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stringlengths 6
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stringlengths 16
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stringlengths 117
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A0A3B9NU19 | MQSTFFWYDLETTGTDPILDRIVQFAGQRTDSDLRPIGSPVNFYIKPSVDTLFHPDATLITGIDPDQIDAEGLSELAGLRKMLACFTEPGTCVVGYNNLNFDDEFVRQSLYRNFFDPYAREWQNGNSRWDLINLLRMTFALRPAGIKWPKREDGKPSFTLVKMAEANGLSHENAHDALSDIEATISLAKLVKTAQPKLFDYHFQMRKKQPVLDLLYPLGKAPVLLIQPFFDSSDRYLAPILPLIAHPSNQNSVICLDLRQDPEAYCALKGDALTDFLLPKRVEGARSKPSVVQRIQINRCPPIAPMNTLPPALAADLSWSPDALTGFVKKIQSYPGIQGALIEAMRRVPEAPVKDAEFQLYSGGFVSEVDRSRFAQAPEIASAPGQTEVFADARLNELLFTFKARHYPDSLDAAQAQRWRDFLSARWQQDARLITLYETTKARLAAQPDSVLLLKLLRRLQWQASLISLTLD | Cofactor: Binds 2 Mg(2+) ions per monomer.
EC: 3.1.11.1
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Length: 472
Sequence Mass (Da): 53130
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A0A183TKS8 | MKRRHVDLLLGVVHAAVAFYLVYLTNEVQPTAYMDEYFHEKQTHAYLAGRWSEWDSNITTPPGLYLLTAIFLKSREIFLGDNTRQDLNVTHFRYLNALHLGVNAFLVSSILSHLNRLPLPLHLLYLTSIVTLPVLFFTSFLFYTDQVSLAAVLATALAFLYKRRLTAFLLACFACSVRQTNIVWCAFLVGMSIASRLSSIRRKRGSPTEASPFSWFCVLLRSPVRVIQAVIQGIAYDAPLLTLVGGLFMAFVWWNGGVVLGDRSSHEFTFHIPQLLYFLAFCAAQTPLRFFLFLLHLSRSLCKRQRMLPLLLLLLFLTALSVASAHCCTVAHKYILADNRHYTFYVWQRLFQRYPVFRYIVTPLYALAGLYVATTFFPTVEIAVGVMTECARCRLLTLLRLAVFVVCTAACLIPSPLIECRYFIVPFVVWRLLTAPHAAAAPIAPLIAASEVLLNVAVNFITVYVFFYKPFFWDSQPSLPQRFMW | Catalytic Activity: a dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a dolichyl phosphate + alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+)
EC: 2.4.1.256
Subcellular Location: Membrane
Sequence Length: 485
Sequence Mass (Da): 55292
Location Topology: Multi-pass membrane protein
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A0A820XLV3 | MTDYELNFSLKTEEMLGRILDPAYRCLVVEMFESINVLLERNPELCFVQPLDVDYLISDAIKLFEQQTKSVDPLKDFYNLPISLVGGSTGYMTQVIINYLFSAQIQKSDVADLNSSASNSICKIS | 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: 125
Sequence Mass (Da): 14129
Location Topology: Lipid-anchor
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A0A0N4YM25 | MAAFESNLRGKERIVVFIFGGAAFSKHLSNTINEMVPGVRTTVCDHFLLDDGFCRITENPADLNIADAVLFHNADYNAALVPKPRKSNRPHVLWSLESPSNDRFRPGPNVINWTMTFRRDANIWYPYGHFRKLKSPVDVDFDEIWDMKNDSKTAVWLASNCFAKNSRTAVVDMLMKQGLHIDRFGRCGSRPPGCDGVNRQGDPCVAELVKPYKFYIALENSNCQDYVTEKFYEALISRMAVPIVLKKEIYVNVGAPKDSFIAISDFKTISDAVKYVNEVADDKEKYLAYHKWRTSYEYVNLD | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 302
Sequence Mass (Da): 34488
Location Topology: Single-pass type II membrane protein
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A0A183BAY8 | MPTLLFRFLILKNRYGQIVEVTKRPKSKWRPVALDTVELEKLATRKLRIGAKAAMQLAERLYTQGYISYPRTETNIFPADMDLASLVRVQLDDSRWSGFATRVLERGPNPRNGKSTDKAHPPIHPLKTGSNLQGNEARLYELVTRHFLACLSADAQGAETLVRLCVGKASVPANSSSSSSFSLPPTDLMTSEDGEMFESKGLVILQPNYLEVYPYDRWTEKDMPNFHLGDWILPTNIEVSNLFVFQFER | Function: Introduces a single-strand break via transesterification at a target site in duplex DNA. Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand.
EC: 5.6.2.1
Catalytic Activity: ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.
