ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A6B1ABZ6 | MAQRTPSQHARSTRGAGLGTEPSSAVWDVVARVDTGELATAAALLHNLHPADQADALAALDGRERRRLLDRIDSHTLAELLPFLTPEELEHVAPDVALPQLTAALDETPAQLGADVLHAIPLTDAELVLDRLPKAGLVEPLLQHDDDSAGGIMAPELMVLGPHLAAEQALTVLRAAAPAPTVRDTVYIVDTEGVLLGSIGLHSLVFAPPMTALRDLMEPIGPTVTTDMDQEDALKILQRFGLHALPVLDDDGRLVGVTTSDDLLDIAQQEATEDMYRLVGLVDDQALTTPVTTALRRRLPWLLLNLATAFAAAAVVAAFE... | Function: Acts as a magnesium transporter.
Subcellular Location: Cell membrane
Sequence Length: 465
Sequence Mass (Da): 49057
Location Topology: Multi-pass membrane protein
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Q7PSX4 | MTPLGKMSSVWLTSVSVFLLLLLQQPPVDGELFTALADMEELLETEAVLITNLDNYVQAQEEKLMQLRQKMHEYRREHAEAARDVSAYLSNPVNAFLLTKRLTTDWRYVENLMTYEVGKEFLENVTAYRSVLKFPSDEDLNGAAVALMRLQDTYNLDTASLARGMLNGVQYSTELSAGDCFELGRQSYLNGDYYHTVLWMREAMDRLTGEVNRTATKEDVLEYLAFSTFKQGNIQTALSMTEELLELVPDHERAVSNKAYYVKELQKEAQQKILRGDDGSEEVPVDTTTKEATPHVYDTNERKLYEQLCRGEQQPPIELR... | Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
EC: 1.14.11.2
Subcellular Location: Endoplasmic reticulum lumen
Sequence Length: 553
Sequence Mass (Da): 63567
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A0A134BKY5 | MGKKNVLAMILAGGEGKRLMPLTLDRAKPAVPFGGTYRLIDFALSNVVNSGYLRSVVLTQYKSHSLDRHLATTWRMSDLLSNYVAPVPAQQRRGKHWYLGSADAVYQSLNIVRDENPDYILIIGADNIYRMDFSQMVDDHIKSGLPCTVAGIRQPIELSSAFGVIDQTNGTINRFIEKPDTCEGLPDDPTKFLASMGNYVFTTKDLVAALEEDAKNEESKHDMGGDLVPYFVKHGGVNCYDFIENEVPGATDRDRDYWRDVGTIDAFYEAHLDLLSVSPVFNLYNFDWPTYTKLDAWLPPAKSTFNDETRRGMALDSIVS... | Pathway: Glycan biosynthesis; glycogen biosynthesis.
Function: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
EC: 2.7.7.27
Catalytic Ac... |
A0A034VMP3 | MAFAGLKKQINKANQYVTEKMGGAEGTKLDMDFMEMERKTDVTVELVEELQLKTKEFLQPNPTARAKMAAVKGISKLSGQAKSNTYPQPEGLLADCMLMYGKKLGEDNSVFAQALVEFGEALKQMADVKYSLDDNIKQNVLEPLHHLQTKELKEVMHHRKKLQGRRLDFDCKRRRQAKDEEIRGAEEKFAESLHLAQMGMFNLLENDTEHVSQLVTFAEALYEFHSQCAEILRGLQETLHEKREEAESRPKAEFVPKTLLDLNLDGTGTNDTDSVSTPAHRASAASPLPSPLRSPAKSLVPGATTPQRQQQPCCQALYDF... | Function: Required presynaptically at the neuromuscular junction. Implicated in synaptic vesicle endocytosis.
Subcellular Location: Membrane
Sequence Length: 373
Sequence Mass (Da): 41845
Location Topology: Peripheral membrane protein
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A0A6S7FLT7 | MARNRVNQQFRRERTFSSSSTVSTDDGHHDLSEQIVVDVTLEYFYKPRTLTALGFLLLYLAYFAFTHDPHLELSKNIFKGLIAISVVFLFVCMLVAPNGPFTRPHPLLWRIVFGISVIYLLALTFLLFLNYRQIKDILIFIDDDLKYAGPDMKEYATDCRLSWAKLYESMDLFILSHFIGWAGKSLLMRHAVLCWSASITWEITEVFFAHLLPNFKECWWDAILLDIVICNGLGIYVGMYLCKKLEMRTYHWESIKDIQSTTGKLRRAILQFTPASWTRVNWTDSNSTYKRLFAVYILGVVWQLVELNTFFLKHIFHIPN... | 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... |
A0A376MW51 | MRIEGQVKVKFDVTPDGRVDNVQILSAKPANMFEREVKNAMRRWRYEPGKPGSGIVVNILFKINGTTEIQ | Function: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the rele... |
A0A2E7UZP5 | MGGILLLEDGRMFTGEAFGARTTRVGEVVFNTAMTGYQEVLTDPSYREQIVTMTTPHIGNYGVNEQDMESTQIHVSGFIVRKLSRRPSNFRSQGGLEPWLRAAGIPGLQGIDSRALVRHIRDKGAMRAVISTDGTSVEALRERLNDWPGMAGRALAYEVSRSSPEVTTEGKSGSLRVNLVDGGAKRNIGRLLAQAGCTVREVPLSAKAAQWMDDCDLLFFSNGPGDPAALGDVVQEIRKVVGKRPMAGICLGHQLLALALGAETYKLPYGHRGANHPVRDEVSGRVEITSQNHGFCVSREALEKIGATVTHTHLNDGTVA... | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1.
EC: 6.3.5.5
Catalytic Activity: 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate
Sequence Length: 364
Sequence Mass (Da): 39158
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A0A6N9N4F8 | MDTIRITKCFTFDMAHALKGYDGLCRNIHGHTYMLRVTLAGKIKHEDSNPKNGFVLDFGDV | Pathway: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
EC: 4.1.2.50
Catalytic Activity: 7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate
Sequence Length: 61
Sequence Mass (Da): 6914
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A0A164BUF5 | MKIAVAGAGAVGGYFGALLKKAGHDVVFLARGKHLEAMKKSGLVVKTNDQLLTIDGVFTDKIEDFADCELILFCVKSTDTESTAEQIASLQNDRAVVLTLQNGVDNEEKLAQILGGKRLLSAATYLSSHVEEPGVIKHSGRAKLVIGALDESLISFRDKVADLFRQAEIFVKTTDDIMLDKWKKLLWNATFNPLAALSKATVGEIMEHKELRKTAENACREVMRVANKIGIPLDEEMFHRTFANSGAALKHKPSMLQDRLKGKRMEIESLCGFIVKKGRQIGVETPVLQTLYSNLLFLETHR | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 302
Sequen... |
A0A3C0K3H4 | MKEVTTADRKDDHIRINLEENVQFNSISNGLDKLYFVHNSVPETNMSQIDTSIDIFGKELRMPLLISCMTGGTDKSGNINRILAEVAQQMGIGLGLGSMRVVLEDHEKIDSFCLRELAPDILLLANIGAVQLNYGVTVDDCRQLVDLSESDALVLHFNPLQEAVQDEGQTNFSGLLNKIEHLCNEFSRDSIPVIAKEVGWGFSEQVCKKLSEVGISAIDVAGAGGTSWSQVEMYRSDDESNKKVASVFENWGISTVEAILNAGKGAPDIPCIASGGLRNGLEMAKCLSLGASLAGMAHPFLVAAMNSPERLMSTIYEIEQ... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Sequ... |
A0A6S7KN11 | VEKFKHNQQPHNSLHSMFNIHTGNTLPLNENWPHLQIDAVSLYLLVLAQMIASGLTIIYTLDEVSFIQNLIYYIERAYRTPDYGIWERGCRSNNGHRELHSSSIGMAKAALESLNGFNLFGSQGTSSSVIYVDPDAFNRNCTILKTLLPRESSSKETDAALLCIIGYPAFVVDDEKLKETTGERVVENLM | Pathway: Glycan biosynthesis; glycogen metabolism.
Function: Phosphorylase b kinase catalyzes the phosphorylation of serine in certain substrates, including troponin I.
Subcellular Location: Cell membrane
Sequence Length: 190
Sequence Mass (Da): 21379
Location Topology: Lipid-anchor
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A0A0N5CVL4 | MNSSNILIFQVEVSKVEAPPLFDKALITHLERLSLVRFSDEQAIYNLKQAVSYANQLKLVDTTGIEPLETLLENIPCPLRDDIVDEDVMTKNEVLMNAAKTVEDYFVTPPGNIPLEESDKQYLEKIEQ | Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Catalytic Activity: ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln... |
A0A0A9Y7X6 | MSWDSPRRDGDILCCCEFLDSGGERNHILACCCNCQELDLCCERLVTCQKVPKTIIWKIFSTATNRMRVPWRGGAVQISLDSVAPVLLIPVILLIAAHGPMMSVITFSFLPLFLLYTHFLFMKIKPHNSFFLSWTITSTVLLFLLLWSFSEMLEIRNDEFFVFLLITAAALYSINKVKQKEILSFVTEDQLLDGGEKCSECSILLPPRAYHCTSCNACILKRDQHCSWLHCCIGQYNHFWYMMFLIATLSQFVLYSNLILTTACHPFRVIGSIMLPDDCSDVYFDLVYAICFVSSIYCIEGAAFVFSVLALECWLITLGI... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 367
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 42155
Location Topology: Multi-pass membrane protein
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A0A2E2WDA1 | MPVTWTMLVAVGTGGALGAVARFAVSRQVSLWLGAALPWGTLAVNVLGSFLLGFLAAWFRSRTELPPEWQALWTVGFLGAFTTFSTFSNEVVGLLQADASLRALATIAANVLLCLCCCWGGVWLARSFGAALNAAA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 136
Sequence Mass (Da): 14280
Location Topology: Multi-pass membrane protein
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A0A5K1JEJ1 | MEKTLILLAGPPATGKTDLADRIKARHTSESFLSVSLDDVKEEYWDTYGFNNAEEKAQVDASALQEWFRRLDVAMADGPQIMCDYPFSAKQHDRLAELADKNGYRVLTIRLVADPVMISKRYRARDLKPTRHLAHIVTHYHKGDVLEDRSKGDDLVDLDILVDRIKNRGYDTFELGHTIELDVTNVDTVDYPGFLAKVDEYLDDPSSVATIAAKAGAELTDENLCSRIDYTLLKPTATWDQIDAICAEAFEYGCASACIPPSYIARAHKVYPDLALTTVVAFPLGYMTSSAKAAEAADAYANGASEIDMVIDQGMVKARD... | Pathway: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2.
