ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A3XPX4 | MYTTQQSMRWFGPSDAIRLDDLKAAGVSGVVTALHEIPVGEVWSIKAIQERQEYIDSFGLRWNVVESLPVSEAIKQRRGDFERHIVNYKTSLENLAQCGIYTVTYNFMPVLDWVRTDHRFENSDGTLALAYDHIAFVFFDVHLLQRPGAKLSYTEDELQAARAYGERLSDEEQNELFKNALLGLPGSKGHFTAKQILELLADYAHIDEHQLRKNLICFLEEIIPVAKSCNVQMAIHPDDPPFSVLGLPRVVRNYDDLKQIFEAVPDQANGLCYCTGSLGADPETDLIQVLETFKERIHFLHLRNIKRYDAKLFQESAHLD... | Pathway: Carbohydrate metabolism; pentose and glucuronate interconversion.
Function: Catalyzes the dehydration of D-mannonate.
EC: 4.2.1.8
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Length: 393
Sequence Mass (Da): 44763
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K0KTB1 | MPIKRHQWGSHTRQYIEELKINPQSKDAVITIHGGGWVSHQEAAKDYFEMSNTVDFDANFFGVDYRLSASSFEGYVLPDPIDSYVKAPYHLLDILHGIEFIFDNYEIERVHLIGHSVGGCTALQIQDFASLIPHGLQQLVKHGVITESEEKKQLKFVEETLKKWSKVELLNVIYLSGVYDFPLALSKVASLGPPKGILDNYIYINDAFVSEEHYTQGCTITSTILNPPLDTLKAKGKHVIIHSFEDEFVESFQPLGLANFFYKLNVPVEVYIDDFDLHHKILLNGKAFKIIERILNDH | 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: 298
Sequence Mass (Da): 33963
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A0A078KI19 | MFTYKNFIELSKAGYNRIPIYRDIFADIDTPLSTYMKIDKKSWTFLLESVEGGDKKGRYSTIGLPCNERIEIRGKIVYFYKKNLLFKIIKVNNPLLWIEEFKLYYKSPIIDNNLSFYGGLVGYFGYDTIFYIEPNILNINKPDPINVPDILLLVVNNLLVFDNISGRITLLTHANPADNKAFENAIKYLNELEFQLRNNFIKKHNSINKNIYNINKNVFYSFTENGYKNAVNRIKDYILAGDIMQCVLSQRISMNFNASGIDLYRALRSINPSPYMFYFNMDDHEIVGASPEIMIRLEGKNITLRPIAGTIHRGKTIEED... | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of... |
A0A952III2 | MSSSKQKAQSGGSAGGQVNIQTVTVVQNVSTDPDGQCLQQVKNILQASHNITIHVVPVDNKTDHPEVPKEAANPDLVIVLGGDGTFLRASQCFVEQKIPLVGINTGTLGFLTRIESDKIESYLSRLLAGEYRIEERMMLAVSLETQPQTLLVAANDVVVKNRNPSQMCSLNLFINDVLVSTYDADGIIIATPTGTTAYTLSAGGPVISPEVEAISITPICPHSLSAKPIVIPAGKTLRVESAVKNRPVVYSVDGQESGTLEPGQNLTLFRAPYPLKMIDFGQEGEDFYLLLKQKLHWAMNPRWKTQ | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A952ILD7 | MTPLRSLQDIATQVQGTVVGDGSIEVTQLVHPMMATSPQDLPFAIEPQALEILPHTPVKAAIVSKEMTVPDGVLAGYIVVERPRVALAQLLNIFDKPVHAYDGVHPSAIVESSAQVDPSAKIGAFVYVGEGAKIGKGAVLMSHVTVGAEAVLGEDVLLHSGARVGERVILGNRVILQHNVSIGADGFSYVTPEKGSIESARESGGKIEAQNSEIIRINSIGTVILEDDVEVGACSTIDRANLDATRIKKGTKIDNLVMIGHNNTLGENCLVAGQAGISGSCKVGDRVVMAGQVGLKDHISIGDDVIIMAKSGVMNDIDPK... | Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.... |
A0A952ILS4 | MLNNPRVIFLFILILVGAAIGILWKMDFNLGLDLKGGTRLTLEAVPTADVKEVTPQVMESLRYIVDRRVNGMGIGEAIVQQAGDKRIIVEIPGVKDPDAAKKILGKVGNLEFRMLDENGLWVSSGVSGKDLTKAEIGPTQTGDYVIHFELNAAGGKRFGDLTQKLVQEPNEARRHLGIFFDGEMQSAPIVRSAIQNGAGIIEGYDTREEAKEIVDVLNAGALPVDVEFVEENTVGPLLGQAAIQQSLFAGALGLVLVIVFMLLYYRTQGFVADLALVVYTLLTLALYNLIGVTFTLAGIAGFILSIGMAVDANILIFERT... | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Location: Cell membrane
Sequence Length: 415
Sequence Mass (Da): 44511
Location... |
B9SV03 | MGSEERATETSVLALPLPFQGHMNPMLQFSKRIASKGIRVTLVSFTNKVLIGENGPINVEVFPAYSSEEDDGYLNNLQATMRQTLPQIVAKHSESGFPVSCVIYDSLMPWVLDIARQLGLPGASLFTQSSAVNHIYYKLHEGKLNVPTEQVLVSVEGMPPLEIYDLPSFFYELEKYPTCLTFMANQFLNIEEADWVFFNTFNSLEDEVLRGMTSQWPVKSIGPTIPSMYLDKRVEDNREYGINLFKPNVENCMKWLDLREASSVVYVSFGSITDLGEKQMQELANGLKRSGHYFLWVVKEPEEKKLPSNFVEETLEKGLI... | Pathway: Pigment biosynthesis; anthocyanin biosynthesis.
EC: 2.4.1.-
Catalytic Activity: an anthocyanidin + H(+) + UDP-alpha-D-glucose = an anthocyanidin 3-O-beta-D-glucoside + UDP
Sequence Length: 453
Sequence Mass (Da): 51333
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A0A1L0FF15 | MDEYVDSVIKPTNNSNNKRLKNICIKKPIIIGNNSVRLTEEEKLNNPKIPREHTHRWQIFIMSPTPKGDLDLSFIKKITFKLHDSYQPAVRTIEYQSFIKQSTQNVPGFLVEETGWGEFEVGIKIYFQDGSQEKFLQLYHPLRLHSYYLILNNETGEYDQKPCVQKEGENLTVDNEKNGMVKSFYYDEIVFNEPYADFFTKWLMESNSIMFTNTSDALKSSENNVLYQHPFSEEMELDELERLENGLSKAEEMLNDLRRQYMEKQKALAN | Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for an H2A variant leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes p... |
B9TBB4 | RRRRSMGSTLLSDLGTEVLVPVCAIVGIIFSLVQWYLVSRVKLTSERHAPGLSPSSGGGNKNGYNDYLIEEEEGLNDQSVVAKCAEIQSAISEGIIITTIILTT | EC: 7.1.3.1
Subcellular Location: Membrane
Sequence Length: 104
Sequence Mass (Da): 11208
Location Topology: Multi-pass membrane protein
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B9SHU0 | MSSNSKFDLTAVPGIQNTSPPSPPAYQKADCLMTLWLMDMANFSFSKFSDSQYDSSQSTSTPDSKLLNRTLAPSFDKVSDFKYESSQPISTPDDKLLKRTLAPTFDGGSVSRNESSQPTTVRNENVLNGNLAPKFSERSGSRNDSSQASSNANDILLDGLICPGFDERSCLSRRQSILYRRTSPHKPSPFLLSKLRNYENLHKRCGPYTKSYNKTLKTLKSGHINSATECKYIVWRPDNGLGNRIVSMASSFLYALLTNRVLLVDHGADMTDLFCEPFPNSSWLLPMDFPLRNQFRNSELRYAHSFGGMLEKDGTSVKST... | Function: May be involved in cell wall biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 622
Sequence Mass (Da): 70702
Location Topology: Single-pass type II membrane protein
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B9RM43 | MAFNPDNSDGHLNPIRLKVILEASRVKDQEAVEVPRGSLNSLNMSISENQEEAEPFYILDIGVVISLVEKWSHHLPHVKPFYAVKRNNESALLIVLATLGANFDCASQAEIEAILGLGISPDRILYANPCKSVSHIKYAARVGVYLTTFDSKEEVDKIRKWHPQCSLLLRAEIQNDKSSWIHLAANMAHIFLRKFLEYTHILK | Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
EC: 4.1.1.17
Catalytic Activity: H(+) + L-ornithine = CO2 + putrescine
Sequence Length: 203
Sequence Mass (Da): 22929
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A0A2G8XT74 | MLVGKRGADATASLGVGEPQLKRRQVETGNCVVDCGAYRLLASCYGDKGMRKQMEDEHVIVPSLLPFQPALSPAYDFALFAVFDGHGGRQSAAFVKEAFPSELAAQLLLLQQEKENGSSSTVSAEKADATASAASAGGLTDREMKQVIYGACRKVDARIATEIPSCRDGCTAVVALFHGQQVYVACLGDSAAYLARRKDRTLHCIPLTEVHRHWVIEEKERIARMGGTIENGRVNGSLEVTRSFGDIS | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 248