Sequence Length: 249
Sequence Mass (Da): 28207
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A0A0N4YWP2 | MEVAKKEGMRLFEGIYVMTGGPHYETPAEVAMLREMGGDAVGMSTCPEVIVAAQCGIKVFGFSVITNMANTDIDDAVVVSHEQILKVATEAGSIKVATFLLAEKTTYKVCPIRVKVASLFHSRKVVDKNPTEV | Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.1
Catalytic Activity: 2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine
Sequence Length: 133
Sequence Mass (Da): 14365
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A0A8T7AEH6 | MNFVALLLGLSVERLLTNLFHLREFRWLDPLFDWLTVKLKDQSRTGAVIGVAFSTFLIVLPVALASAMLSGTLFQVPYFLLAVLVLLFSLGPRDLKKEVDEYCAAAKEGDEVELCRVARELWEGELQHDPEIQVRLVRRAIFIQANNRIFAVVFWFLLLGPTGAWLFRVLDLMRRRLAFEYNRTEHDFCNTALVWAVRSVHGVFAWLPARVLIFTYAMAGSFDGAIAAWRAYLRKNEEESFRATNDLLDRVGDGAAGGLPDDLSATALDYPAVANYVDLAMDLVSRTLWLVWCPAIAIMTLTDLLS | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Subcellular Location: Cell membrane
Sequence Length: 306
Sequence Mass (Da): 34577
Location Topology: Multi-pass membrane protein
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A0A814ERD5 | MMSTTMEHDPASEELAAHPSRLPTHPKEMAEERKSEPEGIFSPSVLHPLDPLTANEISLTTKIIQESSYFQKYLRIVTIVLLEPEDKSIILNFQPNTEIHRRVTVFIRDPVKHVTLEMIVDLTKKTIKNVLELTNVQPGLTYDEIIAADSALRSDKNFLAAIAKRNLDVNSIVFYPFTACYRDQSDAASKRRIYRPLSAVSYGNEDNYYAHPIEGLVITVNLDDMTVEIEDHEVVPIPTNTANYNPESISTPNNVPYFPNGVRDDLKPLIITQPDGPSFKVDGYQVTWQKWRFRIGFNVREALVLHCIEYFDKARWRSIIYRAAMSEMYVPYGDASPTHSFKNVFDMGEAGLGLLVNSLVLGCDCLGEIYYFDVVVNNNQGKPVLLKNAICMHEEDAGLLWKHTEFVEGRTQVRRSRRLVISTVATIGNYEYAVYWYLQQDGILNYEVKLTGIIAPAAIESGKTPVSGGLVAPGTYGPYHQHFFNIRIDWMLDGLKNSLVEVNCEPLPPGKANPTGNAWTAKETILSTVDQARRTIESKTSRHWKIVNPSVLNHVGQPVAYKLVSMGNVFPLCQENSSQYKRGGFTRYHLWATVFDSNEMYAAGLYPNQNAGDDGLLSYSEKNKDKSLVESDLVTWYTFGCTHIVRPEDWPVMPVENTGFRLIPHGFFDGNPSLDVPLPSNHCHMKKNSEECKRNDN | 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: 697
Sequence Mass (Da): 78808
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A0A6A0H1V1 | MDESWECLSPLLHPAVAAGVKEFNFPKMTAVQAACVPNMLSHYEVVAEAVTGSGKTLAFLVPTLQIILQREYPIKKYEVYAMILSPSRELASQIHGVLQVLLKHCKEVSSLLLVGGGAVSEDVAKFESNGGHIIVGTPGRIEDIFNRCESGSTSLKLACRALEILILDEADKLLEVGFTETISTILACLPKQRRTGLFSATQTSDKVKLIRAGLRKPRRIRVMQSPQQ | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 228
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): 24944
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A0A183THC8 | MSESSRDNAKSEPGEPSSSQCPPEGNEVPSSSTSGTTGSFECNICLESAKDAVVSRCGHLFCWPCLHQWFETVRSRPSCPVCKAAISRDSVIPLYGRGGDHKTDPRSKIPPRPPGQRTEPQQGSRVS | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 127
Sequence Mass (Da): 13703
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A0A0N4Y2X2 | MALAQTIASFLGATLIGQMNTVVALDRFLATVFPIWYFQTTIRYPITVLSVAYGISVVALILNWVLVLTNPVEKYAQISSLCSFVGSTYPGFRDTLMYYRWVCIVIAAVMYIVMAVLIRKRFKITSQLFAPSMSKIQNNKIMRSHVTMALMSGRKIAAATVQNRTQTPFWVWLRNKLLAVQRQPVTPPPGLPTADGKAEYHNPLRFPKTQSARPGSAEAPSLPGGVHHLISENYYYTRDGRREVLPPKPLYKADGQHVEFATYTGDKLSRNREEELITQKEDPELSRLERFDRFAASKGPLVNMRPTPVSMGKHFGMLGKMYGEHRFALAPNEQKAFKGFLDQAFVKVFKSYVWDQWLYFVPQTVAAYLLYDWAKKRNYQVCRKNPADYANDQ | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Membrane
Sequence Length: 393
Sequence Mass (Da): 44805
Location Topology: Single-pass membrane protein
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A0A8T7D1D5 | PRGLSQAEQLPEPVFTPSTKAEEGEHDENIDFDSTVRLIGRELAEKVKSVSLQLYREAARFALERGIIIADTKFEFGTDSSGNLVLIDEVLTPDSSRFWPVDEYRTGTSPPSFDKQFVRDYLEGLAWNKQPPAPRLPADVIAQTAEKYKEGQKRLTG | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2.
