTHGMAYIEMTCRMMEQFGVLTEHPSPDTFLIKAGQTYRAQDYAIEPDVSAACYFYALAALSGCSVIVDGVPEHSLQGDTEFLNILEKTGCRVTRTNEGICITGPAACAESAGVKSADAGSKTASPASHASGSVSHASHASGRLHGLTVDMSSCSDQAITLAAIAPFADSPVTITGIGHIRGQESDRLSAITENLTAMGIRCDERADSITIYPGVPKPAHIKTHDDHRLAMGFAVTGLFAEGIVIENPSCCKKTFAEFFECLEKAVENLQK | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
EC: 2.5.1.19
Subcellular Location: Cytoplasm
Sequence Length: 470
Sequence Mass (Da): 49847
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A0A9D8PPY4 | MSADDLHKWGKTERGPRSVYFRTFGCQMNVHDSERMRGLLSRDGITAVDSPHDADIIIINTCSVREKPEEKTYSEIGRYRRLKEKKEGLVIGVTGCVAQQKGEEIVRRFPYVDLVLGTKNVGAISNIISEIVSGKKPIVKTEFHDNNCIEPFEPFPRDPDNYTAFVTVIQGCNNFCSYCIVPYVRGREMSRPSTDITDEIKSLIDTGIVEITLLGQNVNSYSDPKNGLRFPELIRKISKIDGIYRIRFVTSHPKDMSDDLISCFKEIETLSSHIHLPVQSGSNKIIKMMNRGYTVEDYIDKIERLRSVRSDLAVTTDIIVGFPGEDVSDFEGTLSVMEKVEFDNAFSFKYSERPGTAAARLEDDVSPNEKSRRLEVVQDLQKRLTMKSNLKNIDSIYDVLATGLSIKDPEEITGRSDQNKIVNFKGTESAIGSVVPVKIKKAFNNSLWGEVIQP | Cofactor: Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
EC: 2.8.4.3
Catalytic Activity: [sulfur carrier]-SH + AH2 + N(6)-dimethylallyladenosine(37) in tRNA + 2 S-adenosyl-L-methionine = 2-methylsulfanyl-N(6)-dimethylallyladenosine(37) in tRNA + 5'-deoxyadenosine + [sulfur carrier]-H + A + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
Subcellular Location: Cytoplasm
Sequence Length: 454
Sequence Mass (Da): 51167
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A0A2K8NS24 | MIRCQKTFKSTTSKPTLYLVGTPIGNLADLSPRAQTILQEVDWIFCEDTRTTEQLLKHYGIQNKLISCHKFNEQSRVDKLQQILATGQSMALVSDAGVPIISDPGAKIVREILHRLPNQINVSGVNVGPAYIHALVASGYESPNHYFYGFLKSRGFEAKKRELTNVLMTLPEKTIIVFYESVHRIKETIAFLAEILPPTTSVMIARELTKTNEEIIQGPISELAAYVAADQMVLKGEFVVLVSKETNWSKNWTLDEIVQATQKLTSEGHSLKAAASIISLESGWPKNKIYQLMVEKQK | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 298
Sequence Mass (Da): 33360
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A0A2H1V1I0 | MNPSGVRFTDHLMGLSHLSQNKTATLFTQLYRGHATRTVMPLANLYDDIRLILRSEGDLSTEGLSAGPPKDLTVTTKKFFRELFPVAYHNVLKLDAKQFTPDYEICLKDAYDAVQPFGDVPQQLGTSLARSLEAARALLQMLAVGADTLSAAEHVLASGADNCAERLLRTGGCSRCHGHEARPCRNYCLNVARGCIGSLLSELDGPWAGYVEGVERLTKVDADVALRELETKVSKAIMYALENRAVSENK | Function: Cell surface proteoglycan.
Subcellular Location: Cell membrane
Sequence Length: 250
Sequence Mass (Da): 27370
Location Topology: Lipid-anchor
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A0A225MRK4 | MTKPLNKVFIASRGEIAVRIIRACRDAGIQTVQAYSTADSETSAVHMADESICIGGPKPSDSYLNATALIDAARHSGADAVHPGYGFLSENADFAQAVEAAGLVYIGPQPEIIRMMGDKVKARQCAQEAGVPVSMGSPDTIESDEQAIDIANRIGYPVLIKAAAGGGGRGMRVARNEAELKDNIGRAIKEAETAFGSGAVYIEKFLERIRHIEVQIFGDGNEVIHLGDRDCSIQRRHQKLLEEGPASVLDPETREHIRNAARQLGQSLGYRSAGTVEFIVDPRTREFYFIEMNTRIQVEHPVTELLTSTDLVAMQLAIAAGERLSLKQDDVKLRGHAIEVRINAEDPNKAFIPRAGTITQFHMPSGPGVRVDTHVYPGYDLPTNYDSLLAKLIVWGKDRNQAIARLRRALCEVHIEGVTTNVKFHQRLLAEADFLNNDTYTQFVKEQMYSKHPMRNLL | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
EC: 6.3.4.14
Catalytic Activity: ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate
Sequence Length: 458
Sequence Mass (Da): 50438
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A0A6V7VMF6 | MKRLDCKALHYQWGRKGAESTVAQLRKDTIEEDEFYAELWMGTHTRGPSQVKEGEARIPLADYFRDHPDVLGQHERDGVGLQFLLKVLSVGKCLSLQLHPTREQARELHAADQTNYPDANHKPELTIALTNFEILCGFQMPDKILSNLRSHEALVELIGEKVLSSFGATTDEEEKKGALKNIFTQIWTIPPEEIGTLLTKLLSDIFLKEQRSQTDELIMGLSEHFPEDIGILAPLFLNYVKLEPGQATFLGPNEPHSYLSGDCIECMAQSDNTVRAGLTPKFKNVPLFCENLTYRMGGPPIFEPQHLAGGVFEYSPEVQEFAVHKLNKEVSVVQPIAAASILIVVNGSATILPSEGNEEKIEKGDVLLLPQQLGAKLNENSDDFLAFRAYTPPPKEK | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 397
Sequence Mass (Da): 44316
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A0A0P8Y625 | MRLMGKSSYNSFGILGGSFDPPHLGHLRLCEIALKKLKLSKIFWVVTKKNPFKKKAFFSLKKRLYESKKISKSNKKIKVIYLDKKIRSSRTINVIEYLRKINKANKIYLLIGSDNLVSFHKWKDYEKIIDLCHIVVFSREGYDKMARKSAIMESFKNKKIKFIRNKKINISSTIIRKYYNNQ | 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: 182
Sequence Mass (Da): 21532
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I0HG84 | MPVAAPPRERVTDDPLHAHGGGHRGGHGAGHSGGHGAGHSGGHGPGDGHPAGAPAGEAHRDGAPAVPPLTATAPPAEPEADPPALPIEEPGESPAEPLTEAEVDGEALAAEIGNELAAQSGESPQTGESPQTGQSPQTGEPQPAPARAEPHEWRGIILVTGTDTEVGKTIATAAMAAAAQAAGLRVAVIKPGQTGIATGAPTDAEVITRLAGPETVRTLAEYPEPLAPLAAAKVAGQAALDLFETVDAIRAEAEKHDLVLVEGAGGLLVPMGLRPSGEPWTFADLATTLGANVIVVARAGLGTLNHTALTLEALHRRGVYARVILGAWPHDPELVHWANLGELVPHLVGALPSDAGSMDPGVFRRSAPGWLTPALHGVLDNWRVWAEEAG | 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: 390
Sequence Mass (Da): 39481
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A0A1G1LR46 | MISPAEAMVLIRRHAVKPKIKIARLGECLGAVLAADIRAPFPMPVADNSAMDGFVIRSKDAGLASVKNSVRLKIIGTLKAGDSKQVHLVSGTACRIMTGAFMPQGGDCVIAKEDAVIVGNHLIVKHSVCEGQHIRRRGEETRKGQKLLTQGVILHPARIGILATFGYARVPVYCKPKVAVLATGSELVTPGKKLSRGKIYDSNSWMVCAALERMGIDPSRVLTLRDDRGKVKKAILDVLRESDYLLLLGGVSVGDYDVVKDALKQSGVKTIFWKVSQKPGKPLFLGRKYKKVVFGLPGNPAAVFTCFYEYVYPALRQTMGFVRPGLEEETVKVSGRVLPDSKRCLFLKAKMEVRSSWRLPKARILSHQGSHMLSSLAEADGFLKVPASGNSAPNKKGFQMDFLPYEVDGEKDVK | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 414
Sequence Mass (Da): 45197
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A0A4Z2DEG1 | MVMDTTCSPMTERYLLSTYRHVLELFILISMSVFGAKSVLKLFKKYKGEFLRAGFAGVDMNKPTKPTIPEAQGVICGVVFLSIMFLFIPVPFWRFLVRKAETQSNEICSSDKIREGQEAFFKSQFIQYLAGLLSVCCMLFLGFADDALNLPWRHKIGFPFVAGLPLLMVYLANEGTTRIAVPVMFRGSLGGSVDIGVLYYIYMGLLTVFCTNSINIYAGINGLEVGQAIVIGASLILFNLIELMGYHWRVHLFSLYFLIPFLAVCWSLYRVNRYPAKVFVGDTFCYFAGMTFAVVGILGHFSKTLLLFFLPQIINFPI | Pathway: Protein modification; protein glycosylation.
Function: Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis in N-linked protein glycosylation pathway: transfers GlcNAc-1-P from UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol.