Sequence Mass (Da): 26705
Location Topology: Peripheral membrane protein
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A0A2Z2P7X5 | MSMSSNSTSKTDPVSDVQSLRKIIHVDMDAFYASVEQRDDISLRGLPVIVGGQPNGRGVVAACSYEARKFGIHSAMPSAEAGRRCPHAMFVKPRFEVYKQVSQQIHTVFREFTDQIEPLSLDEAYLDVTSNTLFAGSAYRLAREIKTLIHERTGLVASAGVSYNKFLAKIASDYKKPDGLFCILPAEGETFVASLEIGRFHGVGKVTEARMHDLGILTGGDLRQWSEAELAHEFGKSSRYYYQVARGIDDRPVRVSRIRKSMGSERTFGDNLHERTEMLDILVTLLDDLIDQLAAKSLSSKTVTVKVRFADFSTFTRAHT... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A0B2V9N2 | MTLLQRSSLLFAVIRHASSKQIQLIGCGNGVGGRQLGCEYAAQIMRRSPLLKRCNIEHRWVTMIHEVPTGRQRAAIPGISKLAEQLAFAIQQRVLLNQHPVVIGGDHSCAIGTWSGLAGTLRHSGNIGLIWFDAHLDAHTPETSETGNVHGMPVAHLLGYGDKLLTSIFDDQPKIRPSNLVYIASRSYESAEKKLIDKIGAKIFSQHDVDELGCETVLNEAIKIAKKDTLGFGISIDMDGFREEDAPAVGTPEAGGVIADRFLEAIAKADLDKLLVTEFVEFLPRLDKAQRTEKLIIRLIEAIYGNKFSHHR | Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Length: 312
Sequence Mass (Da): 34342
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A0A2G9PS18 | MLTDALKKIVLNATMIKGLTSDALRDLARYEETTTEFGSARYVTKIRSRSAKFTEIAIDGTLTDDQKRVVEEVITFLKGKELICVERTMCDNPDMKIHCKTYYTKDYARIGYMWHNSLFDLSEKHVAEQTVLQVPEWKERKIIVDAKNKVTFILGSDYFGECKKAHLRMAMYVMKQRGGLGLHAGSKLVRVKGDDGKIIEKGVILFGLSGTGKTTLTVHDFGLEDPEGVVIRQDDVVLMDDNGFCYGTEDGFFIKTEGLDEDQTVLYHAATMPHAILENVHVGENGKVDFCDYEFTTNGRGIIRRRDIEQADDSVDLRKA... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 4.1.1.49
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Length: 498
Sequence Mass (Da): 56161
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A0A0H5BX74 | MHIVSFITFFTLALILCALLLIISYFLGERPTNLNTSSSKNIPFESGVNPIKQEKLQFFAKFYLLAMSFVIFDIESIYIYTWATIIREANWIGFIEAIIFIVNLLVSLLYLIKKDVLNWKSLSNKKQT | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 128
Sequence Mass (Da): 14837
Location Topology... |
A0A8R1E6V2 | MRNNMIKQGSGIFFDWYIALKAAEERKTIISIETSTEQCNPLWSVSEDEIVYGIEASLKELEALHAERSTLLWNSTSRENELVKHYKCGTLEDKFFNKKEIPTEMVHNIEEFRAANIREKLNYDIFTQRNYRMARRMDEVFRQKSNHIVFVAIGAGHFFGDNSVLRHLQRKGYIVQQIGENDKMYLVFFFQLNIGNINLSFQLNHKCTSSSKAKIQTCMEKRARVE | Cofactor: Divalent metal cations. Mn(2+) or Co(2+).
Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway.
EC: 3.4.-.-
Subcellular Location: Cell membrane
Sequence Length: 226
Sequence Mass (Da): 26516
Location Topology: Single-pass type I membrane protein
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A0A0B2V6V5 | MEWTVAQLGGAYVIAIFSIQYIMRERKAFDLQRALYVWNAMLAIFSIAGFIRLTPTFIGQFRERGFISTFTEVGPCFTDNVAGYWTFLWVVSKIPELIDTIFIVLRKRPLMLMHWYHHACTGYFSFVAYASGNAFMIWIVWLNFFIHSFMYSYYMLRSMRIRVPPQVAQIITGAQIVQFLITQAIMAYLAILCMTTNANYDVTLKAFLLGAFMEITYTMLWVQFYYVSYIDNGGKKYKDHQKLIKGNKAQ | Pathway: Lipid metabolism; fatty acid biosynthesis.
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: 250
Sequence Mass (Da): 29214
Location Topology: Multi-pass membrane protein
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A0A1I8NMR9 | MEDFESVTLANQRKALHREQTRTRHILLGIYNYGRFLGIINAYWDRQQARVIPLSKYYRAVTTIFKLAIVIGYWDVIPELVHNFIAKPNSFEQLFSLVQVISVVVFSVGLVILKIRDDPKLNKMINDFAQLNKEVAALDSIPFTLTRRFVALFSLKTVITLLGYVNEMPNILDVEGLNIYSPVNIAIGIYLWLGSMYVLDGCYMGFLLLSMMYYNIGKHLRRMLANMKHIEISSQVGSSLTNYNRMKLLCDYSDKLDHISSLYCRLYRLTKDFVCLFQWNILYYLYYNFMVIFLLLNHCIWHYIQDGSIHVAEILYVFVK... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 417
Sequence Mass (Da): 48473
Location Topology: Multi-pass membrane protein
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A0A1X2HDH6 | MSDRKRSGSTSSSRPPKKKAAAPDNQKRLDLFFPPKSVDSKPNNDNRHELDDVTNQSPQQISLGSDDDLERDTDSPKVMLSMDNNDQGLEELAVYKSSMYTDQFHEMLSVVLNDEHFLFTASEIKLLDEIQHLEDESLHLFVRLWMRKYGWIRLDKLDYRNHVRDAYQSAAVLCDAGLVSDTINDPSEALALLPLDELKALADECGVQPGKGTKNRSDYSRALAMYGNRKKKEVWLERIRKCMGAVVKIKPHVSELLRRVHLVYFRLTEDTQQSNPMTSAIMSRINKWTFPDYIPCRTSCVWLSRDELLAYEEALAIRRS... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A7S1SNW9 | WADDNSADIPPVPSFGGDLPEGADAAQPATSVAQEPLPGDGDDPDGPPPGFESVKPGTHNGGGEADDTDAPDSLLNTLQEPEPETEIKTVSSDKSMYSSAKTFEELGLSKELLDGLYNEMKFERPSRIQATTLPMILSPPFKHIIAQAHNGSGKTTCFTLSMLSRIDPGLREVQAICLCPTRELVVQNLMVLEKMGKYTGITATSTATTETGERRSTRAKIKDQVIIGTHGTLKNWVSKRIL | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 242
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): 25977
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A0A7S1SRB3 | HPPYPHYWDRLLPVAYMMYASPLGTQAILFSKSVSTLLRATLAGDSQLGYWFTYVILVAFIFTIIFWATRLDKSLKLFPAIVIVPTMQIGWTIFSIISGGIYFQEFQGYSPLQMGMFVLGVATIMVSVFFLTPSTADKYTEMEDMSAREAPLDVTDNTLAEPLSPGYRTSSDEELPQRVVNVKDLVA | Function: Acts as a Mg(2+) transporter. Can also transport other divalent cations such as Fe(2+), Sr(2+), Ba(2+), Mn(2+) and Co(2+) but to a much less extent than Mg(2+).
Subcellular Location: Cell membrane
Sequence Length: 187
Sequence Mass (Da): 20999
Location Topology: Multi-pass membrane protein
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B9RSR3 | MYKTPSSGCISLTLFMAPILKTLFFLLLSIISTRSHQHPLDPLTPKELTLIQSILQYAYPNSSHTLAFHYVGLQEPPKPLIISWVQNPSTRDPPRQSFVIARIDQSTHEIIVDLSLNKIISDQVYDGYGYPILTLEELNAAHSLPLVYAPFLESVNRRGLKIKEVVCGSLSIGWYGEVKMKKRTVKVTCYYLDGTVNLYMRPVEGVTMTVDLEDMKIIGFNDRLTVPMPKADGTDYRETKQKHPSVQSLKGITVVQPDGPSFTIDGHRVRWANWNFHVSFDQRAGPIISLASIYDVKRQKFRQVLYKGFVSELFVPYMDL... | PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.