EC: 6.3.2.6
Catalytic Activity: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + ATP + L-aspartate = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate
Sequence Length: 157
Sequence Mass (Da): 17627
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A0A8S9DYQ2 | MKIPPLDKAVDVIKQGGIVAYPTESVYALGCDPRKLATIHRLLDIKQRAIEKGFILIAADFEQLQPYLGPVDQTIMKKIMATWPGAVTWLMPVADNVPPSVRGNHEGIAVRVTAHPVAAALCRAADTALISTSANTAGKAPMRCAEDVGTELGSLVDYVLAGDVGDAVKPTEIRDALTDEIIRSA | 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. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 185
Sequence Mass (Da): 19697
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A0A7T4VIC1 | QHLFWFFGHPEVYILILPGFGLISHIIMQETGKKETFGSTGMIYAMISIGALGFVVWAHHMFTVGMDIDTRAYFTSATMIIAVPTGIKIFSWMATMYGTKIKFSPQMLWASGFVFLFTMGGLTGIILANSTIDIVLHDTYYVVAHFHYVLSMGAVFAIMGSFIHWFPLFTGLYMNKKWLKIQFITMFVGVNMTFFPQHF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 199
Sequence Mass (Da): 22649
Location Topology: Multi-pass membrane protein
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A0A140X397 | TTTAFSSVTHICRDVNYGWIIRYLHANGASMFFICLFIHVRRGLYYGSYTFLQSWNIGIILLFTVMPTAFMRYVLPWGQMSFWGATV | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 87
Sequence Mass (Da): 10129
Location Topology: Multi-pass membrane protein
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A0A814C3N2 | MQYLFILLNIVYGIGLLLFLNGFLLTRRTILQNSTDISSQQQFKNGSSEFNQIVLLVIDALRYDFIQPQQHTKLNPFYHNQMSHVQQLLIRHPRQARLVKLHADPPTTTLQRLKALTTGTLPTFIDFSYNFFGYEVNEDNILFQSHNNNKWNISFLGDDTWLTLYPTMFHRHHAYPSFNVYDLDTVDNGILEHLDELIKQQKSFIIAHFLGVDHCGHRYSPSHTEMSRKLRQMDMVILNITSQLKSNSLLIVVGDHGMTSSGDHGGDELNEIETAMFVYTNKQNYFTLLEDSSTTIHYSQMDFVPTLSWYLQILVPYSNLGFVINELIPEHEHLDAMKQNFNQIRLYLSKLSSVDSTLKLSNELTMLYSRLNS | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 373
Sequence Mass (Da): 43304
Location Topology: Multi-pass membrane protein
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A0A7J3HP20 | MNQRTLVNPFIPHNEEEIAEMMQTIGIKSLEELFSDIPREYIITEEPEFEGPLSEKEMINQIFRIASKNLTFPKLQLHIGQGAYLRYVPAAVKEVLRRSEFLTSYTPYQPEASQGILTALFEYQSLMAELLGLEIVNSSMYDWSTALGEACRMTIRLTGKKKILVGRYTFKQRLETLSTYIEPISGVVREIGYTPDGRLNIDELEQNLNDTAALYVEYPNSLGFITQNLDELADIVHRKGAYLITGVEPTVLGIIKSPGELGADIAVGEGQSLGLPLSFGGPSLGIFACRDDPKMLRNMPGRLIGMTEDVQGTRRCFTMVLQTREQHIKREKATSNICTNQALMAIGVAAYLALLGKKGLRELAEYIFALTDYAIKRFSELDFVKVPLAGLPHYQEFAYTVRGLAAHEVLSKLLKKGIVGGFNISEIYPEFREAIVTCFTEVHDNKSVENYVAALSEVLPK | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 461
Sequence Mass (Da): 51583
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G8YS25 | MKVITVIAQLLAITSWVDATSKQRVYRDLGTSSRVKYFHSRIPIHEANALLDPKVEGNFIGSYEVLKIGKNDHESAYLCYVPSDETTNSSEPETGIHDSYLYVEKEKELIEKGVRELPRSFSNKFCLFSNGLNGGYWTFAYCYGNKVVQFHDDTMRFMKTGKHYAENPDFVFTLGHFKKSKKKNRSKLEEDGIYLSDFTLHDEFSEPLSTNLGFANRQRYLKHTLNDGSICDITGRPRSIDVVYKCIPSSQGEAQIIDVQELKSCKYHMVVGVPSLCNIEEFSPDTFEDMSIDIDCKLIDQETKGESNTKQSDSLTTTHDDFLAHTYDKSLFLSTRNLTNDFKLNLFDFDLTYCGLGFYLGHHKTDTPYLSDYFGNRSILVFNGLYFSTEELIGKMANMLSTTIGSKISSPVTIDGKPVPLSWNDSFILWYELYDFVGYLHKLVRIQKVAATDSRIISIQVIDPATMTDQDGDFVQLQHDISAFKDSNFEAFTQALTGIMSDLDDSAEQIDDEIVSPETTVITVTEKTYITDNSAKDTKAPDPISLQHDEL | Function: Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 551
Sequence Mass (Da): 62488
Location Topology: Peripheral membrane protein
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A0A0C5BCM0 | MARATKSRRPERNETRTSENAPNPVWFKPVMFGFMLLGFAWIIVFYLSQGAYPIPLGDNNKFNMLIGFGIIFIGFLMTTRWR | Function: Involved in cell division.