Catalytic Activity: a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP
EC: 2.7.8.15
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 318
Sequence Mass (Da): 35821
Location Topology: Multi-pass membrane protein
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A0A357LBX1 | IERAASEIGAALRDKAAYTVVAVKSTVIPGTTDGVVLHALERASGKKAGPDFGLCMNPEFLREGSAVEDFTKPDRIVIGAIDPRAAEVFGRIYAKFDCPKPVISLRNAEFCKYASNALLATLISFSNEMAALCEATPGADVEVALDCVHLDRRLSPVIDGQRVKPGILSYIRPSSGYGGSCFPKDVAALRAFARDRGVDAELLNAVSAVNDRRTAAVLDLAEARIGAFKGKRVGVLGLTFKSGTDDLRHSPAVTLTEQIIDRGGHVTVYDPIATEIARNAFGDKVRYAAGALDAVNGADVTVIGTAWPEWSALNWAAVKSAMRGNFVFDARNSLRALSLDPGLVRIQIGAGA | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 352
Sequence Mass (Da): 37300
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A0A671KWV4 | MPAKCLTIFLFAFCFAFCAVASALVKQKLAQVILKKQKAVLERTNSNPLSSPSVAYRLETALITAHSCLSAHAHRLMCFSSDFKIKVFSSEPNLKVKHKLKKHLNTRKSPLTRKESAPPAVKHRVPDTLGNYNTLPLLLRSVVIIRRSHTFFPCSNTSQKYNMIFYFRHLSDIVFIKHPEILSLQSRLWETQKQLQHLRRQTAHMETLAVPMMLGAAHRPLSRTQSSPASTSLTLPDKALPLTTAQEPPQSQPRFTTGLVYDSQMLKHQCTCGDNSSHPEHAGRIQSIWSRLQERGLRGQCESIRGRKATLEELQSVHTERHVLLYGTNPLNRLKLDNRKLAGILSQRMFVMLPCGGVGVDNDTIWNEMHTSTASRLAAGSVTELAFRVAKGELKNGFAVVRPPGHHADPSNPMGFCFFNSVAIAAKQLQQKLSASKILIVDWDVHHGNGTQEIFYNDPSVLYISLHRYDNGNFFPGSGGPAEVGSGAGEGFNVNVAWTGGLEPPMGDAEYLAAFRMVVMPIAQEFSPDVVLVSSGFDAAEGHPAPLGGYRVTAKCFGFLTRQLMALAGGRVVLALEGGHDLTAICDASEACVSALLGLEPLPESTLLQTPNANGVLSLQRVLQIQSECLALLSSQSASNYPEMHWLPGSTHLFNSLSLIIIMIIVVAPHGSCSAKIFL | Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]
EC: 3.5.1.98
Subcellular Location: Nucleus
Sequence Length: 679
Sequence Mass (Da): 74477
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A0A2K6PQI9 | ASSARPCPPESRKPRWRRSLARARGRADGRCPSPGRETAVGTAGLGTEERRALEREQARHGDLLLLPALRDAYENLTAKVLAMLAWLDEHVAFEFVLKADDDSFARLDALLAELRARDPARRRRLYWGFFSGRGRVKPGGRWREASWQLCDYYLPYALGGGYVLSADLVRYLRLSRDYLRAWHSEDVSLGAWLAPVDVQREHDPRFDTEYRSRGCSNQYLVTHKQSLEDMLEKHATLAREGRLCKREVQLRLSYVYDWSAPPSQCCQRREGIP | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 273
Sequence Mass (Da): 31390
Location Topology: Single-pass type II membrane protein
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A0A6C0N8C5 | ICQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLSSSGVEAGVGTGWTVYPPLAGNLAHAGSSVDLAIFSLHLAGVSSILGAIN | 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: Membrane
Sequence Length: 123
Sequence Mass (Da): 12978
Location Topology: Multi-pass membrane protein
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A0A381H474 | MPLSDSEKAALPKTDIRAVHEALDVEHRAYSREDDSPQGSVKARLEQAWPDSLAEGQLIKDDEGRDQLQAMPKATRSSMFPDPWRTNPLGRFWDRLRGRDVTPRYLSRLTKEEQENEQKWRTVGTIRRYILLLLTLAQTVVATWYMKTILPYQGWALINPADMIGQDLWVSFMQLLPYVLQTGILILFAVLFCWVSAGFWTALMGFLQLLIGRDKYSISASTVGNEPLNPEHRTALIMPICNEDVDRVFAGLRATWESVKATGNAAHFDVYILSDSYNPDICVAEQKAWMELIAEVQGEGQIFYRRRRRRVKRKSGNIDDFCRRWGNQYSYMVVLDADSVMTGECLSGLVRLMEANPNAGIIQSSPKASGMDTLYARCQQFATRVYGPLFTAGLHFWQLGESHYWGHNAIIRVKPFIEHCALAPLPGEGSFAGSILSHDFVEAALMRRAGWGVWIAYDLPGSYEELPPNLLDELKRDRRWCHGNLMNFRLFLVKGMHPVHRAVFLTGVMSYLSAPLWFMFLALSTALQVVHALTEPQYFLQPRQLFPVWPQWRPELAIALFASTMVLLFLPKLLSIMLIWCKGTKEYGGFVRVTLSLLLEVLFSVLLAPVRMLFHTVFVVSAFLGWEVVWNSPQRDDDSTPWGEAFMASRFPAAARPGMGGWHGLAGFTFPVLAGADCLLADPVAVCVRGFQPFNGRLAHQTLEAVPHPGRVFPAAGAGGY | Pathway: Glycan metabolism; osmoregulated periplasmic glucan (OPG) biosynthesis.
Function: Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
EC: 2.4.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 721
Sequence Mass (Da): 81383
Location Topology: Multi-pass membrane protein
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A0A6V7U879 | MFSSLKRANYNVIEEVEDENEPGTLKSMELGRVTDIKLNEEEEVEEECHQHFESSAPPIHHGVAVSFSGKGDAELQASSDPAAEWDHIKDVDQFFAYIYEYYQQRGLTCIALRSLFSLLRFAFVVLFSTFLVNCVDYDVLFYNRNTTLDGRPLPAKRAIHNAFIPRCYARINPLMSLALFLAALFWLAHLFRIFCRLVQFSEIRRFFISQLEIADSEMQNLTWAQVVERLCGVQKRLHLIVNREAITPLDVCQRILRHKNYFVALVYYNILPPRIRLPFFGHVHYLSNGLRFNLEWLLFWGPWSPWKGPYALKDEFKDPAKLPMIVRQLQRTLTIMAIANLIFFPFVFVYQLLFSFFSYSEHYQRDPNVFGMRKYSNYGREKLRHFNEMDHELDARLNKSYEFAARYTDQFISPLTQIIARNIAFVAASFFVVLCALTAIDEDTLKIEHVTTILSITGGAVLISRIFIPKENMVFCQHLLMQQIVANIHYAPRSWLANAHSTEIHKEFVQIFRMKTELLIEELLSPFLSPFILYFCVWKRVPEIVVFLHENTVTLEGLGDVCSLAQMNIARDGDTRLVSLNQSVCVDDNENNKNKVSTRRRRTPCGKVELSLLNFATQNPDWVPSGPEAEFIANVKDLVSTEVFGILENMENQRLLYQRSNNKSVVLPTNAEKNYPSTLQKSSEENVTPTTSQQQPGPVLAEQKEEETFTGVGGLPSASQIERQRQLQEQSLANILSNSSSLRGMLTTSIHSQLNLQQQHQMLLASSFIAPASLSATVQPRTEQENKATEMSLNALAINHILAINTNPNELIQQQQNVRSRYNKNNRGYGSIRNKGGIITETQPILDSMAESNIWGVPDLTATSRLNNLFTSSINSSSMLLGGGERGGNFKGREKEEEEEMKQLNKTVKEQPSTTTSLSITAPPPPPLQPFYVDDKKVLKK | 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: 941
Sequence Mass (Da): 107531
Location Topology: Multi-pass membrane protein
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R6BKG4 | MQIKSGIDIIEVERIKSSIDEMGDNFLDRVYTENEIQYCESKKKNKYQSYAARFAVKEAAFKAVSTLIKDKYSISWKNIETTNDENGRPSVKFISLTKEVEKELAKIESIDVSISHLEKYAVATVNILF | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
EC: 2.7.8.7
Subcellular Location: Cytoplasm
Sequence Length: 129
Sequence Mass (Da): 14809
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S2XNT2 | MNEWKKLNQKIASQSLKKKWAISSAAVIFLSFATMSIILYVALKGWLYQQEEQEVNRTMQDLTAFFESQGPFLTVQDIQSNTGLMKSIVDKDQTVRLLNADGIEVLQINNTSTFKAFKDIDVPEEGYALNDYDNSSISAIGNVRLGRFKGYIQLEHPLKSFQSTKTYILTAMLLFSVCALLLSGWIGYILASYLLKPLKDLKMTMDDVVAHGFEKELTISYDAKDEIGELIIVYESMMAKLKYSFEQQQQFMADASHELRTPIQVVEGHLSLLNRWGKDDPEILEESLGISLREVHQMKTLVDEMLELARGEQMKAQPPTNILEQTEEVIEELVQVYPTAYIEHKIPIDRSLHVLISSNAYQQIMRNLLINAIRYSTEPARVHISYERKTKYIIVHVQDQGIGIDPQHETKIFDRFYRVDMARSRDLGGSGLGLSIVKMLVENARGSITVKSELGKGSTFSLVLPLIE | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 468
Sequence Mass (Da): 53203
Location Topology: Multi-pass membrane protein
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A0A1G7BKI2 | MVAAIVAFCVGVLFCLLLTRPAIVVLKRLGWSQFVRADGPQTHLVKKGTPTKGGLVFGAGTVVAYAVAHAVTGEAVTTSAVLVLLAMVGMGAVGFVDDYLKTHHQNSAGLPERAKIVGQLLVIALLVPVALWGADRAGRSLVSSSITFVGDVELLDLARWGPVVAVVLALAWYGFLSIGTTNGVNIVDGADGLLAGCAISSLSAYALMLVFQAQNSCSGAGGAGCFDTVHPQDLAVVTCALLGNLVGFLWWSCYPARIFMGDTGSLGIGGFLVALAVLSRTELLLPVIGVIYVMVTSSVLIQRYYFRFTGGKRFFKMAPLHHHFELSGWSESTVTIRFWLISAFGAITAIMIFYSTWLARTGSAGP | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
EC: 2.7.8.13
Subcellular Location: Cell membrane
Sequence Length: 366
Sequence Mass (Da): 38575
Location Topology: Multi-pass membrane protein
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A0A969FTQ3 | MNDLSTESVLTGTAAAPGIAIGPALRYRQPAVAGHGFRLVQAESRYRETGTAHLEIQRLDEAIAATDAAMRETEARLQAEGKGAESHIFESHRALLHHPGLYDRAVTLISKAGWRAPDAIVEAGEHQASPLGDTDNPYLKAYAANIRDVVGQVRRFLVREQTLADLLTRPSIVVADDLGLSEWMDVPRERLLGLALAAGGTTAHSMIMARSLGIPTVIGLGTAALRTLRDGVMLALDGTTGQVVVAPSEETIAHLRVVAAELAEHQAAMYRQRDLPSITRDGQHVVLLANAGTVIEAQAAREWGAAGIGSLRTELLFLGQPKLPDEEEQLALYQAIAAELPGCPVTVRTLDVGGDKHLPSFPLPRESNPFLGWRGIRIGLSQPEQILLPQLRAMLRAGADADVRIVLPMVTTVSEVREVKALLQQAHGELVAAGVRCCAVPRLGVMVEIPSAALVADCLARECDFLSIGSNDLIQYTLACDRTNQRVANLYQPLEPAVLRLIANVIEAAHRYGQRVSLCGEMASDPTLTALLIGMGVDELSCTPMALPLVRAAVRATSAAKARELAQAVLQAACLDEVQVLIHTYGPTEVEVEGEGEG | Function: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr).