Function: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Ca... |
Q5TNL1 | MDTKTALPWVIIVAAGLFLRAAISLHSYSGQNQPPKYGDYEAQRHWQEVTVNLPVSDWYRNTTDNDPLYWGLDYPPLSAYHSYLVGLWARRWHNESYVALYESRGISTDQHKQFMRNTVLLLDVLLYLPAILYATYTVRKRLANDRSEVAEWASLTLAVLFPGQILIDNGHFQYNNASLGLCALAVVALLERKTLAGAVLFCLALNYKQMELYHALPFFFYLLRDCFTGSDKSSTVLERLTAGVSRLAVLGVTVLATFLVLWLPWLSSLEAAGQLVHRIFPVARGVFEDKVSNVWCMVNVLVKLRNFPNTTMALVCLLCT... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 534
Sequence Mass (Da): 59631
Location Topology: Multi-pass membrane protein
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A0A399YSF9 | MSDALDATPEHLQPDDYRSGVVAVVGRPNVGKSTLINAILGQKIAAVSPKPQTTRKTQFGIYTTDAVQILFVDTPGIHLPRHKLGEYMVQVATQALKDADVILWVIDTTEAPGKGEQAIAEMIASVQTPVMLALNKVDTLAPDADLSAHLALTPHVEAHRISALTGEGVAALVESLAARMPPGPQYYPEDQVTEVNLRAIASEVVREKVMSNTEEEIPHATAVEVTEYRERPDGTHYISATIYVERLSQKGIIIGQKGQMIKKIGTEARQDLIAIVDGPVYLDLHVSVLKNWRSDPRAMQRFGYRVQRDKE | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Subcellular Location: Cytoplasm
Sequence Length: 311
Sequence Mass (Da): 34083
Location To... |
A0A2N5VZA2 | MSIPPFFNRGTGTTSTLTGKGRLSSRDPDRAVRETDLDAAAARVSAISKNYLHDRFAGLLTRPSHAGEGSTLRPPWVNIGTHHRTYVIDSLTERFMVGGQGAKKKQVLSLGAGSDSRFWRLRERYCTTGEAWPVGRWVETDLQMTVGQKIRSVLANDSLRALCGPQLAVSPGPELPVGAPAPYIDLPSDPTDLYADNYCLLSADLRRPAELIDKLQSVPPTGSSKDPLLDPAAPTLIIAELLFLYLSPSHTAACLAALTAFFKGPLMIITYEALDLGDSFSRMMVQNLAGRGLSLAGFECNRSVASQIARLEEHGFTEIV... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl es... |
A0A358QMU1 | MPSPTKSSGKVGIHVNDLFGGVCRAPAPDLTGGVGPLDPEGRSGAGGILAADLTRRSVCVLQVVLIAAQVVLAILVILGILLQTPKATGLGGVIGGGGDSGGGYRRRRGLEAGLLRASAVFIALFVIVAAINVWINNTA | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 139
Sequence Mass (Da): 13905
Location Topology: Multi-pass membrane protein
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A0A510DWG4 | MEPEFFNSIAEKWQKIWEEKGVFRADPSNDRSNKKFITVPFPYTNSPMHIGHGRTYISADVYARYLRMKGYNVLFPFAFQFTGTPILSVADAIRKGDTELIESFSTIYNIPKEKIQEMKDPFKLAEYFKSEMEKTAKKLGLSIDWRRTFDTTDENFQRFIQWQFEKLRKGGYLVSGSDVVGFCPVDNFPVGMHDTKGDVEPEIEDMDVIFFDGESFLFPVATSRPETVFGAVGIAIADEEYVVVEETENSKHKSYVVSRKVFGKLSYQKSLKEVRSISPEELVKLKARNPLTGRDVKIVKGRMVNPSFGTGLVMLVPAHD... | Catalytic Activity: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
EC: 6.1.1.4
Subcellular Location: Cytoplasm
Sequence Length: 945
Sequence Mass (Da): 108925
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Q7QBF1 | MALIIRSIYSGYSYLVDKTDERVVELPLLRSVWTVPLITGAYLYFVLDLGPKLMANRKPFEMRRFLCAYNLAQVAANVWTFAMGVRYLRTYNFSFVCQPLRLDRSDQSMDEMHLAYAYFLLKILDLADTVFFVLRKKQSHVTFLHVYHHTIMALSASLFLRYLSGGHCFMLGMLNTFVHAVMYFYFFLTIYRPEAVRGASWKRYVTLLQMAQFAYNVLHFFRPIVLGVDCGYPRAVMWFVGMQNIFMLLMFSDFYRRAYLRTPKAAAHAN | 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: 270
Sequence Mass (Da): 31707
Location Topology: Multi-pass membrane protein
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A0A520XX50 | MPTFRPDLVDIPVYRPGRTPGEVRREYGLESIVKLASNECPYEPFPPVTEAIGRAASAINRYPDNGTREVRSAVAAFLEVSPDQLWFGGGSNELIYVTALAVGGPGTSAVYAAPSFGLYRIATRLAMAEGVEVPLDEDDRHDLDAILAAIRPDTTVVYVCNPNNPTGTHVSAAQVEAFVEAVPERVLVVVDEAYFEFPTAPDFASALPLVADRDNVVVARTFSKAYGLAGLRAGFFIGPAPTLEELRRIQLPFSVSTLAQVAAIEAVKHQDLVQERTSANRRGLEAITAGLATRGIDFADSQTNFVYVRPPMDATGCFEA... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9.
EC: 2.6.1.9
Catalytic Activity: 2-oxoglutarate + L-histidinol phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate
Sequence Length: 357
Sequence Mass (Da): 38574
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A0A0A9XLA5 | MATDELISESDKPIVMRALLLRHRHVQESESRGFRFNVRRNTSSYSSLQNLNEEARKRSLIPAASAVDTTKTNLLSPPNLFNHTAVDIKEETYLSSTEDLARKVHKESILKRIPIGAEATTVLVGAVEFLEQPTIAFVRLAEGIHIPSITEVPIPVRFMFICLGPSSADLDYHEIGRSISTLMSNPEFHGIAYRAEGRKELLSAINEFLDSSIVLPPGNWDRNSLLPFEDLKAKSDAIRRRQSRVALPKITADQKALLPEVIDEIIHVPVLGPVVRLKRHGDGDGWKKKDDPLRRTKIPFGGLYNDIKRRFPHYLSDFRD... | Catalytic Activity: chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out)
Subcellular Location: Cell membrane
Sequence Length: 674
Sequence Mass (Da): 74826
Location Topology: Multi-pass membrane protein
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A0A7D9DX79 | MAENFQGSAQNELILSRSFPCQLIKWKASVDQKVSKGSILAVYKKISGEVSNKSEIVVLPKLKSHVGGSVKRLLVAEGEHVKPGQAVILLDVCEHKTVMKEMCAECGADLRQEPGIPGQLKEPVSASVALVHNIPELRVSQKEAEILATKDKVTLLRNGKLVLLVDLDQTLIHTTTENVHPDMKDVYHFQLPGQNCWYHTKFRPGWRKFLEDMSKCFELHIFTMGSRMYAHTIARMLDPSGVLFADRIRSRDESFDMFSKYRDLRALFPCDDSMVCIIDDREDIWDCAPNLVTVKPYRFFTGTGDIHAPPGSEQAFTHPP... | Function: This promotes the activity of RNA polymerase II.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 818
Sequence Mass (Da): 91156
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A0A0A8J7R6 | MNVNNCAKIVPVIIAGGVGSRLWPMSREEHPKQFLPLLHDSLSLLQQTLSRVNNKHFDAPLVICNEEHRFLVAQQLKELNLLNNNIILEPCSRNTAPAITLAALSLKNKDCIMLVLAADHFIGDGDYFLNFIKKASTAIDDQSLITFGITPSHPETGYGYIKKGKSISDDVFMVDKFVEKPNKEKAEEYIAEKLYLWNSGMFMFKPMAYLRELKKYHPNIYDVCSSSIDSIVSDMDFRRIDKTIFESCANESVDYAVMENSSHVKVLQFDSQWSDVGAWGALWEISDKDTHGNCISGDVFLNDSKNCYIKSDGVFTSAIG... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Length: 469
Sequence Mass (Da): 53048
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A0A090IEM6 | MASLHFKFAAMNSGKSTQLIQAHFNYIERGMYPLAMTPECDSRYGKGVIGARVGLKLEVDVFEKETNLFTTISTRLENQKIDVFIIDEGQFLSREQVYQLANVVDQLNIPVIVYGLKTDFKLEMFEGSYHLMCLADKVEELKTVCWCGNKAHMNARVSDSGVVLREGEQVEIGGNERYVSLCRKHFMNGNASR | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
EC: 2.7.1.21
Subcellular Location: Cytoplasm
Sequence Length: 193
Sequence Mass (Da): 21872
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Q7Q862 | MSNYVERMSVQYHNFSQGADPLIDSWPLMQTPTPILTISGLYLLFVLWIGPRWMEHRKPIELRRTLIVYNAAQVIISTAFCLTPFFTGLFGQYMSMSCGEPMTGISKELQLSVWNGAWMYLLLKIIELLDTVFFVLRKKQNQVSFLHVYHHTIMVLFTWFYLKYIPGTQAAFIGVLNSFVHIFMYTYYLLAALGPQSPKEKKLWDQKYLFWKRHLTTLQLLQFGIMLCYFVLINSMQCQVPRALTYFFVSNITIFLFLFINFYRQAYRKRPATVKAD | 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: 277
Sequence Mass (Da): 32687
Location Topology: Multi-pass membrane protein
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F6ZX71 | MTVTLDFEESLTDSPRTRAAMEEVECEVSDLESRLEKLVKLSSHMNDGGRQYCSSSRHFVEALRDLSHHSQKDSMLSECLERFSDGLSKIIDSHVELLENIQFSFKQRLLHLLKEDLRSFRDSRKDMERCREGLESALHHNAETARRKAQEAQDAASAVQGSRKAFRDRALEYALQINVIQGKKKFDILQFMLQLMDAQASSLAQSHHAMQALDQYRNELAAQVHRSVLEAAREQRDMEQKVTLIKAKDPSDEDSVLQGDGAQVVIEGYLFKRASNTFKTWSRRWFSIQNNQLVYQKKVDVLTVVIVDLRLCAVKLCPEA... | Function: GTPase-activating protein for the ADP ribosylation factor family.