Subcellular Location: Cell membrane
Sequence Length: 82
Sequence Mass (Da): 9549
Location Topology: Multi-pass membrane protein
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A0A182EU79 | DELFIMLKKPEKGPVTVLLGAQWGDEGKGKIVDYLIAKDKVQVVARCQGGNNAGHTVVANGRKYDFHILPSGIIAEKCFNIIGNGTVVNLDSFFEELNHNKITNIPGWEERLLISDRAHLVCSIHMFVDGYSEDRLNINKIGTTKKGIGPTYSNKCFRNGLRVGDLVYDFNGFSLKFRELIKYYQGQYPDLEVDIDLELSKFKKHAEKLNELALVGDTVVALDELRSSGKTVLVEGANGTML | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular Location: Cytoplasm
Catalytic Activity: GTP + IMP + L-aspartate = GDP + 2 H(+) + N(6)-(1,2-dicarboxyethyl)-AMP + phosphate
Sequence Length: 242
Sequence Mass (Da): 26936
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A0A967TX34 | YYLVLGLRYGKARHGVRERLGIYRQDLRRLLQGHKVIWVHAVSVGETRAAIPLLKALRLSYPDAQLVLSNVTETGRKIASTIKVVDHYIFFP | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP-3-deoxy-beta-D-manno-octulosonate + lipid IVA (E. coli) = alpha-Kdo-(2->6)-lipid IVA (E. coli) + CMP + H(+)
EC: 2.4.99.12
Subcellular Location: Cell membrane
Sequence Length: 92
Sequence Mass (Da): 10542
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A0A6U2NYI0 | MAVAVGFCTSSSSTQGASATEVIEILSDDDDPTDDAQPEEDDSMQLHASQMDKVKEQKSLSQTKKRDARGIFKMKPFNAFFLSGLKGYKEVKAKYFNFEKGLESKSEARRLALQEADKAWAQVALACQNFHKKRNGSYKFAFEACHDKLLEEKGKDLSKLGSTTQDAFTSSMTNCNNEIIASRLQKLCAAMGAEAELTRLRKKSGQRASLGTNDDSMSKPKRNISQQYRSVTYDRIATTIRQYPSQVDLNCIDYGYGTSHTRAKKRNDPVFRIEDYIAKPTRSSTNGVERPPLIKAGGSCFRRLIRAIIFTEGPSGANFSLLEFDNEHKEDQKLLQNEELEAVGTFSKIWGVGVTSAARFVIYGLLTIDDLRRDKEVIASMNPQQRIGLSHFEDLIPKIPRREVEELRDYVRNVVNKLSDNKVSVTACGSYRRGCESSGDIDIMLLPNEKEGAADDAALNIMIPVLDNLRKRGFLTDDLALPNAFGENDGLIPGSDALSYMGVCRLPGAARLHRRIDIKAYPGVQGPFALLYFTGDAYFNRSMRAFAKKAGLTLSDAGLAICERRQMGGKSLKIHVGNSVLCEDEREIFNVMGVNFVEPTGRICVGTEGRLHGSYGGEGIPSLEVLMGEESEESDIEENGGD | Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 642
Sequence Mass (Da): 71039
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E3M354 | MSDVPEDANAGCPGTGSAGAGKASGCAGCPNQGACATGQGPPPDADVPKIQDRFSRIKHKILILSGKGGVGKSTLTSNLARALASDPSKQVAILDVDICGPSQPRMMGVEDEEVHNSADGWTPVGIQPNLTLMSIAFLLGDKNDAVIWRGARKNGMIKQFLKDVDWGEVDYLLIDTPPGTSDEHISLVQFLLQAGTLDGALIVSTPQEVSLLDVRKEVSFCIKTKVPILGVVENMARFVCPNCAHTTLLFPTSTGGAEKMCQDSNLELLAQLPLEPALAKALDNGEDFFETNPDSTLAKSFMDLAEKVKAKLK | Cofactor: Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.