Catalytic Activity: L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate
EC: 2.7.3.9
Subcellular Location: Cytoplasm
Sequence Length: 598
Sequence Mass (Da): 63924
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A0A6N4RCA1 | MPTTSAAKAPATVLVVFGASGDLTKRLLMPALYNLAGNHLLDEEFEVIGISRSAMSDAEFQGKQAEFMSTFTQQRSGDSSQKLDEVAWKWLEKRLSYTSASFTEDDTYQQLSKRLGKRNAVFFLAVPHEAFLPIVNGLHANGLMQQGKNTSRRVVIEKPFGHDHASAINLNQHMLGMFKEEQIYRIDHYLGKETVQNISALRFGNRLFESTWNGEHIESVQITAAETVGVEGRGSFYEPTGALRDMIVNHLFQVLSLITMEPPATKSADAIRTEKAKAIQSIVPLSETDLQHDVVRGQYTAGTVNGKDVPGYTQEDSVAPISGTETYLAMRLKLDTPRWKDVPFYLRTGKRLATRKTEIVITFKQPTTWTQDPVAANTLVLRLQPEEGITLFVNAKVPGQTQELQSVALDFGYKNAFELKPNTGYESLLYDVFIGDQTLYNRADIIEAGWEKIQPILDAVAQNKLKLHPYAAGSEGPQIADNLPCRSGHEWRKLV | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Length: 495
Sequence Mass (Da): 55209
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A0A9D8PLU6 | MDNVIWIIPLLPLAGFLINGLGGRRLPDWLVSLVGVSLPVASFVLSVWAFLKLLKLGEGAEVTCTLYTWIFSGDFQVSLAFLLDPLSAVMALVVSGVGSAIHLYSVGYMHDDKSFARYFSFLNLFLFSMLVLVLAEDLVLLFLGWEGVGLCSYLLIGFWFDDMEKAKAGKKAFIVNRIGDFGFFIGMALIVLTIGTLNVPGMKEILESNPGVITTGMATAITLFLFVGATGKSAQIPLYVWLPDAMAGPTPVSALIHAATMVTAGVYMIARLNFLYVLAPTTMIIVALIGSLTALYAATIGIAQNDIKKVLAYSTISQLGYMFTAVGVGAFASGIFHLMTHAFFKALLFLGAGSVIHAMSGEQDIRKMGGLREKMPVTFWTFLIATLAISGIPPLAGFFSKDEILWKAFSTHLGGIGVLFWALGLVAAVVTAFYMFRLFFMAFTGESRASEDVKKHIHESPVSMSSVLILLGILSAVGGFIGVPELLGGHNTFERFLEPVLPHLGSRFSEHDAHLWEIVLLALSLVAAATGIFLAYVMYVKKTDIPKNFAKNYKAIYQLVYDKYRIDELYDRVFIRPFFALGRIFSGVVDLWIIDGIVRLVTAMTAGLGRAFNVSQAGDVRVYGRVLLGGLLLILIIVVFGRV | Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Membrane
Sequence Length: 643
Sequence Mass (Da): 69987
Location Topology: Multi-pass membrane protein
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A0A7S0SDK7 | MGRHKRQRLPAALFIGGSSLIFATFVFVAPAMPRLNPATLDFPPVLHAVQTTADAHGAGKDTPREFVAQHGKQMDEVPVRVGLPFIPARDEAGRAVSSGTGAHNLREEVTMAGQADNPELVSSASEVSAAHARMDAPFGVRVEHGSELQANVIDPRSIQIVSLDNPRAFLYKRFMSDAECDFMVAHAKPNMYKSGVVNADSGGSSLSNIRTSTGSFLPLGMNDLVKRVEQRIASWSQIPVSHGEPMQVLRYEIGQEYQPHFDYFFHKGGSANNRIATVLMYLSDVEEGGETVFPNTQKPERRNETQFSKCGNTGKAVKPSKGDAILFWSMKVGGELDGGSSHAGCPVVRGEKWTATKWMHVSSLRLPDAHHKVFYEGREVSTESCNDTHATCHGWAEQHECTKNPGFMLEACPLSCKTCSGRWQAGSYQQPSTLAAAA | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 438
Sequence Mass (Da): 47698
Location Topology: Single-pass type II membrane protein
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D8IDY8 | MNITAKTTLTALFASPCKHSLSPIMHNKSFEKLSLDYVYLAFEVDKNNLKEAVASIKTLNMRGVNLSMPNKKEVIQYLDNISESARLSQSVNTIVNDNGVLTGHSTDGKGFIKSLEEENVNIKNSDVTILGIGGASISIITEFALYGVKEISVFKRDNNWTEQKKIIDNIQDKTNCKIELYTLDNKKELKKQIDKSKLLINATSVGMKEDASIIEDKTFFRDDLIVADCIYSPAKTKLLQIAEKENCKIINGMGMLLYQGALAFEMWTSKKMPVDYIKNIIFN | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 283
Sequence Mass (Da): 31766
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A0A1F7FE20 | MQNKLRLLPSVDRALQNPKISAAATVYGPETVKNELRKALDSIRKEILANENAEIAAAEELIEMIADRVIAGCKIISQPSLRPVLNATGILIHTNMGRAPLGKKVFADICATITGYSNLELNLETGERGSRNIHASSLLKHITGAEEVLVVNNNAAAMVLALTTLAKDREVIVSRGELIEIGGSFRIPDILAASGAKMIEVGTTNKTRLSDYENAITTNTAILLKAHKSNFSVNGFTEEVELAELVKLGKKHNIIVLYDLGSGLLVKPATLPLASEPDVKSSLATGVDLLTFSGDKLLGGPQAGIICGRSELVKRLAKAPLMRALRVCKLTLAALNSVAKCYLDEATMLEALPLFTMLNMTPEQLHQKAQRFQQILRQHDVSVELTETTGRSGGGTLPDLAIKSWGVVITCDEKSQQKRSDFASRLFYGLLALEKPVMAILRQGELVFDVLTLEEEDFAGIAAALQSLTGHGCRQ | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
EC: 2.9.1.1
Subcellular Location: Cytoplasm
Sequence Length: 475
Sequence Mass (Da): 51263
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A0A9D8PQD8 | MEKELKELEDMIKYTFRDKDLLRLSLTHSSYVKGEDVFGNERLEFVGDAILDLVIAKALFELYPDRDEGWLTQVRSGLVDDQTLFAKAESLGLGEYIVLGKGEASQGGRTKPSILSGAYESLVGAIFLDGGYEACESFVKSEFQSVLIVDDDHDPKNAKSVLQEIVQKESGDLPKYEVISEEGPDHKRKFVVAVYIDGVEKGRGEGRSKKEAEMAAASSALDIEE | Function: Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
EC: 3.1.26.3
Subcellular Location: Cytoplasm
Sequence Length: 225
Sequence Mass (Da): 24892
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A0A1Y1S156 | MEKINNFFVIEGLDGSGTTTQLHRIGRRSEGLSPVLFPTFEPTDNPIGQLIRKILHKEVTVPHDTLMRLFSADRSLHLFEKNHGILDRIASGETVLSDRYLFSSVAYQSLYASLDDVLQLNHFPLPQRVFFIELSPELCASRRKTRSKEELFDETEMQRKIRDNYYRAFECFPDLDIQIIDGSASIDEITRIIWRSLPYPPIE | 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: 203
Sequence Mass (Da): 23532
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A0A9D8KGQ5 | MEEKYMRRALTLARRYEGRTSPNPPVGAVVVLGGEVVGEGFHKGAGHPHGEAEALNAAGKRAKGADLYVTLEPCSHHGRTPPCTEAILKSGVKRVFIGTDDPNPIVMGGGARILEDGGVQVSFVEPGGRLGRDIRVLYEAYKKFVVEKRPFVVLKAAMTLDGKTATSTGDSKWITSERARRFVHGLRKRYDAVLVGIGTVKADDPELTVRLTVGRNPTKVIIDPRLEIDTGANIFTKGFTKGGADVIIAADEGADEEMAKKIEGTGATVIRLKRGEGREGGLDLDRLLSELARRNIMSLLVEGGAKVFTYFIKYGKFDKIIFIYSPRILTGSDPLGLTAGEGPREIGGAVKLENVSVSRIGEDIAVVGYRMGGQGRV | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 377
Sequence Mass (Da): 40527
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A0A2N3DM33 | MTPRIIIAARPFEEGKARLSAALSPAARARLNRRLFDHVLAAAGPERCIVVSRSAALLDRARAAGATGLAETGTELNAALTEAAAAAGEGPLLALSTDLPLLTPADIAAMIEAGASADIVAAPDASGTGTNALLMARPGLIPYRYGPGSFTAHQDAARRAGLHFARIDRPGLAQDIDTPADLARLPPDFRRP | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
Function: Guanylyltransferase that catalyzes the activation of (2R)-3-phosphoglycerate (3PG) as 3-[(R)-glyceryl]-diphospho-5'-guanosine, via the condensation of 3PG with GTP. It is involved in the biosynthesis of a derivative of the hydride carrier cofactor coenzyme F420, 3PG-F420.