Subcellular Location: Endosome membrane
Sequence Length: 783
Domain: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisph... |
A0A3B9VER6 | MYESGMVVVDGLFISNSYLLTGKDFQNLLLWKPRVGEAYTVCNAERKFFRARVTKLKSDKAEIFVFEGPCESVESDLTITLLQAIPEKERMELIIQKVTELGVSSIIPFKSKCSISIEERDAKQKKSHKWGEIALKAAKQCRRASIPQVHPYCNFADAVHATAQCDLKILFWENEKDTDLKKTILNVKDLGLNNIAVMIGPEGGFEDAEITGAREAGFITVGIGQRILRTETAAIVTVGLIQYELGNLG | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A6L7M9X6 | MGLPTEDRKVHSIVAANQNQYWFNPQMRGFAEECGVFGVYGPGHDVARRTYFGLYTLQHRGQESSGIVVSDGKRLKLHKRMGLVSQVYDNQSLSELRGDLAIGHNRYSTTGSNRIENAQPIVTETEFGPLAIVHNGNLTNTDELRQQLLAQNKTILGTSDTEVILAVVASAPGSDPVQKIVNGISQLQGSFALIFLTADRLIAVRDKLGNRPLCLGRSDDTILIASESCAFAALEANFERDILAGEVVVIDAEGVSTISRDHMAPPALCLFEYIYFARPDSDIEGVNLYRARLAMGRALARQAPVDADLVIGIPDSATAA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2.
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
EC: 2.4... |
A0A376YED8 | MPAIGELRQPVWPAEVYGSISHCGTTALAVVSRQPIGIDIEEIFSVQTARELTDNIITPAEHERLADCGLAFSLALTLAFSAKESAFKASEIQTDAGFLDYQIISWNKQQVIIHRENEMFAVHWQIKEKIVITLCQHD | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provi... |
A0A1W6S4L2 | MYVPLLRPSLFMCCSFRYARILIGFCRFLTAIAIYSSIWVAPSDSQQGENYRIIYVHVPAAWMSSLIHIAMAISSVLFSLTKHPLFQLFSETGAKIGASFTLFTLVTGGFWGKPMWGTFRVWDARPTPASILFFIHLGALRFQEFPADVASISTCIGLINIPIIKFSVNWWNTLHQPSSISQFGTPIHISMPIPIFSIFASFLFSTGILFISETRQIILSFHFQRKSQ | Function: May be involved in the export of heme to the mitochondrion for the biogenesis of c-type cytochromes.
Subcellular Location: Membrane
Sequence Length: 228
Sequence Mass (Da): 25787
Location Topology: Multi-pass membrane protein
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Q7PK15 | MECFSKVIVLYQILALQWFSPKRYRTFDCESLFFITLNFCIITGLFCWIYQHQSLVIYSDNALGYVVDFLKFLLMVFTYYSLFLESGYQRGVLYKVWDELERLHNIFPSAKWALQPQAHLRTVALFVVYMSWWELTYAYWITKSARSSNFTILFWVLFLLLHLRQLQILLYTNVLGFCLKAINSELAWTIELSNGASRYGGRRSDGQICGYLRKLMEGFARVERLLELLNQAFGYSLAIIKLINNIYILTDTYWIVHGFMSGKVFDSVYLECCLSSKFICLMINLHSNERILSEFHRTRVLLHCIHLRWQLRCDQGWQMV... | Function: Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Location: Cell membrane
Sequence Length: 367
Sequence Mass (Da): 43337
Location Topology: Multi-pass membrane protein
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A0A162SWJ6 | MKPLQSRLLISFLAITLSMTVMNAIVIRIVATNHFRSFLNGQTRHTEIITMLVRHLTIALSQTLISMAIVIVILTFAISWWLSKRLTYPLRTLIEQAEALAKGHFFHNSNPSNSHNEITYLSSTLNHMSQQLAQQANLRERLIQDVSHELRTPLTALKASLAAIIDGVWMPTPERFALLMAEVTRFEKMVLDLERSMIQTQPTMRAKVPVNISNCLHLAIEHVKAIIEEKKIIFHVGILPVDQYVLTDADQLLQVFVNLLDNAYKYTLPHHSIEVKVEVTSRDIKTTIRDTGIGIPMKDLPYICERFYRVESSRDRKTGG... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 366
Sequence Mass (Da): 41201
Location Topology: Multi-pass membrane protein
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A0A6S7GN33 | MMCIIRIFVALLAVINGLDGKAVDTAVNHQKKGLYFGLMISCETGRSSIDYLDYGCFCGLGGAGTPVDDLDKCCSRHDQCYSDLLTNNICQLSLSTYSITYKYHECSKCAQPDEYSWWDSLGYETVACRKALCECDAVAARCFKKAKFNDLFKHYDQAKC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
EC: 3.1.1.4
Subcellular Location: Secreted
Sequence Length: 160
Sequence Mass (Da): 17890
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A0A7D9I203 | MKLPRFLFYLFLFVIILVLLNVLLMFYLTHSRIYALNDYEKFDFDYKVNEDSFLSIHDLPEDTSGEYYVHKNFIRSQSTDSSRDIVLASHCTGDHLHHLVSLTQVWQGPLSIAVFIPGYNLENTLSTLYILYGCFIKVRRQVTIHLVHPISVVLNDSDLMFLIRKSEEVHTKCSKALKEIKNTNKNVGINYDRKIEYPNNLLRNTAKQGVASQYSLVVDIDMKPNQNLYTDFMNFARKNNLFDGGNSFYNDKSVFVLPAFEINSKKTDDMPKDKSQLISLLDNGAVRPFYYDICWKCQRPTDYEKWRSLAGEDMDVGYEI... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-[beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(... |
A0A523JCR2 | MGRAGELVLLVLAAGKGTRMRSRQPKMLHPVCGRPMLLHVTALGRGLGAKRCIVVLGSGQEELRGALAHEPVEIVVQSEQLGTGHALLQAREALQGHRGPVLIVHGDQPLYRTSTLETLLDVFRSRSADLALLVGELPDPTGYGRILRGPDGRIDRIVEETEASPEVRALREVNLGIYVAEAAFLFKTLSRVADRNEKREYFLTDIVELALEAGHRVETASLEDLSEGLGVNDRADLARAEAVLRRRIAEHWMTQGVTLVDPERTYLDADIEIGPDSVLEPGCRLRAGTRIGAGCRIEPNVVIDASSIGDNVLIKPHCFI... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl c... |
A0A6N9GWK3 | MQEPTTLPSDGSPPSNLDAEVSIIGSLLIDGDAILRIEPFLRPEHFYGEQNAEIYTACRELFMESVGIDQETVRDRLIAKDILEDVGGDAYLSAAVAATPHSVHIVDYAHLVHNAYVIRQLGQAGIQINEIGSNYSNTRDVDRAVKAAEEIIFRIGQTYESADFLPIRDARSIIEFFDPPTVDDTDESNQPIATGFESLDRVLGGFHRSDMIVLAARPGFGKSTLALNVGLNAAKNGKTVGIFSLEMGIDQVAHRMAAAHARINIQNVRNDHLTAAERDRLSDAYGYLSDMRIYVDDAALQTASALSAKARRLKLQAGLD... | Function: Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity.