Function: Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
Subcellular Location: Cell projection
Sequence Length: 313
Sequence Mass (Da): 33101
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A0A813QEN8 | MFCMAVTLLKVLIRLKNGQYHSTEIRDKYRILDLYKQIANELHLSIEQVKLLTIYRSTADGVQVLLYPSSYGMYFDESRTLDTFSILQNEQLYIDIGELFDESTLSMSPSSTASSTSSIVINESNLSPSVTNLQHYQAKPKPQKPVFDQQQHKTSSSITSPPKSMSKALKSSIGQLIRYSVPADNSCLFSSINFVLHSGKMDLASNKYLRNMVATKIESDEKTYSEAILGRKNSDYCKWIRK | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
EC: 3.4.19.12
Subcellular Location: Cytoplasm
Sequence Length: 242
Sequence Mass (Da): 27436
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A0A814VB14 | MGLPMGNSLSPLLADLVMNDFIVKNRDKNKFPYNMLKRYVDDIILMSELDKDQIKDLVAYLNKIDKNNIQFTSEFENESNLSFLDVLIKVDKENHKFKTTWYPKPTAAKSLLDFRMGLLEEGHPLTWNQIAVHLPELKKQALEQLIRIWEKNKNRTNDTQTWGDEVGLKIVEFSLLRFDHASKRVQLLLKAHEYLPKLKKLNEQVEEKSQITWHEEAGDHCVEGVLSSPFDHSSAHYSMVEESLRRRREQAQHLLAKDEYILNVCAFPRMGCAEFTWPVLKSDPLSSWEQSICFPQEFISPIHPQMKIVKNMVERRKSKFKVNLPLLYDQLIPMTPVMLALSAACPIWRGYLCDVDTRWNALCESADDRTEEEKNNQETFVGLVPIIERYVKEELQGVTESSRENIHRYLELISKRAAGTTATNATWMRQFVSEHPSYKQDSLVTEEIQHDLMWAMQKVANGKEEVESKRP | Pathway: Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 471
Sequence Mass (Da): 54853
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A0A815JAK5 | MSSSTGANLTQVSINTKTDSHQQDRRVHQQRSLECFEIIWLDAHIDKKTNDNSNTITQLRRVVNNNLKTFDNPDQCSTYISSIQNQKIFLIVSGSFGEIVVPQVHALTQIELIYVFCFDKAKHEKWTNKYKKIVGAFSDIDSICDKLGVDVNSCTNDLMPFSAISSAEEINKQDPSFMWFQLLLDILLNMKHTDGTKQEMIDLCQERYKDNEEQLKYVREFKTYAPDKAIWWYTCNCFLYGMLNNALRTLDIGTLFKLRFFITDLHDQLKQFHSEFIHSTSIKAMTVYRGQGMSLEELKKFTTGGLLSMNYFMSTSTEKMQALEFVDQAISKSPSNQGILFEMKVDVKTCHKPFHNIQHLSFYPSENEVLFSMGTVFRIHSIQQTGSRSWSIDLKLVAEGDQQLQTLMNHMRKDIGEGSDLFALGDLMLKMGHYNKAQEYYELFLKSLPENHPSIAATYNNMGLVHYNQGNYVEALNYYKKTLEIQLKSLTENHPDIATTYNNMGGVHDNQSNYIEALNYYKKTLEIQLKSLPENHPDIARTYNNMGHVHDNQSNYIEALNYYKKTLEIRLKSLPENHPDIARTYKNLGHVHSNQGNFVEALNYYKNTLEIRLKSLPENHLSIARTYNNMGSVHDNLGNYIEALNYYKKTLEIRLKSLPENHPSIAATYNNMGLVHYNQGSYADALNYYKKTLQIQLKSLPENHPEIATTYNNMGGVHDNQGNYVEALNYYKKTLEIQLKLLPENHASIARTYNNMGSVHSNQGNYVEALSYYKKTLEIRLKSLPENHLDIARTYKNMGGVHDNQGKYVEALSYYKKTLEIRLKSLPENHPSIARTYNNMGSVHDNLGNYIEALNYYKKTLEIQLKSLPENHPEIATTYNNMGHVRDNQGNYTEALNYFKKTLEIRLKSLPENHLDIARTYNNMGHVHDNLGNYVEALNYY | Catalytic Activity: L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-ribosyl)-L-arginyl-[protein] + nicotinamide
EC: 2.4.2.31
Subcellular Location: Cytoplasm
Sequence Length: 941
Sequence Mass (Da): 108744
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A0A0S3IS07 | TLYFIFGAWAGMVGTSLSILIRTELGHPGTLIGNDQIFNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSIVETGTGTGWTVYPPLSSTIAHSGASVDLSIFSLHLAGISSILGAVNFITTIINMKSPGMTMDKMPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 219
Sequence Mass (Da): 23602
Location Topology: Multi-pass membrane protein
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A0A0N4YD47 | MERFNVQLSMIVNTCRATINNKDFVGWLERERFDLAFGHMFDICSIGLIHNAKIPSWIWLNSGSVMDYVAYYIGAPLIPSYVPPMMMEAGGEMNFIQRTKSFIGHGLTQFFWKRLIADPETALFRELISPDFPDLLELAAKCPVVMANTNNLYEIPRPTLAKIVNIGGIGMESRNAKPLPKNIDDIVAKGKGTVLFSLGSVTAAYKMPYEWKMAFLEAFRRFPDYQFLWLPQSDILHHPKTKAFISHGGYNSVQEAILTGMPLIAVPLFGDQPKNARLAERHGFGVILHKKEISIDTISSAIREVTENSRYAEKATRMLRMIQRQPVDPTLQLVKWAEFAAEFQTLENLEPAGNRLNFIQYHSLDVIAFLGAILTLTILVIIVLLRTVFMFVRRLIFGARKQKTA | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 405
Sequence Mass (Da): 45960
Location Topology: Single-pass membrane protein