EC: 2.7.7.106
Catalytic Activity: (2R)-3-phosphoglycerate + GTP + H(+) = 3-[(R)-glyceryl]-diphospho-5'-guanosine + diphosphate
Sequence Length: 192
Sequence Mass (Da): 19801
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A0A7K0K0Q5 | MCSDNPPLPGSMARARELVEILVSKGVRNWYYAPGSRDAPLGYALAGLAETRAIDLVVRIDERDAAFMALGAARVGKLAAVVMTSGTAVGNVLPAVMEAYHAQLPLLIVSADRPASLRGTGANQTTWQPGMFRNFVGFEADLQPEDGLAALREAALRAVEVSLNGSRENATNLGMALAEFSPNQPDLNRPLRNTPTDPGRSLSSTPLHNAPTNPAVQFASATPPSSPDPLCADAPTIPPHEFPGPVHLNVSFVEPLVPAEVEAAFAAKHPAPAPASVPVPVPASEPVSAPDAVAGPGFTGSVIIVGDNQGGPDWRAGERDLWELATSCHLPVLAEPTAGRWRHHPNAVRAASRIVGETALGSGVTSGAVIGRATLTRPIARLLKRLKGMNSLVKMSELAQGSFASQLTENSRKWLENWREEGERLAAELTREWGIHQAACAIWEAEQDIDLFLGASLTIRAFDAVAGTSGVLPSERGNPADSDRVPDLKRIHEPRLSRRVFTNRGLAGIDGTIASAWGVALASGRAVRAVMGDVTFFHDLGALSYGSLETTPNLQVIVLDNGGGEIFAGLEHGQAAPPVRERMFLTPQRPDPAALAAAAGWVVETVRNLGDLRAALARPVNGLSLLRVVLP | 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: 631
Sequence Mass (Da): 66583
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A0A1S8CZS7 | MKGKFIVIEGIDGSGTSTQSQLLFDYLNNQGNKSHLTYEPSNGPIGNLIREIFKGRVTVCSDEILFDKQLALLFAADRHDHLHNPIDGMENFLNKGLNVVCTRYFFSSYVYHSRTHEERQFLYEINKDFLKPDLIIYLDNPIDVSLARMSNRSVKDAYENIEKLKIVKKNYDLVIQEYQGEVVKIPADLPVQNIHQRIIDSINNL | 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: 205
Sequence Mass (Da): 23651
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A0A2X2YG99 | MSPTVAASVWRGWRWWVSHKVNGVSELHSNLMVQSLFADFASIFPTRFCNVTNGVTPRRWLALANPSLSEVLDENIGRTWRTDLSQLSELQQHCDFPLVNHAVRQAKLENKKRLAILIAQQLNVVVNPKALFDVQIKRIHEYKRQLMNVLHVITRYNRIKEDPEAEWVPRVNIFAGKAASAYYMAKHIIHLINDVAKVINNDPQIGDKLKVVFIPNYSVSLAQVIIPAADLSEQISLAGTEASGTSNMKFALNGALTIGTLDGANVEMLEHVGAENIFIFGNTAEEVEELRKQGYKPREYYEKDAELHQVLTQIGSGVFSPEEPGRYRDLVDSLINFGDHYQVLADYRSYVDCQDKVDELYRHPEEWTAKAMLNIANMGYFSSDRTIKEYAENIWHIDSVRL | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate
Sequence Length: 402
Sequence Mass (Da): 45770
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A0A1V5W9M8 | MKFQRIFCVFSPLYWTLTYLRNKAYDTGLYSSTSFTTPTICVGNITVGGTGKTPHVEYICSLLQDTFRTAILSRGYKRKTKGYLLASPLTTVDELGDEPYFLYKKLQKTNVAVCEKRVLGVTKLLQDNPTIQAIILDDAFQHRAIKSGLNIVLIDYNRPIWNDCVFPGGMLREGTYALERAHSIIITKCPNNLTNTEMEMWKRKLHITKQTLFFTTIKYTSIYEAESKKQHDIPTILSSKHILLVTGIAQPKPMYTFISQYCKDITHLNFADHHIYTNDDYALILQQYKTYRTTIVTTEKDAPKILEITRNQLPIYVLSIGITFLNDSETEFQSLIQTHISK | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
EC: 2.7.1.130
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Length: 342
Sequence Mass (Da): 39300
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I0HBP8 | MDVNHRTLPRRKVERTVTTRSEDTQTMDHAPQLIQERSAPPATLVIFGASGDLTRRKLLPAVESLARHNRLPDQFALVGVARTPMSDEQFAESALGGRSLAEKRQLNGGIRYVAGGYDDPETFKRLAEVLDELDAQRGTSGNRLFYLSTPAGAFEPVICGLAGAGLNQESENTFSRLVIEKPYGRDLATARELDGVVHQAFEESQVFRIDHYLGKDTVQNVLALRFANSIFQPIWDRSWVDHVQITVAETLGVGTRGGFYEHAGAMRDIVQNHVLQVLALALMEPPVSFEGENLRNEKVKLLQAIRLPTDRDIADAAVRGQYTRGGTREELMAGYREEVGVDPLSRTETYAAMRLNVDNWRWAGVPFYVRTGKRLPARVTEVALQFQRPPHLPIPTSQLTELDADALVLRIQPNEGISLRFGAKVPGHSFRVRTASMDFSYENTFVEESPEAYERLLLDALIGDASLFIRSDEVQQSWRVVDPIIEHWANDRSPIPTYEAASWGPTDADRLIGRNGRKWRNAA | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3.
Function: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone.
EC: 1.1.1.49
Catalytic Activity: D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH
Sequence Length: 523
Sequence Mass (Da): 58536
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Q0AZ74 | MLLDYHIHALAHGEYDYSESWLRLFAENARRERLAEIGFSEHDEYLPRIKPDKLKRLQEDFPELKIRMGLEVDYHPGREKEIQQMLVNSNIDYDYIIGSVHFIDGWGFDHPDFKAQFATQDIDDIYADYFSLVNQAVNSRLFDVVGHLDLIKIWGHRPVKKSILAYVEPVLNSIKAAGMVVEINSSGLRKAVGEIYPSRQILEPMLALNIPITLGSDAHHPSQLGEGLEEATGLAQGVGYRQLVTFSGRRRQLVKI | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 256
Sequence Mass (Da): 29257
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B1H0L4 | MNIKQIEDEYFMHTYKRGDLVVKETKNQFIWDENGRKYLDFFAGISVCNVGHCNEAVIKAAKKQLDSFSHVSNLYYAPPQIKLGEELVKRTFPGARVFLSNSGAEANECAIKIARKWGFLNPSKEGNRYEIICFFNSFHGRTLTTLSATGQDKFHKFFKPLQEKFVFAEINNMDSVKKLANNRTVAIMIEPVQGEGGIIPSDETFLKELRAFCDDNNFLLIFDEIQCGMGRTGKLYAFENYGIKPDIVTLAKSLANGLPLGASIAGEKCAGTFLCGDHGSTFGGNPVSCAAALAVLNIINSEFLNNSLKIAEYLRIKLENLKDKYSVIKCVRGLGLMIGMDLKINGKDIVNYCMDKGLIINCTNDTVLRLLPPLIITKKDVDFAVKILEGALKWQLTK | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4.
Catalytic Activity: 2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde
EC: 2.6.1.11
Subcellular Location: Cytoplasm
Sequence Length: 398
Sequence Mass (Da): 44407
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H3CDZ9 | AVISMCGHLFCWPCLHQWLEMRPSRQQCPVCKAGISREKVIPLYGRGSTSQEDPRLKTPPRPQGQRTEPESRGGFQGFRDTGFHMSFGIGAFPFGFFTTVFNANDPFHRPGNGNLNNGNNNWQDSLFLFVAIFFFFWLLSV | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 141
Sequence Mass (Da): 16049
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E1QWQ9 | MVDDSSGRLVLVDLADRELGFCEKLPCHQKGLLHRAFSVFLFDGNKVLMTQRSLCKYHSGGLWTNSCCSHPRVGEGLDEAVARRLYEELGISGVTCREAGHYCYRATFDNGIVEYEYDHIFVGDYAGPLSLDPTEAMDARWVDAAHVARDVRKRPETFTAWLPGVLPIAFAAQAVRW | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Length: 177
Sequence Mass (Da): 19841
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A0A1G2HME8 | MFSKKYRLSVKEFENTIKKGKSYSSKFFFLKLLKNNYGVIKIGVAVSKKLAPKSAQKNYYKRILRHLLKESCPKTSVHYNVILTAKENIKNVKFNDLKQDAIELLQKTELHK | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 112
Sequence Mass (Da): 13111
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A0A1G3H2Q7 | MGGLGTAICKALSQSGFTVAANCLPNFPPRDEWLVRMKAEGFDFIVAEADVSNNESCAAMIKKLEEEVGTVEVLVNNAGITRDNLAMRMKDEEWDLVIETNLKSVFRLSKLVMRGMMKARCGRIINISSVVGEGGNPGQINYAAAKAGVAGLSRALAQELGSRNITVNCVAPGFIDTEMTRGLSDAQRDALLARIPLGRLGQPDEIAATVVFLASEQAGYITGSTVHVNGGMYMT | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
EC: 1.1.1.100
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Length: 235
Sequence Mass (Da): 25073
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A0A671S2D4 | MAERGAHLTTAASAENRPSIFEVLAQDSLMSAVKPALLHAVKILATSNPARYGFLWQRFDEIYAILDVLLQHHFLSHTSASFSENFYGLKRVGEDGTRAAHLGLRRRQHWRSLFLLALLPYLHTKLEKVLARQRDEDDFSIRLPQSIMQKLYRAFLAAYPFVCMAWDGWVFCHQLLYVFGKTRTHSPLLWLAGVKLSYLTANDIHSLDLKPSGPALSPSQSFGEKFQRLVSTAVGGLAVSLSTSLSIGVFFLQFLEWWYSSENQSTVKSLTSLPTPPPPLHLHSQETSHTHIKVKLQQESEFLSPPLSPLSFNRPPKA | Pathway: Protein modification; protein ubiquitination.
Function: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling.
Subcellular Location: Membrane
Sequence Length: 318
Sequence Mass (Da): 35864
Location Topology: Multi-pass membrane protein
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A0A2E1XFG3 | MNLLPQFGFFELMLVAVVALIVVGPKDLPKLMRSAGRMVAKARSLAGEFTAAFDQMAREAEMEELRKEIDELKKNNPVADAKRAVDEAVAPVEKEFRDEAREIDKAVREQTSEKSSAPSSASDKAASNPSANEAAKS | 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. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 14909
Location Topology: Single-pass membrane protein
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A0A225MYF0 | MTLNPSPDPLPFDRAIAVKTFLRPIATHLEDPDVTEIAIVRPGELYTREHGAWQLHECQVLTYPHLEALATALAAYNHMAKAPILSVLLPRGERGQIVQPPACLDGTMAINIRKHTQAAFTLDELKAQGAFDAMADTAAECTTGNVSAIDQQLLSLKSAGDIPTFLHVAIQARKNLVVAGATGSGKTTFARSLIDRVPIDERLITIEDVHELILPRHRNRIHLMYGATRGRVSPTDSLAACMRLSPDRIFLAELRGPETWDYLAALNTGHPGSVTTTHANSAADTFNRLAVLIKQSPTGGNLDLETIQAFLRQTVDIVLYFERFRLKELWFEPRRLRPR | Function: Part of the Type IV secretion system.