EC: 3.6.4.12
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 464
Sequence Mass (Da): 51363
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A0A7D9DKM5 | MTSGRNLKCCSNLFCAVLFLKTCVVITTVYVLFNFHFNREKRHFSVQPLARSLTNWTRGYLDRYFERSTSKNSTGIPSKSHKKVLVLVGFNATKKRRVRKRNKRKDGKKRAIIFVGIISAPQLIFRRNALRRSWLKQCKRKGIPCLFFTDSQDMYGNKLPDHINVPLQQEQLLHGDLIQTQSPGGINFARRYLWILNWANARYKFEYFLRVDDDYFVCMDRLLLELPHRSREKLYWGHVHCSPAGGIRVDEGFVIVSNDLAQTFLREQNKTLMCHAYGDQAMAMWINNIPGVTYFGDRRVHHAVAARDHILQYYDDICGN... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 398
Sequence Mass (Da): 46476
Location Topology: Single-pass type II membrane protein
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A0A6S7FBY1 | MGKKNRSNKDAKAKRSKPEEDAIVSSLLEKTSSLLATNAKEQWNEHVAIRELLDKIQKIQVQTEKDEKQKRSDFLPKFSEWLKENGADSENVEVYSSSDYDCGVRAVTTFQAGEKIFNIPRKLILTSEHSSSTFLGSIIETDKLLRVMPNVVLALKLLNESHEEDSFWKPYIDILPRKFSTPLFFTQEELSALQGSQVLNNVLNLYRSIARQYAYLHQIFKKIPTNNKLNFMKSFTYSQYRWAVSIVMTRQNQIPCSSGNGLHLALIPFLDMCNHCEGHFTTDYDLSTDSCVCFALYSYKPGDQVFIFYGPRSNSDFFVH... | Catalytic Activity: L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine
EC: 2.1.1.85
Subcellular Location: Cytoplasm
Sequence Length: 503
Sequence Mass (Da): 57722
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A0A6N6L5T5 | MQEDNKLSRRQFLKILAVAGGAGVVAKLGFDAISRLEKVSETRLLMGTIVNLTVIAPSQTQAQTALDGTFAEMQRLIATFDHRQVDSPVAVLNSTGKLIDASAEMLAVTAEALHVAEMTQGAFDITVKPLLDAYQAGRAPTQKEMDRVDYRGVLIKGKTIEVAQPGMEITFDGIAKGYIVDQGVAVLAEHGFHDVIVEAGGDLRVAGAGENGDAWRIGINDPRPTQEQMLETIAMAPGAVATSGDYIHVFTTDKSLHHIIDPHLGASPPELASVSVIACSAMLADALSTALMVMGPEAGIELVETLPTVEAMTVSKEKHT... | Cofactor: Magnesium. Can also use manganese.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Sequence Length: 330
Sequence Mass (Da): 34928
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A0A6S7FXW2 | MQLFYRFLHFLVTLIFSLLISFRYYFKLTRRKIRGVFYRTSECDIKNGVATLRSLPRHLTFIVMEKDVDLCILARLVVWSITAGISYISIQTSEGDLDKRKTEFYGEVYQIRQEMSTCDYELHFTDKDSAEQNGVNGAAHKSLRKVHVNILSYHEGKEDVTKAAQTFCTKVKNKEAQSKIMNIEHLSNLLEVNKDFPDPELAITFGPVDSICAYPPWQIRLTEFISIPSLQVMDHTLFLQTLQQYNKCEQRLGR | Pathway: Protein modification; protein glycosylation.
EC: 2.5.1.87
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Sequence Length: 254
Sequence Mass (Da): 29564
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A0A803J315 | MPLQLNSTSWILLCLLLQCLADNPGVKIQITQNGLYYGAEYLISQISSVSLSDITGSVTIASQSMDYSLTQVKMVSFQYSNSSANFIPEKGFQISIYGGNSTVNGTWQLDSSIMQDSGLSILTLKGISATVTLGMRQSNKNMVSIFLISCQSEINGIDFRVEGGVDYVYDAVKGPMENIIRSKVNEMLCSALRLQISDWDQSLSAFLSNMSLSSGLDLSLTKDPIFSKQYAEMDVKGGSDTNISMAGGHPSAPMTFSKLPDSMVQVCISEFSLNVAIRASFAANVFTNLFSGFTSFRNIRTSDLSDFLPEISQHFPEPSP... | Function: The cytotoxic action of BPI is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope.
Subcellular Location: Secrete... |
A0A6I8R6U1 | MARTSLQVCALLLAISGMTCILVSTVSTRWRVSSTAGTIITATSIFEGLWMNCIATSSGSVQCKRFSSMFSLAIHIQVCRALMIISLVLGLMSCIVSIFGLKCTKFGTSNEQTKGKIALSGGLIFILAGLLTLTAVSWYAAMITAQFFDPLYLGTKYELGSALYIGWAASLLSILGGSFLCCSFKKKKPATKAGAYKYNYQDPDSDFKQFKERKETSVASKAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 224
Sequence Mass (Da): 24217
Location Topology: Multi-pass membrane protein
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A0A6L7JH07 | MYPWLSARPRIRSRGPRGRNGDGTPRAPDSCHDGPREERVGPIDSLQLKSPAKINLGLEVLRKRTDSFHDLSSIMLAIDLCDEVRVRPVDDPENSEQHDEFSHSGLTEQALNAYCSSVRVKTKPNASVKKTIPIAAGLGGGSSNAAVVLSAANHLSGRALSDSELADVASHVGSDVPFFLSGGCALVAGRGDIRKRDLPIPKVWIVLANPGVELSTPDVFRELDSSEFTSGARTRVLAASLATEKPRWDHLHNGLQAAAERLCPQIRETLAALRAHTPWTLLSGSGATCFGIFEGEESSLAAEKDLTLAGYWTWAGRPMG... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A7DT64 | MQSASKLIYRGKLLGSLPTVGEIHKEIAVSEETVTWISLQRDIIANILLGKDPRLLVIVGPCSIHDVQAAVDYAKRLFVLQNKYLSKMYIVMRTYFEKPRTRKGWKGIMHDPDLNGSYDVEKGIRYARQCLSSITTMRVATATEFLDPFLTPYIADLICWGAIGARTTESQTHRQLASGLHCPVGFKNSTDGNINLAIDAIIAAREQHIVYMTSLTNSISTLLTDGNPHGHLILRGGREPNYGLSDITKAVKLMHDEGINHRLIIDCSHGNSGKVAKRQISVARQVIDNRKKIPGYVAGIMVESFLQDGKQSDSFPLEYG... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 1/7.
Function: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
EC: 2.... |
A0A853T408 | MQRIGFSGTLDPITNGHMWVIGEARSLADEVIVFLSQNPAKRPQFPAEDRKRIIEQSARECGWDNVQVVIVKGDYTARAAKKHGCDYLIRGIRTTADFDYENLIQQTNVDVLQGAKTIFVMPPRDLGSVSSSFVKALEGPVGWNWTMKKFVPGPAYQAWILDCLRKEWEALWHYATASQADIALADHWFAHLTGPQAYGGADRHYHNLDHLVHGLSEIRVWADNTYTPKRDSALVKKAFWFHDAVYSHDDDALYSSEEASAQLWLASGLDAGDNQDVAQLIRATDHFQGPGISHALKDAMLSADLAILGQDEEVYQAYTQ... | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5.
Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
... |
A0A2E7URL2 | MPTIADILQKTEDWFRTRGVPSARRQAQATVGFAIGVEPLQLVLQHDKPLSDAELEQIRAIVKRRGAREPWAYIEGSAGFHAFDFVVRAGVLCPRPDTETLVDAALALIPESADPVYVADVGSGTGCVGLSIAGSRSGVRLYATDVSDIALDVTRENVAALDLSQRVAVLSGPLLEPIPPSRPIDIVVSNPPYIPSAHIDTLMPEVRDYEPRLALDGGADGLDVYRALIPTAARRARKAVLVEIGHDQAEAVTALFRDAGLHHVQVHKDLGGRDRVISGHVHPVDQPAPDTAASADGDHQPARVFY | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release... |
A0A534YIR0 | MPGPTVRHDFPILSRTVHGQRPLVYLDNAATSQKPKPVLEAMASYYERSNANVHRGIHLLAEEATEELESARTVAALFIGARSEHGIVFTKGTTEAINLVAEGWAAHKLKPGDEIVVTALEHHANLLPWQRAAARSGATLRAIPATPSGELDPDFVFGPRTRLLAFSHVSNAVGTLLPVARLVKAAKEHGAVVVLDAAQSVPHLKLDVHALGCDFVAFSAHKALGPTGIGVLWGTPDRLAETEPLILGGGMVREATLGSATFLDPPRRFEGGTPPIAEAVGLRVALEYLTRIGMDRVQAHDRALVRTALDRLRQIPDLTI... | Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
EC: 2.8.1.7
Catalytic Activity: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
Sequence Length: 404
Sequence Mass (Da): 43507
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Q5TR92 | MDLRASAESGHNNELTMTEERKITSTPVMEFYRDKCVLITGGTGFIGRLLIEKLLRINVRQIILLSRPKKGKTTQQRCDDLFSSIVFMNLKKDCPTFIERVKLVDADLQHPSLGLSDESIEYIVNNAQIVLHAASDVRFDQALKKAIEVNVRGTRDLLRIAEKIVNLELFVYISTAYSNCPQGLIKEQFYTPPSEPEKMIQLVEAMDERFEEHMNKTVNDFIHPWPNTYVYTKALTEDVVRQYGELLPIAVVRPSIVIATNEEPIGGWTDNIYGLNGVIAGVALGIIRIMHVDDNNKADIIPADIVVNTVLAAGWQTYVE... | 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: 545
Sequence Mass (Da): 63059
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A0A162SUZ5 | MARAWERPVGTRDFFGDAMRQRNQIIHAIRNTAKTFDYDEIETPMLEYSQTFQFGLLRDDEERLFRTFDPAGHTLALRPEMTTPVARVAATLLAREPLPLRLMYAAKTYQTPTLRAKQTIEVTQAGFECIGDEGLEADAEVIALAVRSLQALGIQTFRIAIGHTGYVQTWFEKIPETLARGLRQAMLEKDWVQYETELKPYQSATWYDAVRSLPRVRGTRTALLQARSAATDPAGRACCDELLTLFDLLDLYGVLEYVHVDLGLVLDHDYYTGPVFEGYAEHLGQPICVGGRYDNLLGCFDRPLPATGCALFVERLMRVV... | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
Function: Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.