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A8TJU1 | FSSVAHIRRDVNYGWLVRNIHANGASLFFICIYLHIGRGLYYGSYMFKETWNIGVVLLFLVMATAFVGYVLPWGQMSFWGATVITNLLSAVPYLGDSLVQWIWGGFSVDKATLTRFFAFHFLFPFL | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 126
Sequence Mass (Da): 14433
Location Topology: Multi-pass membrane protein
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A0A0V0J258 | MSTAISPRIAPRISLSMRDLHCLLMLLACCLGAEATECLKMLCHQTNTSDCHPCVGLNSEQLSRWRRYLDAILSDWRDTSHMPSYYEEIRNQPLCCTLQENGTCHLSLIYEPKVDPTRLYDLKCMDGNDMWTQFRCISGHNTRCCKGNFCNMPTDKEVDAVTRETPQRLHMIVVGAILALVLLLLLIGILLFSRYKRESGHSKAKRNSQNSPSDTCAWISNANGLGSAGDPLITKNTVPSIVAGFGNQRGVYVSGPPSMITSLGSGSATTNLPNPSFHPNPSFTISVPKTSEIITGGGNTTATATNSYAPVSGSAAIMSSQLMGSAGGVVGMLTQQEISLRALLDATGSGSGSGLPLLVQRTVARQVQLEERIGEGRYGEVWRGTWQCDQVAAKIFSSRDENSWARETQIYQTVMLRHANILGFIAADNKDNGLSTELWLITEYHRLGSLYDFLQSHALNAYALVRMASSIVNGLAHLHMEITGTQGKPAIAHRDLKSRNILVKDDGECCIGDLGFAVKLDSVSGHLDVGYNPERVGTKRYMAPEVLDNTLRQSSFEAYKQADMYSLGLVFWELTRRCYAPDLYEPEDYQLPYQDMVAPDPSIEEMKSVVCEQGLRPFLPPVWSQHPILSVLRHMMTECWYASPSARLSAMRIKKDLGHQRKLVNPDDPIKPNCTLHGLPPEESLPRGVFVFQANRGIGFAQPVEDDHSKRENQEQLLTPPQSTAEVPLIDPNLLPEAVKPASYTSALSLNPLTLSVAAVVVTPLNEIEPAFKQPATVA | EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 779
Sequence Mass (Da): 85707
Location Topology: Single-pass type I membrane protein
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A0A846NJ34 | MATETLSPERFRTLDDVDIDDKVVLVRVDINSPINPFTGEIMNDLRIRAVLDTLKELEGSKVVLISHQSRPGMGDFTSLSLHTSVLRSYLGDRVRFVPDIIGPTAIREIRRLESGDILLLDNIRLMAEEMMKAPPEVHANTLLVKTLSKHFNLYVNDAFSCIHRSHASLVGFPSHITSVIGRLMERELRALNRVLGSEKDKLVFMLGGAKPEDRIGVIKNIFESSPKDCSFLLGGVIAKVFLVATGQRLPKSVKKETAAHYEEVEMAKSLLEKYGERLILPVDYAYEMEGERVEEPLENIKNSQMVYDVGLKTIEKYLQIMKGADLFCANGPLGLMENPLFIRGTREALNTAAELKGYKLVGGGHLAALIEIENLKDRFDHVSTGGGSLLHLLSGRIPRALQLLMKS | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
EC: 2.7.2.3
Subcellular Location: Cytoplasm
Sequence Length: 407
Sequence Mass (Da): 45330
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A0A183BD77 | MRKSEICKLKKVLDPARKSRNKRKSVKSSKKSRVPQYSTLTIGNGLMKKVRTKDSLDALIHSSIKEALELFEEDPKAFEVYHAGFQQQLTQWPDDPLQWIVNYVNEISRGRKIRIADMGCGDARLAMALGEEKKVYSFDLVAVNSRVTACDMAHVSHVLICFSQIPCLYWGSLKQSLVTLQSYDTNNSILQTISFLQNSISEI | Function: Probable methyltransferase required to silence rDNA.
EC: 2.1.1.-
Subcellular Location: Nucleus
Sequence Length: 203
Sequence Mass (Da): 23044
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A0A820CVZ6 | MSNIYIQEPATRGKVILDTTVGDIEIELFSKECPLACRNFLQLCMNGYYDGTIFHRVVPNFIAQGGDPTGTGEGGESATGTAFAAR | 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: 86
Sequence Mass (Da): 9247
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A0A5S6R1S5 | MRSLWKKFPFSGNDEEEDIISEVTSGSSLSWGTRIKLFALCFCFGIFFSILGSICVYLHNFTMFSVLFSFGSIMSISSTCFLMGPIKQLKKMADPNRWISSLIVVVMIVMTLFAAFYWKKGALCLLCVMLQYIAMTWYSLSYIPYARSTVRKCFEACIP | Function: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Location: Membrane
Sequence Length: 159
Sequence Mass (Da): 18163
Location Topology: Multi-pass membrane protein
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A0A5N5UBX5 | MPEESDDDTTPPEPAVRRLDDETGDGSDSDADDAPQTGNTPDSDDTTAGATDSDEPLDPEDDPDTPTADPVETPADDDGDAGDDPNTSPTTMADDPFDGYEVDTTPAVERDSLERDADDDEDGPDETDDIGDRGDASFDDGSPGVSGSVGDSAEVAQPGPVSEPEEFEGAPDDQEMPLADHIEEMVKRLGVVIVVMAAVSGVVFPFATYLINFLWFNYLPGTEEICRQVAQVGATNVDPQTACARVYHPLAVVLARLKVATLAGFVVALPLFVYETYLFMRPGLYPRERRYYLASVPTSLVLAAAGMLFAHHLVIPILFDYFVGYSEGATTLAFGLTETFDLIVLMLGAFAIVFQIPLFIMLALMMGLVTRTWLQSRRLIFWGLFAALAFLFTGDPTGLGPIFVAVTMIVLFEGTLLLAQWTGHE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes.