Subcellular Location: Cell inner membrane
Sequence Length: 339
Sequence Mass (Da): 37499
Location Topology: Peripheral membrane protein
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A0A0K8MDM2 | MFVSSEGFLPEFAPGSAEIFIGLSLLMFLVIGAFRGDSYTRTLGYLCIVVALMTVFIISFADKNTGIFFNGLFIRNSFTSFCKITILLTVSCVLWMTLRSLERENMARFEYPLLVLFSALGMLIMVSANDLMSMYLGLELQSFSLYILVALKRDRLIAAEGALKYFILGALASAFILYGSSFLYGLAGSTEFSSLFSVFKDPALTSSPPLVMGILLILGGLAFKLALVPFHMWSPDVYEGSPTPVTVLIATAPKIAAFALFIKLFVHMIGDLNIIWEQAVVILSVLSIALGAFAALFQNNIKRLLSYSAISHMGYALFGLLGKTYEGIGSILVYLVLYIIMTLGCFACLLNLRKNSKTIEKLSDFSGLSRDNPVLALSFAIFLFSLAGIPPFSGFFAKLGVFSIAIKEGYYTLAVFGVIVTVISAAYYLKIIKIMYFEGSLSFDIKNHFDRYVFRETYVVMSIMAFITFFYVLKPSLLSNAAHTAAFALFN | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 491
Sequence Mass (Da): 54136
Location Topology: Multi-pass membrane protein
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A0A5C7EG95 | MNATRSPFFLRTLEPIYTAIALVIVAYHGIAVLWTFHNAMEHYTVHLGAILLLIALYTAIDRGGATKGGKRLAWFVFAGVMAACALISTVYLYAMAQELELNQPFITGFQYFIGLILLIAVFGLNWVVWGTALTVVCLAAALYFGLGHLFPSPVVELKFSPEVVMSYLAGMGGPRGVYTFIPLSADTILLLLVYGGLMTSTLVLDMFEEIGKAIGNLLRGGVAYSCIAASSLVGMVTGQTVSCIALSGSMTIPTMIRGGFTKDQAGAIEVMAANGSQIIPPVMGLGAFLMAVILGISYVEVAAAAILPAFIYMITLAIAVYALVQASPQIPFERQAVDWQKILWILPSFLPSIALVVVLLSLRYSAGLAALVGIATIIGFSLLRPKKYRPSIKGIVLGLRNGALAGAQLAIILAAIGVIVQMLVTTGLGTLFSRLMIDLSGNSLEIALLLGMAITIFIGMGLPTPAAYSLAAIVVIPSLIDVGVDPLAAHFFGFYFAVFSAFTPPVAVGCLMAVRISGGSFRQTCIECFKLGGICLLLPFFMVAFPNSLQFPNFTGETLVATGLLCISTLMFSAAVYGGFMGRLKTGERIYLLSGPIAALLYYEWRNPWIGMAPLVLLIGFWIYRRSKRRMMAKAVAALEIER | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 643
Sequence Mass (Da): 68768
Location Topology: Multi-pass membrane protein
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A0A839SR30 | MTAKQPKKPTQDRRPPALIVAGPTASGKSALALDLAEALDGTVINADALQLYRDLRVLSARPDAADESRAPHRLYGVLEARQAASAGLWRGLALEQMAEARAQGRLPILCGGSGLYIKALVEGLAPVPTVPIAVREAAAGELTRLGNAAFHAALTEKDPEMGARLRASDPQRMLRAWSVLEATGRSLAAWQALPSGDPAPYRFMIVVLMPPREVLRTRCDERFEMMLAHGALEEVGALLARNLPANLPVMKAIGVRELGAYLGGALSLSDATTQAQAATRRYAKRQATWLRTQVGLEGEGRLLLTEQYSESHTQKIFTKIRESLLTE | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 327
Sequence Mass (Da): 35297
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A0A238UMH1 | MGSRRAGGIKKVKRLRVKNPDNMKVPYDLNSYIRVLKLASTPSMDEFMQVSKIAGAGIILVGVIGFLIFAIMSLLPGVGA | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequence Mass (Da): 8620
Location Topology: Single-pass membrane protein
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A0A7J8GR04 | MGNVPSAVKHCLSYQQLLREHLWIADSVAGALDPAQEASQLSGLPEYVKIVEVGPRDGLQNEKVIVPTDIKIEFINQLSQTGFICKAVNKTTNSKVAQASFSA | Pathway: Metabolic intermediate metabolism; (S)-3-hydroxy-3-methylglutaryl-CoA degradation; acetoacetate from (S)-3-hydroxy-3-methylglutaryl-CoA: step 1/1.
EC: 4.1.3.4
Catalytic Activity: (3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA
Sequence Length: 103
Sequence Mass (Da): 11153
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A0A0R6I707 | MGTLYLLFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGIEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWF | 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: Membrane
Sequence Length: 223
Sequence Mass (Da): 23915
Location Topology: Multi-pass membrane protein
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A0A0P9UBJ2 | MFDLLNCMVMIPKMDELLPACNEGRSTFAMKMGLYATNAGAGLTSDLAQSYVPPDLWKRYRSGFFEFGGVPVDKLQKTLEEWKEMLDPAQYQVCRLKGTERPFSGKYNETKTEGVYHCICCNEPLFDSTTKFDSGCGWPSFYAPLEGSAVVEVRDVSHGMIRTEVVCAKCDAHLGHVFPDGPPPTGLRYCINSVCLELVPRQ | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
EC: 1.8.4.12
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Length: 202
Sequence Mass (Da): 22556
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A0A931Q842 | MDYSYIYNIECGGQMEIRSHIKEGIILIDKPKGLSSYDVIRRLRREIGMEKMGHSGTLDPLATGLMIVGVGIGTKKLSELIKLPKTYEAEILLGIRTTTCDMEGEVLDEKSPLELDLSEIAPLLESMRGKIVLEVPVYSAVKVKGERLYELARAGKRVNPPEKEMEILNTVFKKCFRSESYYILELVMEVTSGTYIRSIAEEIGRRLGLPATLNNLRRTKIGNYKIENALKLD | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 233
Sequence Mass (Da): 26271
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H3CE99 | QDALTVVVEDLRLCSVKPFEDIERRFCFEVLSPSKSCMLQAESEKQRQAWIQAVQASIASAYRESPDTSEEKRLDRAASPSTSSIDSASEARERGARGDAILQRIQALPGNQQCCDCGQADPRWASINLGVLLCIECSGIHRSLGVHCSKVRSTLDSWEPELLKLMCELGNAVVNRIYECSSQDGGSRKPLPSSSRQEKEAWIRAKYVEKRFLKKACSAHAGQRKPERRRQECRRHSSSNSLAKTRRRYRQEVGSASPSTLSAEAAKFRRESLFCPDELDSLFSYFDTGSGPRSLSSDSGLGGSTDGSTDFLLFGSVAEEREVSEGSSGEAELERSLYASDTEEGRDLQPGALLHRASRNQNLAAMAEALAHGADVNSADHADGGKTPLIQAVVGGSLIACEFLLQNAADVNQRDGRGRSPLHHATYLGHTGQVCLFLKRGAAQGDADQDGQDPLSVAVQQANADIVTLLRLARMNEEMKESEGQAAPCACSPTEQQLRKCFQEFI | Function: GTPase-activating protein for the ADP ribosylation factor family.
Subcellular Location: Endosome membrane
Sequence Length: 506
Domain: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes.
Sequence Mass (Da): 55234
Location Topology: Peripheral membrane protein
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H3CQL6 | CDLNYYGPLCNKFCRARDDFFGHFSCNLSGSKVCMEGWTGPECKEAVCKQGCHQSHGFCSEPGECKCHYGWKGPLCDQCVTFPGCVYGSCTEPWQCVCDVNWGGLLCNKDLNYCGNHQPCKNGGTCTNTEPNEYQCECQEGFRGRNCDIAVRQCDRSPCGHGASCQEIPGGFRCLCPPGWTGRTCQLDANECEVSVCIHAHSCHNLIGGYLCDCLPGWVGPNCDIRNSSCQDLCQNNGHCEDLVSGSRCVCPPGFSGTYCQNAPRPCEGAPCLHGGQCVETAGTSATCICPAGYSGNLCERALDLCDPNPCQQG | Function: Putative Notch ligand involved in the mediation of Notch signaling.