Cofactor: Contains 1 topaquinone per subunit.
EC: 1.4.3.-
Sequence Length: 689
Sequence Mass (Da): 78193
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M3AY83 | MHLPQQSPKPTRLQKLSSAIAMTSNSAAALWTGQKVIGTTTEATLLKAEAQVEQTYSSEEHYDIRRTLAATGEGQVSFLQSQSTGVIVVRKVVRPVELHEHNRCLWDRGRYKYPNDAVIANLMKPHPNIVRLFSCSRDEDRSAEPGQYEIFMEHCNGGDLYVQAHHFIQKNKEIPDSFVLHATIQLLEAMAFIHHGLRYCGHGKYTVDPGFKSIVHGDLKPENVFLKWSKPRKVDDLPTLVIGDFGGAKPAGKYYHCVSAGTEMFHAPEDVAIVGSPMVECTEETFPLYLKLAEERATPSDMYAIGLILECLVLGQDDPP... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Subcellular Location: Membrane
Sequence Length: 414
Sequence Mass (Da): 46472
Location Topology: Peripheral membrane protein
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A0A3A0BCN2 | MIKTSDIETFILAGGKSSRMGDDKGMLRVNGKHLIEFTIEPLKKSGLNPKIIANNESYKIFGLEVFPDEVKGKGPIGGLLTSMVNCKRDHLLLISCDMPFISEDSVAYLLAESEDGKICVSSDGEKINPLFAIYPVTILGFVNSRINENKLKMTELILSSDHRVINMSAMLKNNPYLFLNINTRSDFENLRHSLNK | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A3N5KX57 | MNFYYASSINGFKPHDINNINKKIITHLKQYGLVLNEDLLEEEGNKERTPEHMNAEVHNQYMEWLKKCDIVIAEVSIPSLGVGYEIGRAMEDGKPVLCLFHESDEKLTAMIKGCDALHCTEYKSSEEALQIIDNFIKRNDEDTKKVKSVKEINSESVQNLITGK | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.
EC: 3.2.2.-
Catalytic Activity: a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a purine nucleobase
Sequence Length: 16... |
A0A0A0C1V9 | MTATGGTGTTTTTDPPEAAPGPPGPSRWAQVRDLAERADGWLLALAVTTLAAVLRLVHLGRPQTLVFDETYYVKDAWTLLNLGYEAQWPEDPDPAFHAGQVDTYLDDPAYVVHPPAGKWVIALGLRLAGADEPAGWRLGTALAGIVTVLLVARIGRRLMSSTLLGGLAALLIAVDGAALVHSRVAILDGVLTLFVLAGFGALLLDRDHARRRLAPGTAPPRAPALWGPWSWWRPWRLAGGLLLGLAVGTKWSGLWFLAVFGLLTVGWDASTRYRAGIRRWWQAALLRDGPLAFVTVVGAALIGYLASWTGWLRTEGGFGR... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A2D2AMF3 | MGEHEKGTNFSLDKKSQWFELEAECIDSLDSIEELFEGSTDGSDITNLIDDEECSQGNSLALFNEKVTEDCNNAITALKRKLVTTPQQAVVDLSPRLEAIKISPQRNIKRRLFEDSGYTEDEAENSIEKVVDASEIPETVGGNAIDNENLNLLNASYGKIILLSKCKEKFGISFAELTRSFKSNKTCTDHWIVLAHGIRVELLEASKIQLQIHCDYVQLIEQDFTGLFCMMFKSCKNRETVHKLFCSLLSCNENQLLSEPPRTRSPPVAIYFYQRSFGNSSFKHGDFPEWIKRQTLLSHESSAAADTFDLSQMIQYAYDN... | PTM: Phosphorylated.
Function: ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of pro... |
A0A0C1N176 | MAAEEKEQLENDKEGVAEGEQTEAEGSSAPPPKSHKKKIIFIAVFLILLLSTGGGILFYLKQQKTEEDKKKLEQKAAEKEIAYFDLDEILMNLNTGGKGQGFLKLKITLQVTGSKNLDAVKMYSPKIRDTFIIYLRELRPEDMQGSIALYKLKTEMLLRVNKIVYPAQINDILFKDVFVQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell inner membrane
Sequence Length: 180
Sequence Mass (Da): 20385
Location Topology: Single-pass membrane protein
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A0A0B2V9P9 | MYVYLRKAFQPNVFGRNAHFVVLFFCFIVLVLKWVTALYVIWFIYDFRCPERGSRPCRLLQNGVQWKYFAKYFPMELVKTAELTPEHNYIIGSHPHGIMSLGAFATFCTNGTGFWEAYPGLKSYLATLNGQFWFPFRREHILKSGVIACSKSSLSYVLSSGKGVAVAIVLGGAEEALDAHPNCYDLLLLRRRGFVRLALETGTYLVPAYNFGENETFTQVTNKRGTLLRKIQVEFRRYAGFSSPIFSGRGIFNYTFGILPFRTPIHTVIGKPIVVEKKLNPTKEEVDRLHQIYCNELRKLFDEHKGKYGIAEDVHLNFY | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 319
Sequence Mass (Da): 36666
Location Topology: Multi-pass membrane protein
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B9TPI6 | PKREIIWKPFLCASRYKSRYRTPTGAVPTTAMKSTAAAPLFQPCSSARAAIRRLCDHLNEAFESTAPAGDSRLRSSNAAFAQRVRSALAEAIADPGLLDESACEGDAHGYRRHLLAADAHGRYAIAALVWMPGQASPVHAHHTWCGYAVVEGELTESLYRWDEAGACATALRTQPRAAGAVSVTRAGHAAIHRLANESGRRAVSLHVYGVAGAQIATHVNDRVRVAESGIESGVESSIGAISSGLNRNGQTVAPDVVAQTP | Cofactor: Binds 1 Fe cation per subunit.
EC: 1.13.11.20
Catalytic Activity: L-cysteine + O2 = 3-sulfino-L-alanine + H(+)
Sequence Length: 261
Sequence Mass (Da): 27627
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Q8SVG7 | MACPSYIRIYNTAGFIVCIVALLASLVFYKTMDPRYLRVAGLSQTFFLMEAANISAKKSNSRYLPTVMQLISRMFIMWVVFWYCGIINWTFPVITTCWYLSDLVRYAFYTFRANTVRVVRYNLFLLTSPIGFVLEMYCLRALYNSLGKIFSYLVVLVALLYIPGFIFLFSHMLRQRKWSRKVKAYKSNRKDL | 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 enzy... |
A0A952P9Q2 | MNNIYIGLMTGTSLDGVDTAICKFDFDGTNFMVEELFFRTYPYSDKIKDMIGGIISDSKLLKDVSQLNFALAKIYASCVSDALNDSGISKDSVKAIGLHGQTIWHQPIAKPYAGMHIASTFQAGSIPALSAITSIPVIGDFRSADIALGGQGAPLVPIFDYHFLKSTTQHVVALNIGGISNITYLEKECSVDDIIAFDTGPGNVLLDIASKKYFGMDYDPGGSFARQGTTDIGKLNKLMELEYIKKPVPKSTGREFFNILLFNKYFESEQNAYDTLNTLTHFTAKSIAENIRSLSAPVDEVIVSGGGARNTFLLELLGCY... | Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
Function: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the... |
A0A0B2VYZ0 | MFTYKFSAIKIAPYCDYDENEHLLFATIFIFSSTVLLILQKRVVCMARVHCSNELIVVTAKTAVTIFSFEVNDAELKLKQQKVLDVDIAVDEIPKLSDGAKTSEDGKKNGCGESSCKAANNDHDDRRKAKNENRPREIGKQILASGFSEDGLLFAVVTSMKTCLVYDTQHDWKLHRRAFRFPKAPAAITFDRDKSHVIVADRSGNICRYKLDECANSITNVHVDINGEESCYEGEPLLGHMSMVLDVALSDDGRFVLSGDRDEKLRISRYPQSFIIHRFCLGHTSYVSSVCVVAQFAFTSGGDGTIRAWNIEEGTTVAVL... | Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Function: Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit.