Subcellular Location: Cytoplasm
Sequen... |
Q7PYM6 | MRKFQRFLASVVALAVLYGVYRYSFRKDSEGNYLFLLPGEGGRSASDSEQQSSAVSSEREWSSVDPSRLANLTGFEYVIANDICKENGSFSELLGVILVTSYVGHDEIRAAHRQAISQQKLLSMGLLRIFSLASIPPTERFITQAAIEAEQRLHGDLIQGNFVEAYRNLTYKHLMSLQWATQHCRGAKYLLKMDDDIVYDPFYIQNYLSDLHQSDEARTHRHQHLLAGYVFRSKKVIRLQANKWYVSRDEFPGDIYPPYLSGWLYITNQRTARALAAESQKAGSNFFWIDDTFITGILAQRLQIQPIALNRWYSSNSEFL... | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 400
Sequence Mass (Da): 45953
Location Topology: Single-pass type II membrane protein
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A0A6L7YFK2 | MRVLGLTGGIASGKSTAAAQLKELGVVVLDADRYGHRAYEPDSPGFHAVVNEFGHDIVGEDGEIDRRILGGKVFGDPEKMERLTDIVWPEIRRLAAEEIAELREREPETVIVLEAAVMIEAGWQDLCDEVWVIATEPATAIKRLRDRNSLNAEQAQARLDSQLTNRERRRHAKIYIDNSGTQKQFRDQIDHEWMRLHRRIKQAEGRARAQARREAEARAAARAKGG | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A1U8CCL1 | MCCQFLRQLLAKESQHSTPVGRFLLPVLMGFRLLLLISSGPGVFGDDEKEFTCHLGEPGCKTVCYDVFRPLSPLRFWAFQVILMAVPSAVYVGFTLYHVIGYREEPGKENKGQESRMGHGEDVSGAASFRLLWAYVAHLGARLALEGAALGAQYHLYGFKMPGTFLCREDPCIGSITCFQSHPSEKTVLLNAMFGISVACLLFTSLELVLLGLGRFWRAYELKLPFLKNLPTAKSSVRRKDPADDLSVVETKEPL | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 255
Sequence Mass (Da): 28313
Location Topology: Multi-pass membrane prot... |
A0A2X1KBA9 | MLKEQGLTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQPDIDGALVGGASLKADAFAVIVKAAEAAKQA | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Catalytic Activity: D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate
EC: 5.3.1.1
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 14504
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A0A496ZHX0 | MKLEEIRSRIDKIDRELLVILQERMGLALRSSKFKETVSDPEREKSMLARIERMNLDLIKGSFSKQLLQTIITESKRLQKENRPLVAFQGEHGAYGEVAARRLVPEGAYIPCMEFVDVFRGVEEGALDLGVVPVENSLEGAVTQVNELLTTTRLKVIGEAKVPVNHCLLATEDTDYREIRMVYSHPQALAQCRGFLTRNKLEPRPFYDTAGAAKMLARENLKAAAAIASALSAELYNLEIIKEKIEDGPSNSTRFLLLSREANVGGGNKTSIIFATPHTAGSLYSVLRLFAETDINLTRIASMPLRSEPSNYSFFLDFEG... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Function: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate.
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
EC... |
A0A935ZQ66 | MIGWLSGTVFAREPIAGEVILDVGGVGYQIAVSLQTLAAVPECGRPCALWIHTHVREDALALFGFADPIERRAFRLLLGVPQVGPKLAIGVLGGFPLAELLAAIEGEQRTLLERIPGVGKRTAERILLDLKDKVGVLRDQLGSGRAPSQPVTPDGSSFADDARAVLVNLGWKVKDVDAALTKVDDGEQPSLDALVRRALAQLMSRP | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an ... |
A0A536M6X1 | MVRLFRRKKDEEPIGAEEDAAGVTAVTEGPVPPPEATAPEDEAAPVDQAVERTRRTWFSRIGGMFRRGLNEELWEELEETLVAADTGVTTTIKVIDDLRERVKQESIRDPEQALGVLKEDLIATLEVDTGRGQIWHSNGHRQTLPRPAIILVVGVNGTGKTTSIGKLAHAYRSQGKKLVLAAADTFRAAAIEQLKEWGQRTGVDVVAHKQGADPGAVVFDALSAAESRGADVLIIDTAGRLHTKAHLMEELMKVNRVIQRKYPEAPHEVLLVLDATTGQNAMHQAKYFTEAVGVTGVVLAKLDGTAKGGVIFSICDQLRV... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 349
Sequence Mass (Da): 38016
Location T... |
A0A3L7WEV0 | METERLHAETLAAAAASIDRAAAIIRRGGLVAFPTETVYGLGGDATNPLAVARIFEAKGRPTFDPLIVHVADRADLVRVFTTEALRDPRLTALADALWPGPLTIVAASLAEIPGLVRAGLPNVGVRIPRHETARALIRAAGVPIAAPSANRFGLLSPTRADHVLNQLDGRIDALLLGEATEVGVESSVVALAPDTPAVLLRPGGVPLEQLRELLAPYGGVEHADRRAPAPSGAALPAPGMTTAHYAPRTPLYVVVPGEVALLRTKLPHLQRVAVVGPDDAATKALAEAARAAGLTVAQSVALSPTLDHARAASRLFDLLH... | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Len... |
A0A0A9YDE2 | MSEILSPRESGVFISKNAKHVSIHEEAIPKMVHDLYLALEKGGLRKYSITEHETFPSKHLSQKEALNYVLFLDALNFCFWSPPGKPHWTVKFQDVSYTGYFALCAAVARAYDEGIHIFDPTVYSKFTLSELEEMLKGENGVPAPMVEERLKCLQEVGTVLLAKFGGSFENVVLQAKNSAQALLKLVVENFPCFDDSCDYLGKRVSFHKRAQILVGDVWGLYYGQGISEFRDVDTITMFADYRVPQVLVAYGILQYSDELMGVLRKNEILQSGCEFEIEIRGCSIRAVDLVVQAMREYMRKDDRVYYSECNDISVDNYLWS... | Function: Catalyzes the hydrolysis of queuosine 5'-phosphate, releasing the nucleobase queuine (q). Is required for salvage of queuine from exogenous queuosine (Q) that is imported and then converted to queuosine 5'-phosphate intracellularly.
EC: 3.2.2.-
Catalytic Activity: H2O + queuosine 5'-phosphate = D-ribose 5-pho... |
Q8VQ48 | MSDKSFIAVVMAGGTGSRLWPLSRELYPKQFLKIGGELSLLQSTLNRLSKLSFDAPLVITNDNHRFIVAEQLRQMNQLSGNIILEPCGKNTAPAIALAAFSALKRDKNKDPILLVLAADHIIKNEEAFCEAIKSAMFMAEEDKIVTFGIIPTYAETGYGYINIGARVESNIEVDNAHFYVAKKFVEKPERELAEKYFSSKKYLWNSGMFMFKASVFLSELKKYRPDIFEVCEEAISASSKDLDFIRLPERMFEKCPSESIDFAVMENTKRCVVCPVDIGWSDVGSWQSLWELSDKSPSGDVCKGDTLTYNTKNNYIYSDS... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Length: 485
Sequence Mass (Da): 54622
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A0A8T7EAF1 | MNKFFGFLIILFLLAMTVCGVGSSLDGLFLIHGGSMEPTFPQDTILGIDNEAYSTSLPQRGDIILFDPPHNPNDDVLLLKRVIGLPGETVEVWAEGVFVNGTLLNEPYNYAK | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 112
Sequence Mass (Da): 12271
Location Topology: Single-pass type II membrane protein
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A0A350IUE7 | MRRRQAGRLGVVFALIGVVVVLVAAAAATLLFGRVELEAAGSGSPVVITVRSGESLSQLADALESQGVIKSAFWFSAYARLRGVHLHAGNYQVDSAMEASEVIDVLEGAPYCPPVSFVIPEGFTVAQIASRVAATKGLDVTRQEYLDAVAQDSYDAPFLSIRPAGDTSLEGFLFPATYSVPDCATAHQVVQEQLDGFRSNVVPDLPSSGSQAYADLITASIVQAEGVSSSFANISSVVHNRLAIGMNLQIDAIVMYGLHQSGLAMSAADEATDTPYNSYLHPGLPPTPIDNPGLATVQAAVHPASTPYLFYVSACGQTYY... | Function: Functions as a peptidoglycan terminase that cleaves nascent peptidoglycan strands endolytically to terminate their elongation.