Subcellular Location: Membrane
Sequence Length: 314
Sequence Mass (Da): 33848
Location Topology: Single-pass type I membrane protein
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F9Z9I0 | MKKNVVVIAGGNSSEYEVSIKSGNHIFSEVDGEKYNKYLMILRGRDWMVEIGDQKFPVDKNDFSFEYQGKKVVFDFAYITIHGNPGENGMLQGYLDMMGVPYSTCNTLVEAITFDKYTCTNYLNAFGINTTHPIMLVRGKAFDKEAVLKAVGLPCFIKPNAEGSSFGVSKVKTAADFDAAVEGAFKMCREILVESFIDGIEFTCGLYKVGDKKVVMPVAEVVPKKEFFDYEAKYDAKMSDEIIPGRFSAEITGRIQDMASEVYDILRCEGIVRIDGFVRGEEIIMLEVNTTPGMTANSFVPKMVRVMGLPLRDVITGIIEEKLKRL | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 326
Sequence Mass (Da): 36402
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D8ICH4 | MLLENRPPYSFIAWLTVLVFLPYVGAIFYLFLGVNWKKSRKKLSARLPEDMIRKHFSSLLEEQMNIIDNMGGNYAKHTNLVKLAIKSGYSPITVQNQVYVFDEGKDLFDDLINNLKLAEKTIHMEYFIWRSDELGNKIKDILIKKSKEGVKVRLIFDGLGSMLRISRKYKRELKKNGIEFLYYHDPFSIFWTRYVNYRNHRKIVVIDGIVSYMGGMNLGQEYIDGGKRFASWRDTHMRIVGDACNLIQNVFVCDWHNAGGRDLDNLMDNGSSLMQELFPSSTTDKYLPMQIISSGPDSKWDSIQKIYSKMIADAKESIYIESPYFVPDDGFLHDLENAALSGINVNLMITGKPDKLVAWWVAQTYFETLLKAGVNIYLYESGFLHSKFCAIDGRIVSCGTCNMDIRSFYLHYEMNAVIYDIDTALKFERIFKDDVSRSHKITMEEYKKQSILIRLRNSACRIIAPVL | 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 inner membrane
Sequence Length: 467
Sequence Mass (Da): 54057
Location Topology: Multi-pass membrane protein
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A0A2N5G5I8 | MKKTAFFLILISLIGKFLGFGKYVALSYYFGAGIISDAFVLSITIPTVIFAFIGIGLSTSFIPVYNDVLSKNGQEYANRFTSKLITLLLFINTALVALVFFNTDTIIKLFASGFTTEAIKLTNTLIKVSIIGVYFSGTIYILSSLLQVKKIFIIPAISEIPINIFSILGIYFASKGNIVYIQLFTIIGTIIQFIILYLLTIKHGYRYKFHNNLFDENVKKLLKNSIPAVLGISVNQINIIIDRTIASHIIIGGLAILDYANRITDVIQSVIVLSIISLVYPQVSKQAVSEDFSKVNYTIYQSVVSIMSIIIPITVYYIVFSEQIINIVYARGKFDSSAIQMTANCLVMFSIGMLSVGIRELLARVFYSFHDTKTPMVYSSLSILINILLAIILTRFIGLSGLPLATSLSSIITVVFFFISLKKKLATLNIKQIVISLMKILTASIIMGFAVKFAFIIMVDYTNEFISLLGAVLIGGAVYLFVLVCININSKQKIKLFI | 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 membrane
Sequence Length: 498
Sequence Mass (Da): 55258
Location Topology: Multi-pass membrane protein
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A0A2N2L1Y4 | MKPQIDIVIEEGISPELERIEQIAETIWEEERVQGEYEISILFCGDDRMRELNRQYRGCDSVTDVLSFSSKAFDLALGVQGEKWICDIIIDTKYIQSQKGSNGYTQEIEEVLIHSFLHILGYDHMKTKDKEKMETKENYYKQLLQGVS | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 148
Sequence Mass (Da): 17260
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A0A1Y1S0G2 | MAISHAVINEISDKTSMVDLVSEYTSLRFSGGQYSGLCPFHSEKTPSFSVNEEKKLFYCFGCHKGGNLFQFVMEMESLNFSEAVHYLGQRAGVEILEEKDRQNQSRVGALFDLYAGVTRSFHYLLKETGTGKKALDYLYARGFSDDIIDTFQLGYAPQDPNWLYDFLKKKGYSSDFLAESGLFSRNDSRYPLFRNRLIIPIASTQGRVIAFGGRLLEGEGPKYLNSPETPIFRKSRTLFGLDKAVKAVRSSGRFFLCEGYMDVMALYQAGIPESLAPLGTSFTQDQANLLKRYADRGILLFDNDDAGQAAAAKSIVLCAKSGIETSIAAVAGGKDPADILEKEGGQALQKLLQYTINSLDYLVEKAMARFSAGTPEGKHRILSDLAPFIEAQDSAVKRDGYLGRLSDMLEVNVTALTADLSQKTTPSREVPREQKDPERIGSDLFLMLGAAAYPEHFPFIRQYVNADDLKDARARQLFIILEDAFRRDELDMNAIAQNVDNEEVRGLIFDKAFSGELGPDPKLVLQEALRRVRYGALARRQKDVIRALDRAERNGVSREELKSLLTEKMYLTDELQKLRVRQA | 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: 583
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): 65251
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W5T0N9 | MILLLAVKGPAISAVAKALDICTIAIRKTIDAGLKKVKEAMKISPNDTLISFDKQPLKLKTSTINTENIKSFKGNAFLNLM | Function: The Vlp and Vsp proteins are antigenically distinct proteins, only one vlp or vsp gene is transcriptionally active at any one time. Switching between these genes is a mechanism of host immune response evasion.
Subcellular Location: Cell outer membrane
Sequence Length: 81
Sequence Mass (Da): 8773
Location Topology: Lipid-anchor
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A0A381GYN6 | MATAFAVRSTSGIEVAIITGRKAKLVEDRCATLGITHLYQGQSDKLIAFGDLLDKLGVAPENVAYVGDDLIDWPVMEKVGLSVAVADAHPLLIPRADYVTHIAGGRGAVREVCDLLLLAQGKLDEAKGQSI | Pathway: Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
EC: 3.1.3.45
Catalytic Activity: 3-deoxy-alpha-D-manno-2-octulosonate-8-phosphate + H2O = 3-deoxy-alpha-D-manno-oct-2-ulosonate + phosphate
Sequence Length: 131
Sequence Mass (Da): 13868
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H3C1V7 | MPAKTYRLGVFVELRKRLQTGLIIVGKDLTTNPGDVSVTGGDSCLNIRTPSKSLSLALPAGVTLEQGSCIPTPAGQSCGDELHFRLRITVSKGPGPEASDSVTEKLRAKRTYCFYCQSCMTRLLEDREFKRVLPLPNGNWNALVDDWCCHPDPFANRKLLPRADDCLLGDSFFLLTRDGSCEQTLAEEGCIYLCLCYFQKTCRRLALVSCQCCSSVVGEAVSPETLRLYITQVVVEPAEGDGNPEPPLSRSVFLERTIAARLLELSSSLSTFHFSVQTPDGKPFLLLWMLNGDSVVASVPETCDEAERSPGPAAASSCDPSLRAARALKLLYTACSHPGPQQ | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 342
Sequence Mass (Da): 37242
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A0A1S2R9K6 | MKYYYSQYERPEIGKLYLLADEEALVHMTYNPADFEKHAAACHPAQMDEHQVFKELRIWLDGYFSGVNKEFTIPLRENGTEFQKQVWNRMKEIPYGETKSYSEIAYEINRPKAVRAIGQASKANPYPILVPCHRVVGKKGQLTGYAGSKTDIKDRLLTLENKNWATRQIN | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 170
Sequence Mass (Da): 19748
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A0A2H6HTP8 | MDLLHHPLAFAMLASYFIGALPTAVIIAKRVGNIDILEQGSGNPGASNIYRLFGPQWASATLMVDLFKGYLPVVLSQQFASSMIHPIYAQNEIAVMVWVGFAAFLGHVFSPFLRFKGGKGAATGMGATFAIAPQATTLAILVYGVALFIWKKFAAGTLAAALSFPIFLYFREGGQEPESLIWGLLVPILLVTTHRQNIARIMHGDELPMNSAKGENKEG | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl phosphate + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-phosphate + phosphate
Subcellular Location: Cell membrane
Sequence Length: 219
Sequence Mass (Da): 23640
Location Topology: Multi-pass membrane protein
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A0A7K0K215 | MLLTMLKTAAEGDLALYDKVLWPFMWIIGWIMRGIHELLGLVGVSQGVGIGWVLAIIGLTVFVRLLLVPLFVKQIKASRAMTLAQPEMTEIQKKYKGKRDQDSLMRMQEETKAVQKKYGASMSASCLPVLFQMPIFLALYRLLYNMKPVADGTLPGNDAIGGMGQVQAQNLWESTFFGQSLGLTMFGPGSDMYTKIVIGIMVAYLVLSMLFQTMFLTMKNMSYEQLHSDNPMVKSTKSMLYFMPLVYLFTGPVVQVGLLIYWVTSNTWMIAQQFFIIRSYPTRGSDAAKWREPAHEKKFEAYRAKEEARLASEIEKINLNEEGLNQKGVQVALRQARLNHIHRLEKRRMELGLDEINLGNVDAVGGNTGGQRMQPGQKGWEEYRAQFEKDLAEEKAKNAAVVEDNETVGKDGLTPAQRAAKQAERRAAERKARQNKSKKKKNNKNR | Function: Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
Subcellular Location: Membrane
Sequence Length: 446
Sequence Mass (Da): 50432
Location Topology: Multi-pass membrane protein
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F2I5X5 | MLFFSWTCDQEVYVKTFLRQKGVSRRQLAKIKYHGGTIIVNNKRVGSKYFLSLGDQVTIIYPAEGSQDQIMAVDFPLDILYEDRDYLIVNKPAGYTSIPSQFKDEYSMANFVKAYFVRKNYENQVIHVVTRLDRFTSGAMIFAKHKYAHSQIDQLMQSGGINKQYLAFTHSAIGSDQHGLIEAPIGRKEGSIIERCIRADGQHAKTEYWLEDSQAGLYRYRVQLHTGRTHQIRVHFAYLGAPLCGDDLYGGSQEAGLSGQALHCQRLAFKQPLTQEDLVIEAPLSQDFKTWLASYQKGDA | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 300
Sequence Mass (Da): 34123
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A0A969FRB8 | MPTAPTPRPRPSDADALPHRVRQRLIEHQLWHRECLVVVAVSGGPDSLGLLHALWRLRTEDDHGPALHVAHLDHRFRGSQSEEEARFVAHIAHEWNIPATVEPYDVPALAQATNQNRQAAARAVRYAFLARVALAVGADAVAVAHQADDQAETVLLHLLRGAGPAGLRGMRVAVAWEEWRGEVPGFEGAAAVSGNRPLLIRPLIDCTRAEIVQYCDEHRLAPRHDPSNESRSYTRNRIRADLLPHLAEYNRQIVAALGRTAQVCADDYAGIQAQLDAVWTADLVRPHEASLRFCKARWAQLLPALQRYVLRRAARLLTGTDELDYTHVEAGRMAVNRATGFQQPLGLGLVLRVEYETFLVGRETPAATGGDENDWSPPQMGAEAVPLVVPGITPISPSWAIESRWVAPAPGALATDGRWRWWAVLDADAFIPDVLVSGPGPDHRQDQGQDLEGPVVRRRRVGDRFRPAGGAGSRLLTKFFGDQKVPQAWRAAWPVLATSSCVVWVVGLRVDQRFQATGATRRPLWLLLRRGAEDGGDGSPGWQAGDPTS | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 549
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 60336