Subcellular Location: Nucleus
Sequence Length: 466
Sequence... |
A0A1I1H3G1 | MGIYVWLFFALMAVIGAITMLFTRNLMYAALSLLVVLLSVAALYVLANAEFLAVTQILIYIGAVLVLLVLGIMLTPRAASQPPTVTSYQWAMGLFLAGSVGFFLTKIIAQADFIQDKETARPAPLQEIGTRLITEHLLTFEVAGVLLLVALVGAAALATYKSKATQTADFD | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A3G3BDA5 | TLYFIFGMWAGMLGTSLSWIIRIELGMPGSFIGDDQTYNVVVTAHAFIMIFFMVMPIMIGGFGNWLVPLMXGAPDMAFPRMNNMSFWLLPPSITLLIXSSIVENGAGTGWTVYPPLSANISHNGASVDLAIFSLH | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
Q75F73 | MSFSTLYNTLFRRNSVFVGTIFASAFVFQTAFDSGITAWYEKHNKGKLWKDVKLQLQNGEDDDDDE | Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... |
B9TC77 | MKRGLILTLCKWLLACVCLAIATVAAASEHIKLQLKWHHQFQFAGYYAAQQQGYYRDEGLDVEIIEGSKDRPPLQQVLSGQADYSIGDSEILVSRVAGKPVVALAAVFQHSPYVMLSLNESGIYQPEDLIGKRIMMSGDQGGLQFKAMLLKRNIDIRQMTILPHSWRLQDLIDGKVDAISAYAMDEPVQLQQMGYSPAIISNQGYGVDFYGDILFTTERELGMHPER | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the a... |
A0A0B2V8E1 | MLSALVSVVVLHLLPTWAVWTVLSALAIWDVIAVLCPFGPLQILIKLSRARNQPIMSALVSVVVLHLLPTWAVWTVLSALAIWDVIAVLCPFGPLQILIKLSRARNQPIMSALVSVVVLHLLPTWAVWTVLSALAIWDVIAVLCPFGPLQILIKLSRARNQPIMSALVSVVVLHLLPTWAVWTVLSALAIWDVIAVLCPFGPLQILIKLSRARNQPIMSALVSVVVLHLLPTWAVWTVLSALAIWDVIAVLCPFGPLQILIKLSRARNQPIMPALIYSCQ | Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
EC: 3.4.23.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 280
Domain: The PAL motif is required for normal active s... |
A0A0B2UPS1 | MHVATFILLLSFVSFSSSQMAALRGRAYVFTAQANNNNPFPLAGILDFTENNEILTVNGSVSGLTAGQMHGFHVHAVGDIGNSCNAAMGHYNPLGRTHGGPGQPFPTVRHVGDLGNVQASAAGVANINTNFRRVGLSGPFSIFGRAIVVHAMQDDLGLGGVPASLTTGNAGARVACGIIGRLKRKGVRRNGVVSGVKKWPNARIPYVISSQYNERERAVGVLLFMLCKCFSDVGRAGGRQELSLDNGCLQYDTAIHELMHSVGFFHEHERWDRDSYITILWHNIDRDAYDQFGKVDLSESSYYGQQYDYYSIMHYDSLAF... | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 463
Sequence Mass (Da): 51369
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W6JTM4 | MRRLVVTASGGPFRGRSRDELREVSPEQALAHPNYAMGRVITTNSATLVNKGLEVIEAHLLFDIPFERIDVVVHPQQWIHSMVEFHDGSTIAQMGPPRMLVPIALGLSWPERLADIDEPCDWTRAQTWDFHPLDDEAFPAVRLARQVGTAGGTYPAVYNAANEVCVAAFHDGTIGFLDIVDTVARVVEAHDGSPVESVEHVLAADAWARAHATALIQLD | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 219
Sequence Mas... |
A0A0B2UPG9 | MSNKSSERILISGLAPDTTHYMVERYFSQLGTLTECVVMVDRESGNCRGYAFVNFVEKSAVDECLRMQYHFIDNVKVQLRLINSTEDNSILAKVPVKKILISFVGKDLSMRHIHDYFSNFGNVKVDCGGNDEKYEYFAYVLFDDEFACRTCLAIGEHSIAGQVVDVRAVVRKEDLMKAEQADRERAEREAQEIAAKAELEERQSTRADSRPPVSTACYSQQQAYDSTGAHQSWSQSCVGTSKQHEWPAVSSDASLPLTTVSYGTLMAPLFPTGPLPVYTGNGNVGHQLPVAGIAPSYIASSPLLTQSTLQPTTSAYMPQM... | Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 842
Sequence Mass (Da): 94587
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A0A3N5L0J2 | MTDSELNLKYHLKKLSNTAVRIIVGIIGIPLVIALAVIGNIPFLIFCVIVSFLCMNEFYNLFERPKKTPSIITKWAGGFSFHKIVFLIISSLIVVCFYFQKFNYVLILYFLMFLYLTADEVFKTDKHFEAIGTWMLSIVYISTPFGLLSLMDSSAFISNNIVNYAILIMAMVWASDTFAYFGGRTFGKHKLAERISPKKTWEGSIFGFIFTIITGIVIHYIYYPQMKLTHFIAAALIVGVSAQLGDLFESQLKRWVKIKDSSQLIPGHGGFLDRFDSILFAVPAVYIYLYLNSIFK | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 296
Sequence Mass (... |
A0A2I1FSS4 | MSFDIFWDKLDKQVAQKVQDIINEQFRTSNNKPSFIGDIEISEFDFGTVPPSIEIIDVTDPFPEFYLPDNTVVDVDAKSDLSESGGNVNGVGNGVRNGNGGIGGGIGVERVRTRESVVNSEQRTFHHNNSSSSFTRSNPLNNNNNNNNRSSPFTPPITPINRSSSFTTTPITPINRSSPFTTAPITPVNRSSPFTTTPIPPINRSSSFTTTPITPINRSSSFTTTPITPITPIISPSIVTDSSVDYLNYQRQQQRLREQARNDEIPLHLREDYKDYNIQIDDQTQYEPSNSEGEEVPLKQDTDAQIHIEVSYKGNMKMVI... | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondri... |
A0A0B2ULQ5 | MASTNQLCLIVVSILITVECEVRTPAHRLKCTNGGVCERPDLNTLKFFLVGDTGGLPIYPYTTYGQNKVAKALSQMGEEKSSEFQISLGDNIYYTGVKNIFDQRFESSFEDVYLGDAMQKPWYMIGGNHDHFGNITAQVAYTYHSSRWTFPSLYYKISYKFSEKGISVDFIMTDTIVLCGNTRDVEDAGFFDMIFADVSADPDNPKDPKAAQTQWKWIERQLNESTADYLFVAGHYPVLSISEHGPMKCLVEKLNPLLKKYRVSAYFAGHDHTLQHLAVKDSSSEEDVFIDNETEPLMMHYIISGAASRSDRSKKHEGDV... | Cofactor: Binds 2 iron ions per subunit.
EC: 3.1.3.2
Catalytic Activity: a phosphate monoester + H2O = an alcohol + phosphate
Sequence Length: 331
Sequence Mass (Da): 37333
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Q05399 | RNPVTTTLQFTQMNQPSLGHGEAPAAIGRSIPAPGEEYKVVLTFGSPMSPNANNKQTWVNKPLDAPSGHYNVKIAKDVDHYLTMQGFTSIASVDSR | PTM: Specific enzymatic cleavages in vivo yield mature protein(s). VP90 undergoes a cascade of proteolytic cleavages presumably mediated by host caspases and extracellular proteases.
Function: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. Thi... |
A0A087SWZ0 | MFFKILLYLATPISSKLVNFVQSLSDCYDDYLIKRTDPTVMNWALVSNDALNFFIIFCYVSFVLRIGPAIMKNREAYDLRWLMVPYNAALVIMNFYIFWEYAKVRWSGESEDTCTTLEFSDNPKTYRLAEITWWFYLTKYIELVDTVFFVLRKKERQLSKLHIIHHSTIPIVVWSMLRSEPGGYNSFFPLANSFVHVIMYTYYGVAAIGDHVKIHLWFKKYITMTQMLQFILVLYYMLSRPFYGCQISYRSLCINSFIAAFFFILFCNFYIHEYWLKQQCKLAEGNPENICEKRKCK | 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: 297
Sequence Mass (Da): 35453
Location Topology: Multi-pass membrane protein
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B9R8G7 | METRNSMQVIIAAPGVEGKTVKSLPKTEHSLTEFVQSVILNTQVTKEPFYVLNLGAVAELMDTWSRQLPMIQPFYAVKCNSEPSLLGALAALGCNFDCASKVEIQTILSLGVSPDRIVYANPCKAESHLKYAASVGVNLTTFDSVYELDKISKLHPRCALLLRLKSPDDSAAKWASLGSKFGALPQEVEPLLRAAQAANLTVSGVSFHIGSESTNPNAYRTAIASAKAAFDTAGRLGMPPMTLLNVGGGFTAGSFFDEAATVINSALQDYFAEYPQLKVISEPGRYFAETVFTLAASIIGKRVRDDVREYWLNDGVFGSF... | Pathway: Amine and polyamine biosynthesis; putrescine biosynthesis via L-ornithine pathway; putrescine from L-ornithine: step 1/1.