EC: 4.2.2.-
Subcellular Location: Cell membrane
Sequence Length: 340
Sequence Mass (Da): 35917
Location Topology: Single-pass membrane protein
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A0A6I8R1Y3 | MHGFQAGMNITIVQAISSLKKYPLPLNSGKEAKILQNFGDSICKMLDDRLEKHYAECGPNIPIHTVPSSSSTLRKAQRQPKAPSPLSIPHALEPPEQESQDLSPSKKKKTGGKKQREYVPQRRSGGYAVLLTLYRDTKSPSSRGYMTKAELQKEAQPLCDKSFTLTDPNSKYTAWTSVSTLIQKELVIKTHSPARYSLTEKGLELAQRLEEAEDQGRADGFPRQVQASSNEEEEQEEAESETNPYIHADPVQCPDQQLNLAYSHNAKNTSSDPPSVQYNHVPEFTLHPGDFNILLCVDFIETTGGAAHRKQELVTELRRN... | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of st... |
A0A661WGM3 | MTEFILASKSPRRKILLRNLIDPFIVVNSEVEEQEIPGEKPPELVKRLAKEKALQGAANLSPNSLNNALVIGADTIVVDGEEVLGKPLDQADAARILEQLKGKTHQVLSGIALYDLSSGEIRTSLVCTEVEMREYTEDEIQEYIASGDPLDKAGAYGIQNRDFNPAPQFYGCFANVMGLPLCHLAVLMKEMGIDTDHRVAERCQESIEYQCPVYNDILAGVKRNNPESN | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + UTP = diphosphate + H(+) + UMP
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Seque... |
A0A3B9MCE9 | MSTPAQRMVAEQLLPNGVSDPRVIEVMSEIPREEFLSSRVRRHAYENRALAIDCGQTISQPLVVALMTQALAPKAEDHALEVGTGSGYQAAVLSRLVRHVITLELEPSLAEHASATLSRLGYSNVEVAVADGTFGWPAYAPYDIILVAAASPDVPPALVDQLAPDGRLVIPLGRSSDEHQDLRVYQRRGEVMAWRSLFPVRFVPLR | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
A0A6B1A640 | MSTQTSVSDNETIVARDRVELLRAEILRHNHLYHALNEPEISDADYDALFAELKSLEARYPELASADSPTQTVGAPPGRTFAVVEHRLRMLSLGNAFNAEELLAWRQRAADLLDREEWTYVSEPKIDGLAIALVYEHGRLVQAATRGDGRAGEDVTANLRAIDAVPNELSGNPPPRFEVRGEIYMPKSGFDAMNAEIAEQNERRRDEGRASLTLYANPRNAAAGSVRQKDPSVTGTRPLSIGVYQLGWCDDAVTPDTHWETLGWLSEFGFPTTPDAAHHSGIEDALAACERWTQRRDSQAFEMDGVVVKVDDLGLQADLG... | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deo... |
A0A6B1DZR4 | MTHIPVLLDETIVALMPDGVAPARLVDGTVGAGGHSQALLEAGAGRLLGCDLDAQALRIARQVLGGHSERTNLFHGSYLQMADYARELGWPAVDAILLDLGLSSLQLDDPVRGFSFRYAARLDMRFDTTSDSSAQDLVNTLPAGELARLLFHYGEERHARRIARAIVAARPVCTTRELADLIAAALPAASRRASRIHPATRSFQALRIAVNAELVAIERVIPIAVDLLRAGGRLAIISFHSLEDRIVKKAFRELAENRIAPPGMASLGERRARIRLVNRKPIIPSQAEIQRNPRSRSAKLRIAEKL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.199
Subcellular Location: Cytoplasm
Sequence Length: 306
Seque... |
Q7QA55 | MSEKINSKKSPRISKMTNRSFLWGVMAAFLTWSISIYLYWNLSNTPTNGAGGSEQRLAKAPTSATAAEDTRQLILRNQNSLIDASDERLHKKSSKWAEKGKSLFKEKYARFMHEKEKRRISHRLIDELQPMLIQPNGTDEFGMVQNSEEQFIRDIGYRKHAFNVLVSNKLGPFRPIPDTRHKLCQAQVYDKVLPVASVVMCFYNEHLETLVRSIHTVLKRTPAYLLKELILVDDCSDFEDLTVGGQLEKELAQLGTNKVRLLRNTDREGLIRSRVYGARNATGQVLIFLDSHIEVNVDWIEPLLARIKHDRTILAMPVID... | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 663
Sequence Mass (Da): 75780
Location Topology: Single-pass type II membrane protein
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A0A936PWX1 | MFPDLLTLQTPFGVQALHTYGLLLILGFFAATLVTGARMRQVGMNSDRLVPLMLIAIPSSILGARLLHFLGSTDRADFLAAPWILFDLTQGGMAFLGGAIGGVISGSLYAKRAGLNVWKMADVGAPSIMLGLSIGRLGCFAAGCCHGTACPAPVEGMITGDLFPGGQLVNVEGFPWVAMVFNKGVGVGSIIGAPVYPTQLWESLGALTLFGVLSLMWRYARRFDGQILAATMILYPPMRYTIETFRGDELRGTNLLGMFSTSQLTGLIVLTISFGLIAWRWPKGLAPETPLTTSDLDPDLDPELLKR | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,... |
A0A6B0W9T6 | MTQPIDEAMLNAARAARRERIYRLVRPLEEFGSTEAASGIVIVIAVVLAMIAANTALSSYYDDFIHYHIAVDLGFFHLDTGLQHWVNDGLMVIFFFVVGMEIKREVVAGELAGGRKVWAPIAAAAGGMVVPVLIFFAIVDDPTARQGWAIPMATDIAIAVGVITIVGARVPAGLKVLLLALAIVDDIGAIAVIAVFYTEDINLTALGITVGLLVLVYLMNRNGIEPILLYVVVGLFAWTTAHESGIHPTILGVALGIMTPLQPLYRSTVMPDLIEALMRRIRVIEQEEDVERRHHDRVGALLTLSELSDRAISPLDRIEH... | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Subcellular Location: Cell inner membrane
Sequence Length: 455
Sequence Mass (Da): 48663
Location Topology: Multi-pass membrane protein
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A0A938RB42 | MVTGQRPVLPRIFELLKMTMNPKRVVIIGGGPGGYVAAIRAAQLGAKATLIEKDKIGGTCLNHGCIPTKALLHDARMLHSLRRSSVFKILSIDPSGLLEPMMDRKKKVVEELVKGVEILLESHRVVVKKGQADLISPNQVVLFDGEDGKEILEADAIILAPGSKSKALPGLTPDGDKIITSDEALEIKKIPRELVIIGGGYIGIEFATLFNLLGSRVTVVEILENILPGLEGELVRNLRRFLERDGVKILTQSSVEGVQKNEDGLRLMVKTPQRTQEINAEKLLMAVGREPSLDLNFSKAGIETSPKGIKVNRHMETTSP... | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 498
Sequence Mass (Da): 53929
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A0A179HLJ9 | MTKIPYNRVHVRGDVLFTARGGNIHSFSLLDGSHISAWQHPDVAKVAEAMKAIADAQKAGEAEETQGQIQGTEESEPPAKRQKREGDEGAGADDAPAQKEDVVVPGDAPKEHSKKKGKGGKGNASAKKQVARVPDRPVITLLTSTTDGQHVLAVSGHDKVIWVFEHDGQGGLSLLNQRTMPKRPCAIAIAPDAQIICADKFGDVYALPLIMTERSPSSGAGRVSTSTPAKKSSEPAANTFTVHSQRNLEALENQRKQLELQRQKAAEKEEGPDFDLTLLLGHVSMLTSLVLAESDGRRYIVTSDRDEHIRVSRYIPQAHV... | 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: 546
Sequence... |
A0A4Q0DLR6 | MIRMILAINNQCFIGKNNTLMYRLKDDMLNFKKMTQNNIVVMGRKTFESLNNRGLPNRLNVVVTSKAETFEDIQTITTHDMKRSETFTKEGHVVYITPDSFINQFLPFHRDSEDEIWVIGGAQVYEAATPFASEIICTFVDDDEVGDVALKPKLFGGFTHLATLKSVDVDEDNDKPYEITQLVRHEDLEHKLRELQAQQHEMEKEQTQNNLSTPLENGGLRQGEAFVIAATTSAALSQIDTESREDSSDSDSSSSDSSSSSSD | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
EC: 1.5.1.3
Sequence Length: 263
Sequence Mass (... |
Q4H2Q1 | MLDNGLPRMQCRCIGECPDHKYNSTCDLKPNAKCFKKLYINEYGEEELRAGCLGSQDDYLNQCHNKAKTEFEDPTAVACCNNGTMCNDYLDLGLPEYYDEPSDTPVSEANSDVITVIAVTVPVFCFLFGLIIMFYYIRLCRRESLRRRQIENENKKALCPVLYGDRGDLEGHNEMMENWSSLAGTSSGSGMPLLVQRTISRQIEILHEIGKGRYGTVMLGKWREEKVALKIFNSSDEESWFRETEIYQTVLLRHDNILGFIAADISGAGSWTQLFLITEYHKHGSLYYYLQNRAINIAEALKLAYTACCGLAHLHTEIAG... | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 531
Sequence Mass (Da): 60307
Location Topology: Single-pass type I membrane protein
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Q7Q823 | MKSFTLLICYGLFVLHAARGDEWNYPTPGTNGVMSEPERWGGQCDNGRRQSPIDLTIAAAVRGQFAPLFFSNYMLPLKQPRVTNTGHSIQINNRDSAITMQGGGLGGRFVLDQMHFHWGSEHTLDDTRYGLELHLVHHDTRYASLEDAVQARNGVAVLGVLFHVGSQPNMHIDTILDTATEIQNEVGKEALLRGKLSPYNLLPSNRTSFYRYEGSLTTPACAESVIWTVFTESISVSLEQVERFKAIHDQTGRELVNNFRSVQPLNTRALVYATEWDQQGNNFATKMTSNVVFLGAIVLLVITSRLSYH | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 309
Sequence Mass (Da): 34543
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A0A1B2I4J7 | MAPKIGIIMGSASDIPVVEKGTPVLEELGIEFEVAIASAHRTPADVENYAKGARKRGIKALVAVAGLSAALPGVVAAATTLPVIGVPVKGGAMDGLDALLSIAQMPPGVPAASVGLNGAKNACLLAARIVAATDDELTAKLEAYAEKEASKVRESRKKLENLPAAPADAY | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2.
Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucl... |
A0A8H8LYY2 | MLAARTARRFIPPRTLLTRSFASSSEDYDIVVIGGGPAGLALAAGLGSNKFTSQFKTALVEASNLNNIRTWSESPGHYSNRVSSLTNESLAFIQGSWDHVESGRTCPVEAMQVWDGVSDARIHFLPSDLTRLPTTGEVPSSMATMTENLNLQRGILKRLDELPAVELLDSVKVENIEHGPDEGSNWPIVKTSNGRSLRCRLLIGADGFNSPVRKFAGIASSGYNYDTHSVVATLFHSERPNHASLAHMTQFNSTTAFQRFLPTGPIACLPLSPIASSLVWSTTPSIAGALKATSPETLAVFINAAFRLPEPALHELYASL... | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: FAD-dependent monooxygenase required for the C5-ring hydroxylation during ubiquinone biosynthesis. Catalyzes the hydroxylation of 3-polyprenyl-4-hydroxybenzoic acid to 3-polyprenyl-4,5-dihydroxybenzoic acid. The electrons required for the hydroxylation ... |
Q7Q0V1 | MNNYIKFMEVLGNVKHLKRTGWVLRKVKDCETVSGHMYRMAMMSFFLEDSHGLDRIRVMEMSLVHDLAEGIVGDITPYCGVSREEKLLKEFSAMTEIASLLGPNKDKMLALFNEYEEGKTPEAKFVKDLDRLDMVMQAYEYEKRDSCPQKLQEFFDSTENKFFHPLVVDIVNAIKEQRAKAASTVVDNPNC | Function: Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
EC: 3.1.3.89
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyrib... |
A0A034WL87 | MDSVFEAYLGPDGVLAGAVAGAVGEPDDIPKTNTTVWVLGKRYNAIQELDLIRRDIQSRLWCTYRRGFVPLGAPQLTTDKGWGCTLRCGQMILAQALIDLHLGREWFWTPEIRDATYLKIVNRFEDSRKSYFSIHQIALMGDSEDKKVGQWFGPNTVAQVLKKLVRYDDWCSIVIHVAMDNTIVTDDIYSLCLENPSNDETWKPLLLIIPLRLGLSDINPIYVPALKICFELPGSCGMIGGRPNQALYFVGYVDDEVLYLDPHTTQRSGSVGQKTTQDEIDFDATFHQRYAGRIGFQQMDPSMAMCFLCKSRLSFEVLLD... | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoeth... |
A0A814XNU3 | MPPPTSTVSRKRTRSTNVSEDNNDHEQATSTSTIVSSQPISTAPPKRQRNNPPSTTSSVVSHTNYSLRNRSITSDTQHSSTRISSIENSQRYNLRPRHLQSQIQLPQISTSHSIGVSRRPTSTTHRQIPSTTTTTQQEQPTSSIVQPRQYRLVYISDDDDQPTTTTQSSAAIVNTTFNLVTDDEDDDLTRPQVPPRRTARSTSNTGHNTRSRTSTDPTNTTTIDNQDFSNGGVAHVRLNRAIEIVIDSIQSLEGAVNNFDQLVFRLIYGRLGTRNEFENIEGMIRLSRILNLNFPSRLTQDEIDALPKIKFIHKSESTSS... | 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: 782
Sequence Mass (Da): 88530
Location Topology: Lipid-anchor
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Q7QKD2 | MGALIWRILVLCFIASCSQLPVTVAQYLSSCKTPGGDGEPGTCVLVRECPFARALLMKQKHSNNDIRYLEAIRCGMLETKALVCCNAPNITADSSSSSASIDGLVDGETIDGLVENRFSTPEEKRGLLPEVCGVDTYRGPIRGELAQLFHFPWNVLIQHRTKDGEHRCHCGGSLISDRYVLTAARCIMGIKKTWTIVSVRVGELNLQTDPDCDDSTAGVTECASPVEDIPIEKITVPSNYTGTGSPAVKQDIALLRLARRVEFSESVAPICLPLNTSNWVGYSTEQDGSFYESGWGKTPDAAAGGDNKWNYVSVGVAREV... | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 401
Domain: The clip domain consists of 35-55 residues which are 'knitted' together usually by 3 conserved disulfide bonds forming a clip-like compact structure.
Sequence Mass (Da): 43595
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A0A1B8SYQ7 | MYKLNEQQQHELLELLCALIRHKSENPPGEEQQVAEFIYHYFKQENIDVEMQEVAPGRPNVIAHLKGSGKGKHLLFNGHIDVVPCGCGWSTEPFDPVIKDGKVFGRGAADMKSGVAAMMYAATLLKRNQDAFSGNLTLVFNVDEERINLGMLHYIKDGISADYAIIGEPTSLGVCIAHKGVSRYNLSTKGTAGHAAKTRYPDSAISKMAKILPAIEQHRTSVEEISHPLLGNASMIITTINGGTAPNIVPQHCDIEIDRRLVPGEEKQEIEARLHQAIAQYNKGEEIDYHLDNYLFIPASDIPADHELTKVALDTVSRFT... | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 3/3.
EC: 3.5.1.18
Catalytic Activity: H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate = (2S,6S)-2,6-diaminoheptanedioate + succinate
Sequence Length: 386
Sequence M... |
A0A5B0MVW2 | MFNSNQTTTTTTTTPVRRNNRNSTIGLNSQQQQQQHSLPQLPSTTTTNQQQQQQQPYYNHHHQHQHSESLDYSSAEHLPNLKSSTHSSEHHHQQQQQLTNRHAISSPKLPKSEPLQLRSYSGVLEIRMPNEPQQQQQQLPRNSLNNKSVLHQSSNLSLDKHHRSGNPLISSTGSTLKPRRRPPRVYETHPGNLVFCCRGRLISSKPSHSIPLTRRRRPKNRRRIEEEGSRVEDRAGEEVEEAEGEGESEGRRLYLPLQTLASVALLLAIPILFLYSTAPTLIHRSGFGIFLLALFCYLWMLTLSSMAKTVSSDPGILPRG... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 667
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 75697
Location Topology: Multi-pass membrane protein
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A0A1I8PBU2 | MANLSRESAILFVLAYIFLQVVYTNSYSHFRLPTSIQPEHYHLKVITHMDNTATFRYEGQISMRFRVLEATNNITMHALNLNIDNTSLVLSKVKDREFHMCLEDIDILPEFDYFIMILCQTLIKDEIYRVQMKFSSFLNTKSNGYYRSSYKDAATNETRWLSVTKFEPAFARAAFPCLDEPQYKARFTIWLGHHRSRTALSNMPREKQKPLEDVHDYVWSIFEESVPMSTYLVAYSVNDFVYKASSIEMYKLVLRTWSRQDSINKSGYVVEMAPRILKYYEDVLGIPYPLPKMDQIALPDFNKGGMENWGLVTYAEKVLY... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 925
Sequence Mass (Da): 108510
Location Topology: Lipid-anchor
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A0A7D9L162 | LSERTYSLWGYMWQNVNDFVNPLFNELKTHFLRPRTSPQYIRCWRAMYNRHENVMHSRETVTDAITSLVDQNDSIQDHISLLSKRIELMKIILDKETDNDLKIVNGPEEGVDKVGDERSEGEITTTTDNENPSCEVERELRRQGITLSELVSDNPRLSLDWQPFRGVTQCSCASPIDSLTRKYHCWNCGQVFCRRCIDYQTSLPGHYSENKVPVCKSCFKKIEKKPRTAT | EC: 3.1.3.48
Subcellular Location: Cytoplasm
Sequence Length: 230
Sequence Mass (Da): 26767
Location Topology: Peripheral membrane protein
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A0A084A2M1 | MSSQTVAAKRWFSKEWLLEQKSLIALLVLIAVVSSMSPNFFTVNNLFNILQQTSVNAIMAVGMTLVILTSGIDLSVGSLLALTGAIAASMVGLEINAVAAVAAALALGALVGAGTGFIVAKGKVQAFIATLVMMLLLRGVTMVYTNGSPINTGFTDVADAFGWFGIGRPLGVPTPIWIMAIVFIAAWYMLHHTRLGRYIYALGGNEAATRLSGINIDRVKIIVYSLCGLLAALAGVIEVARLSSAQPTAGTGYELDAIAAVVLGGTSLAGGKGRIVGTLIGALILGFLSNGLNLLGVSSYYQMIVKAVVILLAVLVDDKS... | Function: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 322
Sequence Mass (Da): 33419
Location Topology: Multi-pass membrane protein