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H3CDQ3 | VKSKKKKLKKKLKAADHHSNQPQDQDEGMMGDGQAPPLFSAPHSQPGGRGSLGRTREHFQSERVDQLRHSDLINDYVEPRQTWTTREVAMKVHSSFRVLGLFSHGFLAGFAVWNTVVVYQLAGEQLSSLRNLLQQYQKLAGPAQSLSYLLLAISSVSAFDRRLNLARASMALRGFLRLESAALAFFCGLVLLWSAEQTGPDLHRGSLFSANQTLWPPSSEQQVLRPWMVVNLVVALLVGVAWVVVSTRPNTDYTADFLLTMEVDGLPRADVSLDVQA | Function: Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular Location: Cell projection
Sequence Length: 277
Sequence Mass (Da): 30736
Location Topology: Multi-pass membrane protein
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A0A2H1WCA1 | MKHQRRYKCVAGLLGVRNLRVAQESGIRRRVVVSLRSSQPIRVKARLSQSLTLTFRYYFRLSNILRRTLNLIAYPGDIRRSLFSSYRLLNRFCYVPRRLIAPKPNTYTFTKAVAESAVSERAPAAHYACAIFRPSIVVSSLRHPFPGWIENLNGPSGV | 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: 158
Sequence Mass (Da): 18093
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A0A2H1VFU9 | MPPPSRGIGFGIPYLITIFMGVRVVLHYISALNDPAVQSYLLYSSVLGLKVLSMAFLTARVRYAKNVFANPEDAAAKKGKVKYDDPDVERVRRAHLNDLENIPVFWVLGALYLTTAPSAWLATTLFRVY | EC: 2.5.1.18
Subcellular Location: Membrane
Sequence Length: 129
Sequence Mass (Da): 14404
Location Topology: Multi-pass membrane protein
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A0A6V7TYG3 | MGKLPKNFALLKRSENQRISRRRLQENSSFSSNVSSGEDDKKELLDDIVTDWKDSDWAPSISAVFKILFSIRLSASLWSIISDCDEVYNYWEPLHLVLFKRGFQTWEYSPVYGIRSWLYILLYAGPAKFLIKIFPESKVALFFSLRFLISFFTLFSELFLYRAICQRISNSIGRTFILFSTFSSAMFGASCAFLPSSFSMSLNACASAFYLFEYWSLSIFCTAISALIGWPFSAILGLPIVIEMLIIRKRKLALKFLFYSILFGLSICLLLFIVDTHFFGRPVLAPLNIIFYNIFSSNGPNLYGKEPISFYLKNLFLNFNIAFILAIFAIPFCLLFLIIQKINEEKYKKEDKTILFKNYFENNPLKQWERFRPLIFLSMSAIVWMLIFMLQPHKEERFLFPIYPHICLLAAICLDCLYRLLNKTKFATTFCIAILIIFVIASFSRIAALHRNYSGLLDIYKDFNNKISSDKILIQNTTKILPIRVCIGKEWHRFPSSFFLPESGKNFSEVEMRFIRSEFRALLPDIFPKGSTLSEITRQIPIHQNDENREQLERYVPLESCNFLIDLVGMEPTELEPDYSKMVGKIIIKK | EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 590
Sequence Mass (Da): 68672
Location Topology: Multi-pass membrane protein
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A0A2H1WMJ1 | MHNIRGDLVVGVRSSSDAMNSSVERDETFSPKTKKKLSKKPSFIKNAVLDLFRSKTKNSQKVSRQKSLCESDLQQRHNVPQMPMLRREKSDLSDMSIHMRNQQIRNQMLQRSNSSSCEKPVLKPILKRQSSFCDERNGSICTVRDYDAKPVMKSLRRQNSMCDIETEPKVTPLLRRQNSLIEYNRRGIYGQSPSFNMITKIDPIYQRQQQVKHEPFHPTQPLPPEPVYQSKDHLVYDPIPKPRRTYTSVYDTSTETPYASRSEMSNQSFENPYGNKQTIGMPLMDPPYATRAECMKESPYATRAECARESPYATRADCVRESPYATRAECVRESPYATRAECVRESPYATRNECMRESPYATRADCVRESPYASREECMRESPYTNKQDISRQSDSFYSESPYSSKEQMLRTRLTPDGSYATKEEMLRQRFSESPYSTKEDMLRQRMDLSGKEPLYGKRTYDPPPSTSWNENHYGVRPDRRLQTPVNFPGRVSPMSKCMSEPPYATRTEMMARLGQTESPYATRAEVKSSCSDTQYGTRHDMMDMRPDVRPASAECTYVSKQEILSQKAALLAKKESSYGIRLEEKLEIIKQRNQAKKEMIYQTRKEANESDSVKIREPLYVSKRDLKESVIYESHQETKEVAQPEEQEGSSSSACSAASATSTSARSSPYELGDANHLSRREPVYQTKSEAESGIESETFQEIDFSKLRLTESKTDAEKQKSKNLETSVLKGEPMYAPRLHGKADHISNALKVTTSPVPYESTTSMETHYASECSMNFENKPQSTPYTSQDLLERNNKPSRSVTFCEQILEKSPETSGENSQSMSSSQNETTVIQQNTTVVPSTSDANDSSNKTQEVEPDGPHTTWGIFDSEGGVLEDRQWGVSLIIPPKAIAPGIKQKIYFTVSDPRLSQRVGGPPIDMDNGEAMLSPLVMCGPQGLVFLRPVTLRLPHCANAVPSLGLTIKATDTEAHLSTDWDQIHLPATTTLNTVAVKVDHF | Function: Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding.
Subcellular Location: Cell membrane
Sequence Length: 997
Sequence Mass (Da): 113000
Location Topology: Single-pass type I membrane protein
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A0A7J8E3Y2 | MSVLAQAGGRWRSAAARAVIPCLWRGKYFCSGKEPVENNPVTPMLRHLLYKIKSTGPITVAEYMKEVLTNPAKGYYVYRDMLGEQGDFITSPEISQIFGEVISI | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subcellular Location: Mitochondrion
Sequence Length: 104
Sequence Mass (Da): 11614
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A0A7S2S3D3 | ASGEVTKLIARMGIDRIGFTLLGSLGCVAAYGCFMLHLERNKQLFYLDKVAKRTTVEEAVRDDDPEKLVLIKGVVESQGETLVAPKSQVGCVYYNLTKKRITEDMVKTKERKSKKSSRKGETKTSETTYPSFITSESVVEEHSDQANWAVVSLEGHVESVLPVEGNVKLASQPFVELEESFNQFEEPKGGGNKRTVGYRYTEKILRSGTPVFVIGCIHQTTNGPVLCEPAQGPFIISTYTPSELTSKLKAQKRGWLFVSIILASVG | 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: Membrane
Sequence Length: 266
Sequence Mass (Da): 29357
Location Topology: Multi-pass membrane protein
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A0A6V7VNX5 | MISNARIADTLASDGHNVTLLEVGFREVALNASKVANKILVPGPFIDSKEYDPSLMAKMAFKEVDLTMDFIVGSIWLTTFNNACEKFLLVSEKLFDKLRNEKFDIIISEQLNFCGAGVGHLLGIPTNILVSSCPIQEHVASILGLSNPASYVPSLYYSNLPDKMSIYERTTNLFRQYAGYVYLIYGVDPLTKIFKKHYGATFPDLRTIVAESPFVFVNVDEFLDFPRPIFSNIIYIGGLGMEEGKNTKINKIEVFIWGPSKTSILFIVSPYPFR | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 274
Sequence Mass (Da): 30722
Location Topology: Single-pass membrane protein
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A0A6V7XVM7 | MDTLKIGCLLQGNFLAKLPCYPHEQRNKPNIQHAPIRSVPLNKEEIKLAVKNILRYVPSRFHKELAAPPIEQIKCSNRQAAAIVLMILNNLDPDIAQFPQELVTYGGNGQVFSNWIQFRLTLRYLGEMDENQTLIMNSGHPQGLFPSHADAPRMVISNGMMIPNYSTKELYDKYFALGVTMYGQMTAGSFCYIGPQGIVHGTTITLMNAIQKYLGRGTSPSGKVFVTSGLGGMSGAQAKAAVIAGCIGVIAEINEKAIKKRHSQGWLDIYSSDLEEIICWIKQNKAEKKSISIGYLGNVVDLWERLVAEPEGTILVELGSDQTSCHNPFVEDIIRLA | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
EC: 4.2.1.49
Catalytic Activity: 4-imidazolone-5-propanoate = H2O + trans-urocanate
Sequence Length: 337
Sequence Mass (Da): 37265
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A0A223PK73 | FMGYVLPWGQMSFWGATEITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIIAALVMIHLLFLHETGSNNPSGIPSDSDKIPFHPYYTIKDLLGF | 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: 105
Sequence Mass (Da): 11873
Location Topology: Multi-pass membrane protein
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A0A6V7UGY8 | MSDKSGIRLNDIVQMATEKENIEPEYRMRTIESLARHIEAALRYQHTATSRTQYTLHRVFKCFNLRYYESYVTGMYLATKVFYVGNVLTNLLLVNKFLETNNYSIYGLGVLYDLLLLGKSWTQSGNFPRVTLCDFEVRVLGNIQRHSVQCVLVINIFNEKIFILLWLWFCILFFITLFDGLYWFSVSLFHRDRFRFVLRHLELTSDPDRPELFRKEKRKQVEHFLKAYLKVDGVLVLRMIALHAGVMYCTEITDALWKRYLSQHPENLIDEDSVLINFARTQSIRRRIGCSASSTSLAPNHNGSSGGSAGRRVIQRNAHARLSRFLSYRQVPAAVRNTRGAVVYRPNPRSTPGNTTTSSGSAVERGRIINRCNSPLRIEQESSVDGAQQQAVAVLSQSRVYETIPVSNTQVIVTPSSRPSSRQDEALSKLNRSNLTKQVSIGSCSQTDRPLRHSNIASDDLDDSLCSSESLSHNHSSSSKLTKAIGVVKSPLKKLRSAMLPSSSATKSSAKNSTASDLLPSSDRLSLTRSATPSVHPHDNYQDHSTSTTSSNHNRKISFSLLDTHVEGLETSTGNKSAREVAALEINRLKKKS | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 593
Sequence Mass (Da): 66815
Location Topology: Multi-pass membrane protein
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Q4SRM3 | SKDDAPNDTFMIPRKEINMVTDMGKWKQSQAYADYMGFVLSLNKVVKGKKLTCEYKVSETVQKLLQLLGTLEQWIIETPPVDQPSRFDHPTLEPRHFIDAKVVNEHHQDYMFLDCIKFINEMKTGPFAEHSNQLWNISAVHSWSKVNQGLIKMYRAECLEKFPVIQHFKFGSLLSIQPVK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 180
Sequence Mass (Da): 20929
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A0A1C6C2I5 | MKNEDNTNNKNKKKKGRKKRRPGRIIRNIILGIVIAFAALFLLGNLFFHYKYGETIFSCAKFGKEAVAESTADTFRPNQASTVYSSDGKEIAKLYEDTESTYLDFDNIPKNVINAFVAVEDRTFWKNSGIDVKGIVRVSLNFLKTKGDVAQGASTITQQLSRDIFLTNEKSLVRKVKEIFIAMNLNKKYSKEEIMEYYCNNVCFANGIFGIEDASQTYFNKPASQLTLSEAAYLCAIPNRPEYYNPFKDSSNAITRRDKILEDMYECGYITQQEMNDAVSEEITIAKQEDNDEFYNYETSFAIKCATEYLMGYLYDFNFQYQFDTDSEYAEYHQKYNEVYQQAKHRLYTGGYEIQTSLDLEAQQGLQEVVNNQLSFDQRLKKGSETYNLQSGMTVIDNNTGKVVASVGGREQEGITQALSYNHSFQGSNQPGSSIKPLVVYTPALMKGYTPTSAIPDINVDVAKKSTQKVSSMTGTKYSLREAVVRSKNGCAYWLLNDITPKYGLSFLEEMGFSNLHPNDNNLSAALGGFSYGTSPWEMANAYYTLYNSGTYTKADCLTSIKDNTGKEIYEAPASKEVYSSTASDEIIDIMRGVFKSPGTASSLNWSSSTQTEAAGKTGTTNDNRDGWFCGFTPYYTIAVWVGNDDNSPYPGLSGSTYPARIWKEAMLYMIKDKPAASFDLSVSGSSNTVVPDEEETETDNTDSTDNTNTDTQDNTQQNPADTPQTTPDTPDDNQDDNPDDIQGDIKPDPDDGGSTDTPSTDPDTPPDGGDGGSDSEGDQGQDSQQKPDGSGQGSSSSGSQTNQNSKN | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits).