EC: 4.1.1.17
Catalytic Activity: H(+) + L-ornithine = CO2 + putrescine
Sequence Length: 416
Sequence Mass (Da): 44995
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A0A2Z2NTN8 | MRNSVWQVGDYERLRIGSTNADHYLHVQGNAILATILIFGNSLVLWIFGYGSIIWRPGFEHLRSLHAALPGYERRFCQASHDHRGTLELPGRVVTLVPVRGGSCQGMAFELPPVGRTQILSYLDEREQDGYERVYAPLQLSDGVIVPGLTWIAAADNPSWREGESLDELALLISKRQGPSGSNRDYLFNLEEILKTHDMPDAYISVLAGRVRSLIEKR | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
EC: 4.3.2.7
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Length: 218
Sequence Mass (Da): 24500
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A0A2Z2NVE8 | MPQAVLERMQAELLDYRGRGLSVLEMSHRSADFAEIATTTEANFRQLLNIPSDYSVLFMQGGASAQFSLCVQNLDVRGQVAYANTGYWAGKAMDSARALSSVIEVTHCQEMPLIKVPNADQWACSDSASFLHVTDNETIDGIRLHEVPRCNVPLISDMSSSILSQPVDIKQYGMIYAGAQKNIGPAGITLVIVSDELLERSAERSLPPVFSYAAMAKAGSMLNTPPTFAWYAAGLVFQWLLEQGGVSAMAERNRNQAGRVYSALDQHELYINRIHPQNRSLMNIPFQLKNDSLTAEFLKGASDRNFVGLKGHKSIGGLRA... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.... |
A0A2Z2P3V9 | MVWGKLLGGTFGFMIGGPLGAVLGTALGHTFDKGMKLQLSHDVADEDLAPGEAGRIKMAFFTATFSVMGYIAKADGIVDKSEIALAEALMSSMNLDDELRAAAIKLFNEGKQEGFDAEALVLQFREECQQQTSLYRMFVEILIQAALADGVMTSDEEVALLKVAGILGFSEYSFRQLEMLVRFSMGADQSGGTGRGYGAGVGSGTGSGPKPGAGGGRRRTAPEASGQMTLREAFVVLGVESSDDRSTVKQAYRRLMSQHHPDKLVSKGLPDEMIKLATDKTQHIQKAYEKIKESKNW | Function: Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the b... |
A0A1F4Y307 | MKFEELAKSFIKKSLPDSEVELTGEIPAETVAPYREKALTLLSAQLEMDGFRKGHVPAEMALKRIGETAVLEEAVEIFMRDFYPDLVDVHAPSALGRPDIRITKLAPGNPVGITIVTSVYPTIELPKDWKKVGEGIEIETVADILDAEVDEALTSIRRAHAKASSAETGSSPAGQQGDGSEPISTSTSPTEVADAEAKLADPQNLPELNDEFAKSLGKFEGVEDLKQKIKENMKSEKEQKARDSRRGKVVDALIEKVQIDVPSIFVESELDKIIGQMREDTQRFGLSFEDYLQRVEKTEEQIRADFREQASKRAKLQLTL... | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
Sequence Length: 379
Sequence Mass (Da): 42337
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A0A1F9YH49 | MTLWAVALAGAVAVVFAGVMLFHRSLYVSAVCLLVVLLQTGVIFLLRGAPLLGLIQVMVYAGAVMVLVVVTIMASGGGAGDAPRFADFSFPRWLAFLGLAAALLEGALTLRGLGSAPVMVAAAPGLSAAFGQALFTSYALATEAVTLLMFLASLAIAPDREAV | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A1F3B636 | MKDAAGNANQVLIEALKTARRVFVFTGAGASKESGLPTFRDEDGVWKVYDPMTTATMEGFTRDPVMVWNMYRMRQKQISQAQPNPGHITLAEMECRYPEFLVATQNVDDLHERAGSEKLVKIHGDAWQMRCLECGXXYDTREFDFPDEFTHQTLPACPTDGALCRPNIVWFGEYLPFDPITKATNASASCDLMLIVGTSGEVSNGYGFAQYALANGAKVVEINPKEGALTRHAHFWIAEPAGVALPRLWNLVTESR | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
EC: 2.3.1.286
Catalytic Activity: H2O + N(6)-acetyl-L-lysy... |
A0A1I8Q2V9 | MNLKQRLFAANTIHQCLYVLYFVLHHTGCLCFKIEKGMRIYYTRWSYVYTNIVRFLLLASFMGGLAIKVKDEEQYEAMVGHLSPVSKFVLCFECTISTLIYTQIAFSFDFKRMKHLAYCHRLQSLDNLLLKDFPCVQWNYDKSSRKFNALGSFVGFYFIGISLGFVFYLSHCSCGWQSSILIGFSYACMTCGPGTACFLFVAGMDMIRIRFRLIYKLLQISFGTSRPSLHGDVTRLRKLKLLQYYFQEYSSMIPTINEIFSNVSGTGSFHDFAMLTNMGFMLFSLTMGGKARPYEYIYTVLFMVPRFYKIIMIAVYGRLA... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 412
Sequence Mass (Da): 48163
Location Topology: Multi-pass membrane protein
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Q9G8A1 | TQIITGLLLAAHYTADSTLAFXSVSHTCRNVHYGWLLHNLHANGASLFFICIYLHIGRGLYYGSYLXKETWXXGVILLLTLMATAFVGYLLPWGKMSFWGATVITNLFSANPYIGRTLVEWAWGGFSVD | 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 membra... |
N1Q7W4 | WSNLPKEHKLRKFSEALRDLLENAGYNEMYGIELEAPEGDQPAAHTTLIILQKFLRANVDDLAKAKDQLLHALKWRKDYQPLKVRDEVFDAEKFGKLGYVTRVKGAKETPNDEDVATFNVYGAVGKDIKKTFGDTDAFVRWRVALQELTLRELHLEQADKPIPDYGKGPDPYKSLAVHDYMSISFFRQPAEIKASSSKIIDMFQRYYPETVSYKYFVNVPLVMQWMMGAMKALMSKDSIQTMTWMTYGSELYKYLGQEVPKEYGGT | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced s... |
A0A0B2ULX7 | MDHMKDYPFYCTTDCPTNVSASKYAATLYNAMYLYGIALNKSLTQDPVNGWRSGRKILKNAVGRFNGSTGIVVIGQNGTRSPVYSVDAVNVSNGGLSSYASIEVDGSNYRYWGYVTAAGTIIAAAIISLIVGAIYMARAKMREIERENSMWQIPFTRLERLDDASFFFSVIVKRSNSKSLRSLESSRSSGKSLATTVADSDEIAHFSLDKELVYAEKFHFRIQVNKENYAELRLMRTLEQDNLNRFIGLVLDAPMYLVVWKFCSRSSLQDAIQNEKVQIDDFFAYCLMRDIIDGLNALHSSPVGYHGMLTSANCLIDERW... | Catalytic Activity: GTP = 3',5'-cyclic GMP + diphosphate
EC: 4.6.1.2
Subcellular Location: Membrane
Sequence Length: 728
Sequence Mass (Da): 81671
Location Topology: Single-pass type I membrane protein
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A0A0B2VD69 | MLEHEKEKLEAIRLNFDKYWVPINWIYALIFRARQEGKVPSDSFANKLCDEIKFYRYNMQMLCNYDWVPIPLAYPQLVFLAVYVYFAICLISRQFIITERDAPNKSIIDLTLPFMTMMEFLILVGWMKVAEGLLNPFGEDDDDFECNFLLDKNLATALCIVDDASNDAPQLEKDLFWLADEVEPMYSKESVAQPINPLVGSATQANIPTEETKMVVRKSVDINSIGSTRSSARTSKRWKFSAFAERLHRTHR | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 252
Sequence Mass (Da): 29230
Location Topology: Multi-pass membrane protein
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A0A7X3FIM3 | MSGIDTSTDVKICGLQSVEVLKSIVHLPIDQIGFVFAPSRRRVTAGQAADMISFLKQSSEPSGHIPLTVGVFVNPTLDELAEILAVAPLDVVQFHGDETPENCALIKERFHVQLWKVASIQNQEQQGEPGSCSNSQASSSDHVDASAIRAVQDRKSEYAHSIINRLIPYKDTVDAVLIDTLDPVYGGGSGRTFAWDCIPEVQSWARSQGLPLIVAGGLNADNVSGLVDTYRPDGVDVSSGVETQGVKDIAKIAAFVGRVKKNGSSTT | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 267
Sequence Mass (Da): 28527
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A0A8R1DME3 | MASSTMVEALDFSKIGDTTNSARQALTDCSNFVAKVVMHSSGSAFFHCDTPTGRQPKSVFYSDSLDLSQYEKERLESRKRSSASLSPSCSLMDRKRSRNMSLVAPQSDKICRYSTTSLEKAVDPFKEDDDVFVADDATSFTYIPSEVPRSTTSLWELGGSLERKTSDTSGNGGSFLEKEVKYTLPSVEFPQKASQAYRSISAITLLSEFHRLGDAFHSIYVIVDCRYPYEFRGGHVRGAINMYKRGEINAMFFPDDVDLMVTNKRIPIFYCEYSQKRGPTMANAVRSIDRVRNELRYPHVEYPEMYLLDHGYKALWNRRE... | Function: Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle.