Subcellular Location: Cell membrane
Sequence Length: 425
Sequence Mass (Da): 45814
Location Topology: Multi-pass membrane protein
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A0A183T1P7 | MRTDLVKVNDLQKKRPAQARCLEYVVTHTFVHRQVRAISTWVYSSHFSLALLSFVRGARRLRMALVGRVVVKTLLNSIFPDIQFTMEEEVNNQLPLLDIQVTKLADGKIRTTVYRKATNTMRILHFKNIDKEQETYGEIVQQDFIDHYDNNTYKAIMGLKWASAYCPQANFVVSLDDDFYANPRLLNQLLDRRTALLINQPYQLVGHVYENASPYRTWFSKWYVSLADYPWTHWPPYPAAGAYVTSMQLIRLMALEADHVAYLRFDDVFIGFLALKLNVQPEHDDRFMLSTRTCRIELHKAIACHTVGSPSTVLWLWEHRLDHNRRRLS | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 329
Sequence Mass (Da): 38507
Location Topology: Single-pass type II membrane protein
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A0A6A0GTX7 | MTVTYSRNVALSQKSFSVFLKLLFRWRGSVYKLVWRDLVVFTLVYAALSLVYNFALQDGGKRLFANVVTGVRENGRIEVSSLIFVLGFYTSHVMQQRHAFYSVIPCTDAFAMAVSAALRGRDSHVLRLRQTLVRYANLACTLTLTNICLPLKKRMPTAKHFIETGFMTEQESEIIQNLDPKAKGFGRTYWVPLVWATNVITRSETYVGDREKTTEISGLNTSRMLDELHKLSRSCNQLMSHDQEIIPLVYTQMVTLAVYLYALGAVIAGQFLDGDHTTEGLNYNYYVPAALLLQIGFYCGWLRVAETLINPLGEDDNDFDINPIINRNITVSRQIIGKHGMCPEQFAEDEVDYFTNKWPRNELPYTVASKTFDKEPYRGSFAEYEVRSEKQKFVVSFEPDQVDIEMMTLQEPEDDQVSRKGVLPSVLRRRKSRKTTRHLRPRMKTVSIEELEQQRKRQTKVERQTEKC | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 468
Sequence Mass (Da): 53933
Location Topology: Multi-pass membrane protein
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A0A183AT94 | MFQVLPASCFALGCWQVGRRRWKLDLLAKIDENVKKPPIPLPRDVNTSLDLPEYLPVTVRGQFDHSREVYMGPRALIADLVPDSVLECGNKIMPTPEEKSNSTQEQRRKHVPHLSLPGYFVITPFFLADRPGQSILVNRGWVHMDLLDPATRPMGQVKGTVTISGYNRYPEAALSMGPFSMLVGSPNKKDPHTHPQYFNRQVDDMAQTLGTLPIFIDATYGEFL | Function: Probably involved in the biogenesis of the COX complex.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 224
Sequence Mass (Da): 25244
Location Topology: Multi-pass membrane protein
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A0A814GNI0 | MEPFMTIMVAMDENNGIGLNNILPWCLPGDWNWFLTISTNTIDPKKRNAVIFGRLSYESLLKQDRSPLKHWHTIVISSNSEAIKQQSSETSVTVVPTFERAAQYSYDMFHNADQNIENVYVLGGVQVYDQAVKLKLVKRIYLTRIFATFNCDTYWTTLDLSGFKPVKRNSNEILSTEDGQIKEENGCKYQFQIYEIA | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 197
Sequence Mass (Da): 22708
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A0A183T6Z0 | MTKYNEMKVALQKLQTQAEFQNQVSNLTGRCWDLCYTGTPGAKLDDKRANCLKNCVERYIDVSNYTGRLAKISWMVGHNCIVIIPL | Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 86
Domain: The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence Mass (Da): 9814
Location Topology: Peripheral membrane protein
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A0A846Q3R7 | MGKVVLIVGLPGTGKTTVVLRAVKLAKKEGIKLREVNYGTLMLEKALEKNYVSGRDGIRKLPLESQEELQRRASEEITGLREREDIVIVDTHMIVNTPRGWWPGISVKNLKKVDPEQIILIEAQPSEILKRRRKDASRIRDIEEIDKINKELLYSRDIAASCSVLTGSPVSIVMNKEGKLEEVAERVLNIIRXVVFGVSVLLSLSYIFLNKKFIYTPDYTRKKSIIDQWKREYGEARKKKDSRHVKRLEKKQDQIRKLESQLAMKTMKLFVITTIPFWLVFYLLSQNFSSLGQFLILPLSFP | Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Membrane
Sequence Length: 302
Sequence Mass (Da): 34793
Location Topology: Multi-pass membrane protein