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A0A944NEL1 | MSRIAKSTLIIAFFFGIDKILGFYRALKINQHFGLSYELDVFNVANNIPDLLSALISGGALGVALIPVLSEYIKQKGKPSAWELFSRILNFAFITTGLIAILISIFAPWLVDKIIAPGFPYEQKLLTVELLRFDLLAILIFSISGLVMAGLQANQHFLFPAMAPGFYNLGQIFGILVLAPSEGLKIGSITFPAYGLGIRGLVYGVILGAFLHLTIQVPGLIIHKFKWTPKVDLKNPGVKKVLALLGPRVITMLFIQMFFIVRDNLASGLGEGSVSALNLGWFIMQVPETLLGTAVAIAFLPTISEIFIQGDKNEFMEMVN... | 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: 516
Sequence Mass (Da): 56284
Location Topol... |
A0A6N8YRI6 | MEQQAQNAEREPSFEEALAQLRETVQTLEEGNVSLEEATRLLAQGAELARTCNDLLAKAELQVSRIRRNFQGQADKADEPDSLMASPQQDFGMFDDAPR | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular... |
A0A936U592 | MSMREAIRQVRDAAQTLNARGPKPFPVVVQGLEAVIVGGVLGVERKDWIVPGLRERVGAVLRGCPVERLADASVGARPYRVAPVSQDPANRLLHAVGLSLAERDRATLCFVGQGSASCGAFHEALNLAALHRVNLIIVAHTWNLDEPGAPLARQLAGTLASKALAFGVHATTVDGGLVTAVLSAVAEARAHGGPHLIEARLHRGDDPLRRAEEELTEHEPSAVAQTG | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2... |
A0A803JZ88 | MDLRVLYLIQLGSCLLGVGAGSNTEEEEEERPEDAHPPGHKSHHWNYQDIHQWDSDYPHCGGPEQSPINVVTSATTFDSNLRPILLSGYNVPPSRTLSLENNGHTVVLDLPDSLLIIGGLPQTYRATQLHFHWGSQDDPGSEHTVNGQRFPGEMHVVHYSAEYSSATEASTHPGGLAVLGVFIQEGEEENPAFQNLLPYLQNITEEGESIEIPGFDIRGLLPQRLDRYYHYDGSLTTPPCYQTVNWTLFNQTILLSPEQMDLLEDTIHADHDHILQNNFRAPQSLNGRLVLSSFSPKVSGRRLPGAAPNPAGTSPAPDNS... | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 392
Sequence Mass (Da): 43116
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A0A2E7UV41 | MLEPPTSPRPLRVEWLGRRPYLEVQEEMKALLLRRIAGDAPDTLLLVEHQPTFTVGRRRGAMASVKNPGEVPVVEVARGGDVTFHGPGQLTAYPICALPPHRHDLHAWMHGLEGVVDGVLARWDIKGERDERNTGVWVDGKKIAAVGIACKRWVTWHGVALNIKVNLDYYGRIDPCGMDSSLVTRMADHVSRCPTVRDTARAFSTEFRRWWMDWSKPPP | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-A... |
Q4H396 | MATSSFLAWFWNERFWLPHNTTWADLRNTEDATYAQATDLWVMIPYSIVLYIIRFIIERLIARPLGRKLNISDIPNRPPSSNAVLDKVFSSITRYPKDERLKGLCKQLDWSERQVQRWFRKKREIHRPSKLIKFSETVWRLLFYTGVLTFGIFAMHFTSPKCPWETRMCWVGYPDKQQLTLSSYWYYQTELAFYASCTITQFFDIKRKDFWVMCIHHFATILLICFSYSINMLNIGMLIMQLHDFSDVFLEASKIAKYLKHDVLATTGLVCFSLTFMLARIVYFPFWVLNSIYFDAWEVVGPFPSWYIFCVWLSLLQFLH... | Pathway: Lipid metabolism; sphingolipid metabolism.
Catalytic Activity: octadecanoyl-CoA + sphinganine = CoA + H(+) + N-(octadecanoyl)-sphinganine
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 382
Sequence Mass (Da): 44872
Location Topology: Multi-pass membrane protein
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A0A2G6NL04 | MAGLRLRKASLLRKGWQYDAVFGRGRRLRGEGYTLVVIENGQAESRLGISVHRKIRGAVRRNRIKRIVRESFRIGRSSYPQGCDIVCVIYPDFACTDPDAVTTSVKRLLACRGT | 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... |
Q5TSB4 | MFRIADFTVRWRKMMNKFTCETASISLLHVSSVKSHLLSTMKGSNVASTLDESYENAISSLNSLQSNSSVLQDSILRKHSEDNKHINDTLKYLLRIGVSMDHLNQLPVIHVSGTKGKGSTCAMIESILRSNGYRTGFFSSPHLVSVKERVRLNGMPLSSDKFRLYFWKIYKQLLAYREHSRDMPSYFCFLTILALDVFLRESVDVCVIEVGIGGRYDCTNVLPKTGTVGITSLGLEHTKLLGNTLEEIAWQKAGIIKRGSDVFSVVQPSECMEIIREECRKLKANLFVVPSELKAYQWAKKPELVNESCDILDILELNTS... | Cofactor: A monovalent cation.
Pathway: Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.
Function: Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for m... |
A0A6B1BYA7 | MSGAIQPYPWGSREVLPQIMGVPPTGEPQAELWLGAHPRAPSVLRRSGTNRPLNQVIANDPIGELGEDAAQTFGGELPFLLKILAVDQPLSLQTHPTLSQAQAGFDSEDEQGIPLDAEHRSYRDRNHKPELICALEPFTALCGLRPPDSAAALLDSLEVDALDPAISFLQAGEIAPALRWLLEQTPESGTEIAQQVAAACSKPGPFPDERLWGVRIGEQHPGDIGVAIALMLNLVRLEPGQALFLGAGNLHVYLRGAVVEIMANSDNVLRGGLTVKHVDVPALLDAVNCRPHDVLVQAPTGPCFTFEAPVPDFSLTRVEL... | Cofactor: Binds 1 zinc ion per subunit.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 378
Sequence Mass (Da): 39883
|
A0A2E5IVE0 | MTETVATAEKLEGSRVRLSVEVPVADLQAEYGRAVQRVSRRVKIPGFRPGKAPRQMVENAAGMATVMQEMLETLVPRAYTSALEETGVTPVDQPELDISDPPSLDMPFVFSAEVAVAPTVVLGDIGDVSIDVPDVSVTPEEIDQELEQLRMSQSAWDATDRVAISGDMVQTRIQISAAGLDPDEPQPYNVIVGENGFPEGFDDAVIGQSGGDKVSYEADIPADDPNETLRGKKVAFEIEIDGVSERRLPELDDEFARSVGPFDDLEALRARVSESISERKTHEAQHQIEDGAVEALVGRTTFDIAEVLVDREREQVDKDR... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A7D9HU31 | MFNQRVLVFLIVVTAVICLAYRVHLFYYSPRPVGPTTSYEVLVLPDKQRILYENKTTRLLRDLLQSSYLKIQPFKINGDDIMVFLHIQKTGGTYFGKNLVTNLHLERKCDKVVSMRSRFMCKRPNSDEFWLYARYSTGWVCGLHADWTTWNSCLPKLLKSRLSKKHFNETKLLYITILRDPVDRFLSEFKHVQRGATWLSSKFVCNNKKYKLPICYKGANWSNVSLSGFLNCPYNLAFNRQTRMLANLTEVECYIYDNKIEEFNYSQQYGKLMLESAKRNLRSMAYFGLVEYQRESQYLFEKTFGLKFKKKLTQVPGNET... | Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Catalytic Activity: 3'-phosphoadenylyl sulfate + alpha-D-glucosaminyl-[heparan sulfate](n) = 6-sulfo-alpha-D-glucosaminyl-[... |
A0A6S7FWV2 | MKQQGILLLFIVLLYNISLAFFAPLESNDNSVSVEYGGVTAEQLLAYSKHDAKYNVISNEIDSFSWPSFLKGLECDACKFITGFMQGLFRLNKTDEFIASAAIFWCEKLKIEDTRVCSGIIPEFKNEALSVFDEVGLAPKEICGLILGPSCSVVRDLYPDWNISLPNVPKPPVHPIPSPKPGSPTYTILQLSDVHIDHQYAENTSTKCGEPLCCRKYNGEGKAGYWGSYECDIPMRTFEASLKHIKDIHQHIDFVYWTGDVPPHNVWNQSRTDQLVAMESAVKLFIKYFPNTPVYPAMGNHESAPVNSFPPPYVKGHSSN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 602
Sequence Mass (Da): 69293
|
A0A520Y320 | MKRISPSGPVAGTVRLPGSKSITNRALLVAALASGESRLVGALRSDDTEAMIDSLSRLGVAVSWDGYDLIVAGSDGSLGAGDTEIDVRGSGTTARFLTAACTVRDGTVVVDGNRRMRQRPIGDLVRALGELGAAVEVLGEEDRPPVRVHGPALTGGAAILDASRSSQFASAVLMVAPCADGDTVLELREPIVSRPYIDQTLEVMRAFGAEAAWDGPTTLTVAAGGYAARDFIIEGDASAAAYPLVAAAVCGGSVRVGPLPEGSLQADLGLIPILERMGAEVRREGDDVILNGHPQTLAAVSENMNDAPDAVVALAVAALF... | 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-ph... |
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