EC: 3.1.3.48
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Length: 520
Sequence Mass (Da): 58730
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A0A5B9P7W9 | MSSQASIRKWGPHKLDAAIEQRLQRLAKAEGVARIAVMPDVHLAGDVCNGVVVASERLIYPQCIGRDIGCGYLTVRLREQHIDETIAARLLAGLYRAVPNCKRSVAVTPEFDIELSAAPLQKVFSREGRWQLGTLGRGNHFVELQRDQEEQLWLLIHSGSRAIGQAISAFHLRDAETDSASGLKFLDADSIAGEHLLNDLQWARQYAAANRLAMLDAIERDVLSKLDFDVHRNTMIHLDHNHVQRESFGERQFWVHRKGAQRLLTDQQSIIPGSMGTTTYAVAGRENEDALNSCSHGAGRSMSRKEAAKRIPSKTFRREM... | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 370
Sequence Mass (Da): 41719
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A0A1G7D8G5 | MSKDTETAFAAALAARGLVLPEGMRIGAAARRQALGLGLVAVFLWVLRDKLANLDGAAILAALARVDALSWALAIAATVASFAALAQYDALIHRALGTGTAPGPARRGGWTAIALSQTIGFGLVSGALVRWRMLPDTSLAQASKITATVAATFLAGWSVLTAAVLLVAPVDHQHLPVLAVQGLAVLGLVLGGGLALATLVLPEGLRLGRFTLRLPPLAVMGRILGLATLDTAFAAAALWALLPGSEPLSFLTLYPAFLLAQGAGLVSNTPGGVGPFEITLITLLPGTAQPELIAAILAWRIVYYGLPALAAIALVALRPA... | Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Membrane
Sequence Length: 674
Sequence Mass (Da): 69852
Location Topology: Multi-pass membrane protein
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A0A0C1E5M4 | MPTPRICIIGSINVDFTTYTSRYPEPGETLLASAHEISGGGKGANQAVACGRAAFASKTEHEQDRAGVNTTAVTERSDAPTGSASIAVEGAAGGENRILVVPGANYAGMSDVDEILARARREMAGLSFTGGHEVVVLQGEIPRRTVLGLLRYFNGSRKHNDTRAHVVLNPAPVFAEGIPVDALRGMSVLIMNETEARMMAQFMGVLDSLEPEELATRFHRDVDVQIVLITLGSRGVFYSTKTSAAGFVAGVSVEKVVDTSGAGDTFVGYFAVSLARFLATGMPLASFDTHIEESVRWSNLAAGRSVEKKGAMNGIPFAYE... | 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 ... |
A0A1H4T2J1 | MATAPSRGWWPATGRRRHSHAERPARPLGGLIWLHVPGQASLSAMRELARRLIEEDGVAVLMTGEGGGARAKGVIFDQAPEDGAQTVRDFLDHWRPDAVVFSEGEIRPALLHECAERQLMLIMADASDPWFLRGHESWIPGAMRRSVSALSQVYAIDQAAMRAWRRAGIAPARVVSSGRMEESSLALPCLEAEREYLAAAMMTRPVWFGARVPRSEEGAVLAAQQYAMQLAHRLLLIVMPEDPARAAPLARELADQGWITASRSDEEEPETETAIYIVNDAAELGLWYRLAPVSYLGGGLSGTGLLTSPLEPAALGSAIL... | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A2R8B356 | MARNGPQLDRRAGGRGAPLPSQGVSHKRVRTSQSCETVMRLSRYFLPVLKENPAEAQIVSHRYMLRAGMIKQQAAGIYSWLPLGFRVLKRIEEIVHEEQIRAGHIPLLMPTLQPADLWRESGRYEDYGEEMLRITDRHKRDLLYGPTNEEMITDIFRAHIGSYKDLPLTLYHVQWKFRDEIRPRFGVMRGREFYMKDGYNFDLTKEDALHAYNRHLVSYLRTYERMGLQAIPMRADSGPIGGDDTHEFLVLADTGESEVFYDSKVTDIHLGSREIDYDSHEECRSVMEEFTALYARTDETHDEARFNERVPAERQRRARG... | Function: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
Catalytic Activity: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
EC: 6.1.1.15
Subcellular Location: Cytoplas... |
A0A4Z0MTG3 | MKQLIAFLCLSWLLIGRAVAYDFVVAQDGSGNYKTVQEAFNAVPDFRKKVTTIFIKRGTYKEKLILAGSKNLVKLIGEDLKNTILTYDDYNQKKNIFGEDKGTSGSSSIYIYGSDFSAENITFQNSSGPVGQAVAVWVAGDKARFKNCRFLGFQDTLYTYGYGSRQYYQDCYIEGTVDFIFGSSTAWFEGCTIFCKKGGGYVTAASTPDSTRYGYVFRNCKITGDAPAGSFVLGRPWRPYAKTVFMQCELGEQIRPEGWDHWEKESNKQTASYAEYKNRGKGFQPPRRVSWSKQLTDQQAQEYTLDKVFRNWNPTKE | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 1/5.
EC: 3.1.1.11
Catalytic Activity: [(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O = [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol
Sequence Length: 317
Sequence Mass (Da): 35928
|
A0A0B5G970 | TLLQASEYYEAPFTVSDGVYGSTFFVATGFHGLHVIIGSTFLIVCFFRQLKFHFTSSHHFGFEAAAWYWHFVDVVWLFLYVSIYWWGSCPFSIN | 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, comple... |
A0A8R1EIJ8 | MKGERPAGLGKHVKTSSWVPQNQILHHKNTVMFVSHGGLKSTKEAICSATPTIFVPMFGEQTRNAWLIKENGFGRIVSKFNVNAKELGTHMREVLEHPDYQRNANNFLSLYADQPISTLDEGAFKFNRLVKYGGKMPGWFYPRGIDLSYLMVLNLDILIILPVLCVFLIFTR | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 172
Sequence Mass (Da): 19526
Location Topology: Single-pass membrane protein
|
A0A2H0XJT3 | MDILKAVILGIVQGATEFLPVSSSGHLALLGGFLGFEEGTLMATMMHAGTLLALVVYFREDIARIILSPFKKDIKYLKLLWFLILGSIPVVIFGLLLFPHIEGIFDSPLIIGICLIFTGIILFISGFMKKKKSNMRFWDAILIGIGQAIAILPGVSRSGTTISTGTF | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 167
Sequence Mass (Da): 18145
Location Topology: Multi-pass membrane protein
|
B3CR68 | MQNYYDYFKSIHIISVIFWMAGMLYLPRLYVYHTQVQTESESYNMLCTMERRLIFIMSLSMLLVFIMGGILFFIYNITIYDTWFHVKMLSVLLLSTMHGMFIRYHKMFVNKSNKKSTMFYKVINELVALLIVVAIFMVVLKPYW | Cofactor: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX.