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.
EC: 2.4.1.129
Subcellular Location: Cell membrane
Sequence Length: 808
Sequence Mass (Da): 89537
Location Topology: Single-pass type II membrane protein
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A0A921ML48 | MQRITVIGSVNRDHLYSVPHIVRPGETIASESYRTGWGGKGLNQAIALAKAGAQVSLAAKIGHEDYPSLSALCSAYSLDISQVHACALPTGHAIIQLDTAGQNCIIVHAGANGSFTEQDIQSFLAGCRAGDIFLLQNEINSSAQIISEIKKKGGRVALNPSPFTPDILRWPLECLDYLILNETEAASMTSADSSEKALDHLCSAYPALNVFLTLGSEGSCFACGNTRHFHPTHKVNAVDTTGAGDTYTGFLLAELARGSAVEDAMSIATEAACLCVTRPGAVDSIPSRAELPSLN | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 295
Sequence Mass (Da): 31085
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A0A839SPG3 | MAPGINIIAILLVGAAIGSFISALVERLPDCKGLVAGRSRCPDCGETLKVRDLIPLVSYLLLGGACRACGKAIAWVYPVAELGALFLALTVIVVFRDPATAPGTLWLAAGLGWCLLALILADVRRFLLPDMLVLPLMAAGIASVFLEPQAQWQSIGMARIFGAALGFVLMEAVRRLYFWIRGRDGLGFGDVKLMAAGGAWLGWPLLPHSLALAGILGLVTVFILRLTGRVLGPSDALPFGAFLAPAIWILWILGKTAPDFIGILVGF | Function: Plays an essential role in type IV pili and type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine.
Catalytic Activity: Typically cleaves a -Gly-|-Phe- bond to release an N-terminal, basic peptide of 5-8 residues from type IV prepilin, and then N-methylates the new N-terminal amino group, the methyl donor being S-adenosyl-L-methionine.
EC: 2.1.1.-
Subcellular Location: Cell inner membrane
Sequence Length: 267
Sequence Mass (Da): 28270
Location Topology: Multi-pass membrane protein
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A0A2H0B6M7 | MTIFQAFILGIIQGLTEFLPVSSSGHLALVQHFMGLPQVPIAFDVLLHMATLLAVVYILSRPINDLVVKTYKAIVSRKINQIPKLLWLLIIGTIPAAILGLLFNDYMDTIFQSVRYFSIGFLITSILLNIASHIRSQEKSLKQMSLMESFKIGVFQAIAIFPSISRSGATISGALLAGFGVKDAFTFSFLLSIPAILGASILHIKQIFYINSSQIPAYSVGFIAAAISGYIALLVFRQTLINKKLSIFAYYCMFLSLLIFFFVK | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 29186
Location Topology: Multi-pass membrane protein
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A0A7J8ER24 | MVNPTVFFNFAVNGEPLGCVSFEQFADEVPKTAENFCALSTGKKGFGYKDSCFHKSILGIMWPGGDITRHHGTGSKSVCGEKFDDENCILKQAHGSWPLVHGKYWTQHRRLPVFRLHCQA | 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: 120
Sequence Mass (Da): 13432
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A0A1C5WB81 | MTKKEFKQLTDQKILILDGATGSNLQKRGMPAGICPELWITEHPETLQQLQSEYIKAGSDILYAPTFSGNRIKMEEYGLGDQLEEINTKLVQICKENAAGHVLTAADITMTGAQLEPLGDLKFEELIQVYKEQLSILAAAGVDLIAIETMMSLQETRAAVIAAREVCPELPVMAALSFTEAGKTLYGASAESAVAVLQELGVDAVGLNCSAGPDKMKAVLKKMAEVSKIPLIAKPNAGLPSLDENGNTVYDMNKEDFCTYMKELIGEGAQLIGGCCGTNPEYIAELKALTKSFERPVKTGKSKLYLASEREVFAFTEGQQLKLGEGIDVTKDEELMEELRRDEYETATDLAFDLLDDEADALRFFADADGIDEAEALLSLIQEVTSVVSLPVVIASRHAETVETVLRNYSGIAAVECLAESEDEKTQIFSAVKRYGAKLVTIDKKIIYC | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1.
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
EC: 2.1.1.13
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine
Sequence Length: 449
Sequence Mass (Da): 48905
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A0A1C5NHF1 | MEAGMITTVLLVACATICIGVGIFYFFINNTKNKGRICILLLGIGGGIWALGSALYGNCTDDRLAQDFFCMTIVGFNLYVIAIVIYVACLTGVKIKGYGLMVGLGILTSLVDGVSFGSMRIRHFYRVNGRTCFTTEFHGSVFYHWMYIMLCFLCCIYIVLYWSKKIMRKSQRKYVAYIILGNTIMLLSAIPDTVLPFYGIKSYPSSVYGVTVSFLMTVFFSIRYDTFGISKLTVSDYLFNQIDYGVMVYDYQRTHILHNTNAEVLFGADVEQPFEELVACGGKKEEFAEQLYQGKLEHCKVKCLQGNQILSVTSSMVCDEYGEMQNTIVTLVDITYEEELLERLRVSDRAKTDFLTNMSHEIRTPINGIMGMNSILLRQIDTLPREKIAEYAGNMQRASRTLLAIVNDILDISKIESGKMELLCEGYELASLINDCYTIVASNCKKKNLDLYMEIDENLPSILYGDDVRIRQVVNNFLSNAVKYTKRGHVILKISYSRIDEENINLRIDVKDSGIGIQKKDMENLFQNFTRLEEHKNRNIEGTGLGLSLTKRLVDMMHGEVLVESRYGEGSTFTAIIPQKVICEDGIGDMKQIFENYELSVGAMMPVPQFAGVHILVVDDMEMNRIVAKEMLLQTGAIVDVAGSGEEGLTLMKEQHYDLIFMDQMMPDMDGIATFEEMKRMNHQNKTTPVIAMTANAVKGAKEMYLQHGFAYYISKPIFEEKMWKILERFLVDKQTEAVEKKNSDGGADENKKSLQERFPYLDTKQGMSVCMGDEAFYFKILKVYLKDEMVDTLQQDYEAGDWAQYQIHVHGLKNMSANIGAMELSGQFKGLEYAIKNHDIPDTDYIRSHHDKVMEAYQELLWRLERDI | Function: May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 869
Sequence Mass (Da): 98882
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Q4TBT6 | MVHYSSEVLLREVCDSESGHNLPTVLVEITATVLDQEDDDDGHLLALQIIRDLVDKGGDVFLDQLARLGVINKVSTLAGPASDDENEDESKPEKREPGRRIRQLRFLQTAFGRLLADPRNAHPLFCAALPLAAESRSEFLEKLQRARSQVKPVTSSQPILSTVAPTKLTVGNWSLTCLKEGEIAIHNSDGQQATILKEDLPGFVFESNRGTKHSFTAETSLGSEFVTGWTGKRGRKLKSKLEKTKQKVKSMARELYDDHFKAVESMPRGVVVTLRNISTQLESAWELHTNRQCVEGENTWRDLMKTALENLIVVLKDENTISPYEMCSSGLVQALFTVLNNVSVPRLLLHPQGNAYLCTCTTLPALCTTCK | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 371
Sequence Mass (Da): 41182
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L2GX65 | MLKYINLYNLAGTLVGAFALSSIALNYFSKNMHFIFRIALCQSFYILEVLNILTNASKSRLFPTCMQLSSRLFIIWCICYRYGFADAVVHIMLLCWFVSDTVRYLFYFSRNGTVKFLRYNLFIVLYPLGTLCEIVLVSRVERACTGVLKYFLRVVMLCYIPGFSFLYVHMIRRRRWTDKNRSAAQRKKDK | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain (2E)-enoyl-CoA + H2O
EC: 4.2.1.134
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 190
Sequence Mass (Da): 22415
Location Topology: Multi-pass membrane protein
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