EC: 1.3.99.-
Subcellular Lo... |
V5KCX8 | TLYFIFGIWAGMVGTSLSVLIRMELGTPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLSPSLMLLIS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A939E2E2 | MFNRQLAAELGFDPDWLSSAGGIDFLMGRQPPAGAEPVAQAYAGHQFGNFVPLLGDGRAVLLGEIETPAGQVIDLHLKGSGRTAFSRGGDGLAPLAAMLREYIISEAMHGLGIPTSRSLAVIDPGWQVVRNTPQRAGLLVRTAPSHLRVGSFQYAAARQLADPGSTLTRRLAEFAIERHFSDLLPGNQSAAATDSTSSTAATGGHPDTYRRFIEAVCDRQAGLVASWMGIGFVHGVLNTDNVTVGGFTIDYGPCAFLDNHDPAAVFSSIDTAGRYRFDQQPAVMQWNMARFIDSVLPLVFDGRPTIGGPAHSFAMEQRAR... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
EC: 2.7.7.108
Catalytic Activity: ATP + L-seryl-[protein] = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate
Sequence Length: 510
Sequence Mass (Da): 54820
|
A0A379GE81 | MRIILLGAPGAGKGTQAQFIKENYGIPQISTGDMLRAAVSAGTELD | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 46
Sequence Mass (Da): 4761
|
G0EEJ0 | MLLAIALDGADSPSGGCTTHLASLIFLRLALRENLTPADYPWLVRLNPSIPMKTRGNGSVTLWFSTDSVERARRAAMIARDMLVEYAESTGSKTKASIVAILFSDEALPRREHTLTRLYYDALTRLVPIKHAWEALNKLKLDGAEVLVAEGNSIVGALAGVGARLDFDHTFELLVYMPPRLWGTRPQLEQDAVRKLDHVLGFYGIASIDYATGRALIQPHGPDPVLAGVRSDTPEALANSLQFVPREFYTHAIIYRSNQHTGVHIRDDLVEHIKPYDCIRLHGVLGNTRIIGGGHVIAQFCDDSGCIDAAFYRETGELRH... | Function: ATP-dependent agmatine transferase that catalyzes the formation of 2-agmatinylcytidine (agm2C) at the wobble position (C34) of tRNA(Ile2), converting the codon specificity from AUG to AUA.
Catalytic Activity: agmatine + ATP + cytidine(34) in tRNA(Ile2) + H2O = 2-agmatinylcytidine(34) in tRNA(Ile2) + AMP + 2 H... |
A0A3P6FNE6 | MTLGGGGAPLMLPAKFSVVTEYTDFATPEANFGFHIECGFSYIHSRLPGHLGEFLTLTGAILNGKELVAIGMATHFVPRAKVVALMARLARLDSGDTDVVRSTIEEFSEKVDLDKDSILNKQSIIDACFSKESMKYILVVFLQEAEGSKEGNEWITRILKRLKESSPTALKINLRSIREARNQTLGDCLKKEFRITVNIMRSTISIDAF | Pathway: Amino-acid degradation; L-valine degradation.
Function: Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism.
EC: 3.1.2.4
Catalytic Activity: 3-hydroxy-2-methylpropanoyl-CoA + H... |
A0A0B2UN10 | MCQVVIVVTRASGVVPDASNTHFDSTRLRVLEGLVNEVSSEWCCHLADSDTLALFLPLHKPVSTLSKGAFVSLLEFCEDELAVKRVLICVNKNNITPEISSCFKYVGFTPLHPDHYPSKLDPNTIFAMVPMVLDEDGAHLGKLLDCLPLETVSFAFAYGSGAVAQYGCSTADKMVDFVIASNNSLAFHEENLKRNPAHYSIIRHLGARPLTNLQRGFAARVFYNTHIRHKGKLLKYGVVECDDLQRDLLDWRWLYLAGRLHKPILQVIPPTEALASALRENRASAVQATLLLLPDTFNLEQFFMQIVSLSYKGDFRMFFG... | Pathway: Lipid metabolism.
EC: 2.7.7.41
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 460
Sequence Mass (Da): 51598
Location Topology: Peripheral membrane protein
|
A0A087TLH5 | MVFAGAVSAREYFQCLDDPNCKTFGRQSWLMVAIIITEFLVIAKFDYETITKPLPVHIVYFWVFALCALFFWTVWKFFFLPKLNVSKLDEHLFLVDQNYQVGDGNLIENSALKKNGTYNTYRNTTKKIN | Pathway: Lipid metabolism.
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) is replaced by L-serine.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + ethanolamine
EC: 2.7.8.29
Subcellula... |
A0A454A0K9 | MRRSTKWMITVHYYIALITGILSFCIDQTTGEVYATAIVTVYSALISVAVFGLVPLLYYVDYNSPYLHVQISGLLFVLRVIGLMVTVICNWTKRQEFMATLRDLMKARDYFLKRWPLSEKLEQKYENTLRMKYFCGFATTASMLLLSREFFKLQFKVDSKYILPATMFMISVFNVILVNYFLCILHLNTLQMALNEEVKKILKMSRHLWHLQRSKQIGSGALITQSCKLSDDLDELAAIQYRLHLLGHRVFKLYDIQAACFTLMIYLNNVSVYYMTYASFYRDQVIAKQYSPWVLMFMPLFLTFYYIDLTLFTLTKLAYP... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 347
Sequence Mass (Da): 40722
Location Topology: Multi-pass membrane protein
|
A0A7S1X5L2 | WLATMHWRDAEEGSWRRRGWRLLMLSDNVVQTARLANFLVFIRTGDYRTVLERLLRARLLYSQPTMQRAISFEYLNRQLIWQELSELILNILPLVNPEKLRGVMLRWLPPVTASNGSTGLTSLKSQRSPQSCPIC | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 135
Sequence Mass (Da): 15782
Location Topology: Multi-pass membrane protein
|
A0A448UYL2 | MQTLIINAHPDPQNKTAYCTNRLVDCLTKKLPDASVLNLYNEDIPELTAETLPVFSGAYSGEGKDAELSKVAQHFLARNAELLEQFKAADRVIIAMPMHNFSVTSRLKDYLDNIIVPGQTFQYTREGMQGLMGGHKALLVQSSGSVYSTGPLAPWEQSYPFLRIVFGMLGFDSTDIVRAEGTMDPNIGPDVAVERACAELEQKLPEFLA | Cofactor: Binds 1 FMN per subunit.
Function: Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
EC: 1.6.5.-
Catalytic Activity: 2 a quinone + H(+) + NADH = 2 a 1,4-benzosemiquinone + NAD(+)
Sequence Length: 209
Sequence Mass (Da):... |
A0A087TFI4 | MTFNCLGQQTNSTVKVETEDGAMCVKSNFKLQNILQDDVSNSDLVLEAAFRLQLSSDVVLKAIALDSDQSPSILEYFKEEVLLNVPYNILCTNCNTVLSSQPLTFKSIEEFPGEYSELSETWFCHKHPEHRGTVLANALYISQMYFHLQNSIVDRLHSMTDHEEYKCLKCSSIC | 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... |
A0A0K6GX48 | MTDLRPDPDALLARVQAEAARACRGRLKIFFGAAAGVGKTCAMLEAGRARLQAGVDVLVGVVETHGRSETALLAATLPRLPVKRIPYRGTVLLEFDLDAALARHPALILVDELAHANAPGSRHLKRWQDVHELLAAGIDVYTTLNVQHLESLNDVVGGITGIRVAETLPDWVFDEADDVELIDLPVDELLARLSAGKVYLPEQAARASQHFFRKGNLIALRELALRRTADRVDAQMRDYRDHAAIRDVWAVNEGVLVALLDVAEAERLVRAGKRLAERLKAAWHVVSVETPSTRRTAHRREALAAALRLAESLGAVVHTL... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 908
Sequence Mass (Da): 97611
Location Topology: Multi-pass membrane protein
|
A0A0B2VTX9 | MPRRPRRFLLIVLTAVIGVVVLSLCSNLLLDVGHSLVQEHNRHDSSGDGDEFVYRKKEVRLFVGTPFFRTPVGNAYLDNCSVREHNRHDSSGDGDEFVYRKKEVRLFVGTPFFRTPVGNAYLDNCSVRKHCKIVDDKDSSDAVLYHAPDFVLMGTLKPNQITVLWSLESPINHRFYQNFERQINWTMTYRRDADVWFPYGVITKRREPIRVDFDELWKSKKKMVVWLISNCGHTNGRIELTKALQEAGLEVDIFGACGRRPTPNDCDGVNKQGDRCVAELFKPYMFAISFENSLCKDYITEKFFEVLEKRYAVPIVMQRK... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 435
Sequence Mass (Da): 50411
Location Topology: Single-pass type II membrane protein
|
A0A136N183 | MKASEFKFKQFIIRQDACTMKINTDGILLGAWSSVEGKKKALDIGTGSGVIAIMLAQRSPHLLIDAVEIEESAARQAQINMMRSPFASRLITYNMSIQEFTNIAKHQYDCIVTNPPYFTGGTIPSNLQKAGVRHTISLSHDELLSVFSKLLTTDGAANIILPFTEGLSFIEKAASHHLSPSQITKVYPKVDKPVERLLIRLQPNYSGPPIEHELIIHNSNDPKDYTPAFATLVRDFYLFM | Function: Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
Catalytic Activity: adenosine(37) in tRNA1(Val) + S-adenosyl-L-methionine = H(+) + N(6)-methyladenosine(37) in tRNA1(Val) + S-adenosyl-L-homocysteine
EC: 2.1.1.223
Subcellular Location: Cytoplasm
Sequence Length: 240
Seque... |
A0A0B2VCT5 | MSQSLFERLKVHKSAVITLKRQYRMNRAIAKLSSALFYKGELKCANELIAEASLENMGFENLDQLSLSEGLQLNVSNGVDGSVVFIDTQSPKNSECRMEFGASPGAVYNSGEIKIVNKICCLFIRLGISTEDIGVISVYRYHADVMRKAIPKGVEVNTVDQYQGRDKRVIIVSLVWTERDGARRSELLSDARRVNVAITRAKHKLILVGCKQSMMSYETMAALIGLIPESQIKSIAEPSKEGTDGFGGDS | Function: Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA... |
A0A379GEM5 | MKKYFLLFALLMLSGLAYSDDEKEVPAVITEQPFIKVEEEKVTLTSPDQIIPSRQETRLFATTAPTYGALKLQGASPDGYLEFGVRSDEYVSQAILDLEFTPSPSLLPIESHLNIYLNDEIMGVIPLKKEDLGHKNHITLPLDPRFIQDFNHLKFTFIGHYREICENQANTTLWLDISKNSQTASHLSIIEIE | Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Function: Binds the cellulose synthase activator, bis-(3'-5') cyclic diguanylic acid (c-di-GMP).
Subcellular Location: Cell inner membrane
Sequence Length: 193
Sequence Mass (Da): 21926
|
A0A386I3J8 | VMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLMLLXSSSMVEVGAGTGWTVYPPLSSTIAHAGASVDLAIFSLHLAGISSILGAVNFXTTIINMRAPGITFDRMPLFVWSVLITAILLLLSL | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A8R1E9T2 | MFTGKIKQFSYKVLNKLFPYFPQNSFLGAFAKFNTYTILWRMEKSVAGAEKLEHLHLVKWLPQKDIMRHPKMKLMIAHGGYNSFLEAAQAGIPAVLMPLFADQKSMRNGLNDTEWLRFLINLPEL | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 125
Sequence Mass (Da): 14519
Location Topology: Single-pass membrane protein
|
Q6SL05 | MINLFQLFFVFGLILGILISISSSSWFGVWVGLELNLMSFVPLVTSVFNRLYSEAALKYFLIQAFGSVILLFSVLGYVFSSSLFFLIFLMGSLLLKLGAAPFHFWFPNVMGGLSWMGVILLMVMQKITPFVMLNYIYLCVGDYLLIFLVMSILVGSLGGLNQLLLRVLLAYSSIGHVGWMMGGILVSDVVWFLYFIIYSLCSLALILFFMWGDINCFSQLYGSLFFSYSYLLFIGLLLISLGGLPPFLGFYSKWMVIFGLLNLNYSLICLFMVMFSLIVLYWYLRLGYSLLLGGYDFKGWLLYGVGGSGMFYLLSFFVVL... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A959RJR4 | MIYFFDVFITVILFSLFAISHSILAAFDVKKRITEKIGSKIAFYRLFFNISSIIFFIAAYYLSPKPNVIIYDLQFPYDLVIFSIQLLGIIGFFWAGSYINLKEFLGITQIKRYYQGNYKVDNLDEYHELVVNGPFKFSRHPIYFFSIIVLGFRSSMDLFYLVFFLCMLAYFYIGSVYEEKSLEKRYGKSYLDYKISVPRLIPIPVKIIGRK | 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: 211
Sequence Mass (Da): 24903
Location Topology: Mult... |
Q8SUH2 | MTFLCDGRIQSFFETNGRRNHRSFVVLLGENAKLQLPTVHRVLQGHSHGPVETVVWCHKNDITKKVSRKASGKKQRGAVQNEESEDDLSLFIKSNDIEFIEYKESERILGRTVDMLILQDFEALSPNLIATSVETVRGGGAIVLLLDSTCSMETLISHRVDIHEKIGEFEPRYNKRLFRSLMNSRFALFLDDKLNMLDGVSMPDIQNPGVVERKATPLEPHSSGNEVLKGLGKTGDQIRIIEELFKALELRESRTIFSITASRGRGKSAALGISIAQAVNLGLLSVYIASPAIENVKTVFMFLITGLEKLGYKRYVDFKI... | Function: RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) in 18S rRNA. Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tR... |
A0A2N2SSN7 | MIEALMSVTSVIGRALFNLPVPGDYELVQMLSAMGIAMCLPYCQLKRGHVFVDFFTLWAPTSLKRVLDAIASLLLAGASFLLAWRIWDGMLEMREYGETSMVIALPVWWGYIPVAPSFVLLGIAALYTVFEELSGKESA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 139
Sequence Mass (Da): 15381
Location Topology: Multi-pass membrane protein
|
A0A1I8PH47 | MGVTFANPEDCILTKKDKIAYDNPHIERVRRAHRNDMENILPFFTAGFFYVLTNPSALLAINLFRLVGVARIIHTIVYAVVVVPQPARGISFFSAFIPTVYMALQVAIFAL | EC: 2.5.1.18
Subcellular Location: Membrane
Sequence Length: 111
Sequence Mass (Da): 12470
Location Topology: Multi-pass membrane protein
|
A0A6C0X5M5 | MNFYLLKGWGVLLLGFSLLMGYFSLMTLDSDSSLFIEWEFFFLGGSMFVVSCIFDWMSLSFLSTVSLISGSIMFYCLYYMANDKNGNRFILLLLLFIFSMMVLIVSPNLVSLMLGWDGLGLTSYCLVIYYQSENSESSGMLTILSNRLGDVGILIVIGLWSSYGSWNFDGWVMKDTLLISGMLMLSSLTKSAQVPFSSWLPAAMSAPTPVSSLVHSSTLVTAGVYLIIRFYEVLKDSGILFFIFMVSFFTLFMSSHGAANESDLKKIIAFSTLSQVSLMMMVVASGSPMVAFFHLVMHAMFKSSLFMCAGVLIHENSGCQ... | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed... |
A0A7S1X6R4 | MPMERSTPRLVALMLSLLLALLLPGRGAGASAPPRLSDERLVFSTAFGHIEMAFYPDVAPHTVSHILKLARIGGYDSNHFFRVDKGFVAQVGEVADARLVPLTPLQKMEAVKTVPLEVSPEVKHTKGVVSLGRFDDPHSGRSSFSLLLGDAPHLDMKYTIFGQVTQGLEVLDKMQLVETKREGIFVMPKERITIFSSYVYSSSAAFSDTGTCEQRLRELSERFNIQSHQLQEARARCLPG | 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: 240
Sequence Mass (Da): 26539
|
A0A0B2UR22 | MLSAPYTMITFPFLFALMFGDLGHGLIMFLAALFFIMKEKQLEAARISDEVKLRFILGVLHIFQTFFGGRYVIFLMGCFSIYTGFIYNDAFSKSFNLFGSSWRNIYSRRFLDDQPAERFLMFTPEWAYYNVVGVSW | 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: 136
Sequence Mass (Da): 15938
Location Topology: Multi-pass memb... |
Q5J809 | FFGHPEVYILILPGFGMISHIISQESGKKEAFGSLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATLHGTQLTYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLVHWFPLFTGLSLQPTWLKVHFAIMFIGVNLT | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A1X2HCR8 | MVFSLRYRRTVPKTASSTASPFLYYDQRKDIHQNENSDQEAEHKARDRGPKAKSTAWFDTAQLLLSTMLALVVRLWSLGSPSTVITSEIALCKQVNWYLQHKFFIGAFPPLGGLFYATIAWFLGYDGAEEILYAGQHMASFPLQKLRLASAVTGTLVIPVGYLTIRSLGYSRAASTLIAGLLILENGFVTQSKFVLPDPLLCFFSSLTAMIWAVQLRAEKPSWRCQIFTGLCIGCAMSIKWQGILSMAVVWLSNGLQFWEKLGDKRNSARALAIDFMKRVITAAIVPVCVYFAFFQLHFGLIPNSGDHDLLISPQLKYFL... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
B0LXM1 | VIYYNANWELERTNQSGLERCEGERDKRLHCYASWRNSSGTIELVKKGCWLDDFNCYDRQECVATEENPQVYFCCCEGNFCNERFTHLPEAGGPEVTYEPPPTAPTLLTVLAYSLLPVGGLSLIALLAFWMYRHRKPPYGHVDIHEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDFVAVKIFPLQDKQSWQSEREIFSTPGMKHENLLQFIAAEKRGSSLEAELWLITAFHDKGSLTDYLKGNIITWNELCHVA | Catalytic Activity: ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-seryl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 263
Sequence Mass (Da): 30006
Location Topology: Single-pass type I membrane protein
|
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