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A0A0K8U1Y4 | MASIKLSNGLQLLSRNSTSRALSSSVVNSWRNYSNSRGDLETTTHTGQVFDKDDYRNVRFVNAKRYVNENWGIKLIDEIPPIEVTDRVVYCDGGDANLGHPKIYINLDKPGPQICGYCGLRFVKKDGHHH | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 130
Sequence Mass (Da): 14665
Location Topology: Peripheral membrane protein
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A0A813UYW1 | MLNGVRSLSYRVSAPAEHQLSQLRIKILNVKLPSSTKLVDVCVILEVDSKYSYRTEIIKKKHRPLSQITSSSTSNATMSTVLNSTSPSISATSNTSSHPTVNVNESFDVLVTNNSKILLKVIAPTRLFGTNDIGQVKFDIKTILNEYQMKRHTFQETSPPSYKTELPLENSSRRTADHLNNSGTSTTASERGSIEILLHGAILNESENTTNNSNETAHIENNTLLNNTRSLSICQQDHPQNSLTTSNRQLLTSLENHSIPTESAVLNSPIRHPQNQSSSADASQPSRRSILLKQPSARDVDTGTASPRRGSGSSSSDAVSGSTRSRRHHHLPLSRPTSNTPVTSSNLPVPATTADASSISSVTPAQLARIKETLPQGWEIRLDSQNRPYYVDHNTRTTTWLRENVLPPGWERRVDARGRVYYVDHNTRTTTWTPPTALHLQNVAHWQNQYARSHSMFNQFEHRFLPPTAGTGAIAISGSENPLENAAPAITEEDIPLPQGWQQMFDIQGRQYFINHLSKTTQWEDPRKMNTGDQLLSGWEMIYTKEGQPYFVDHNTKTTTLQDPRLSGLDASNSRHGSRIPLYQRSLPFKIEQFRYLCNTNISSGQLRLTIRREHLFYDSYTHIMHCQSSELRRHLYIVFKGEEGLDYGGVAREWFFRLSHEVLNPMYCLFEYANKNNYYLQINPASSINPDHLSYFRFIGRFVAMALYHGKFIDNGFSMPFYKRMLGKKLTILDLESLDPDFYNSLTWIKNNNLSENDDLELYFNSSYELLGKVEYEELKPGGNEIKLTEENKEEYIELLTQWRFKRSVEPQTKAFLLGFNEVVPSQWIQTFDEREIELLLCGISKIDVGDWERNAIYKHFTESSKQVQWFWQFVREITDEQRSRLLQFVTGTCRVPIGGFAELLGSNGPQKFCIERFGKETMLPRSHTCFNRLDLPPYKRYDQLKEKLLYAIEECEGFGQE | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 963
Sequence Mass (Da): 110040
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A0A2P2I1R5 | MSEEEQLSLYRDLARYPVLKDAYIVAEKNNSIVCESQWSTRNLSVLKQVGSMCTQVVTGEASSIPRHTPLLNNVVLIGRSGECSAMLVQSGGAGEKEETLVCYIFLQQPSQPSTIIDLSKTKLHGKVYSDGELGCLVFSPNSSQLAFVAEEHRPKPSSMLDPPSQEDEPSGRGQQFSRLPDWGEQFTGKHRSVVVVVPCKDTGSVPEKQSGRVVLNPPADYAGVGQLQWAEHNTLVGVAYIDASPRLGLIYCRIREAVIFHVSLNDGVFKELTPRGWWVGSPRLSPDNTRLVYLRGSVGGPHVREAQLVTRPWSSEPEIQVLEPRVVVDYVPSEVLLPEGGRFAGLTGASSLPLRCFIDKGNTLVFTTQGRFAMHSYTLDLESGSVVQVLQEGKGGSVQILDATAHHLLYTCSSFTSTPSLRLATVPSFQQDPVVLVESIRTVGEEELSVLDSPPPHPVPEYRDVPVPILYCAPPPELRSSSGVPLIVCIHGGPHSIVTNSFILSVSLFVSLGYAVVFPNYRGSLGVGSKGIHSLPGHCGDLDVKDCHAVMQDCLQRYDYLDSENVFLYGGSHGGYLVTFISAKYPEMYRAVSTRNPVTDMAGMIDSTDIPDWAHVEASTGESDSSPPSAAALAKMAAASPMWSIDSVRAPTLLMLGSQDRRVPSSQGWKYYELLKHRGIPTSVHVYPDNHALATVEHESENLLLTLRWFKKYAKMIIK | Catalytic Activity: Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide.
EC: 3.4.19.1
Subcellular Location: Cytoplasm
Sequence Length: 719
Sequence Mass (Da): 78597
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A0A814LLD7 | MRIVLHTSHADTTFLATPDISEILETLLKQEGYADKPRSQANEAYVAQFNKSHLALPPTRNVAIVACMDARIDPAKILGLEEGDAHVIRNAGGMVTFKDADLQDKLKKELHSTADHIAFLSIAKLEDSVRDDVDFLKSSPLLFKDVPVSGWLYDVKTGKLNRIV | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 164
Sequence Mass (Da): 18153
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G8YIW3 | MLARQYLKKNFAAPTRFFSSGKVAFQKTPEIYENGADRPKELISGAPAELTTKRVVRIYQEAKSATQSGQFNSSHWKLNWDVLGKGNRWENDLIGYQSSADYMQGTTMKFDTKEAAIRFAEGQGWDHYVQEPKKKHFRKKEYAMNFYHSSGPLKHIRTK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 159
Sequence Mass (Da): 18403
Location Topology: Peripheral membrane protein
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A0A158R1A5 | MSWRVEDVYSDRCILLTGSTGFLGKVLVEKMLWALPSVGQIFLLIRPIKGMSPKERLEKVLQDPLFNRLREQRPHVFEKLVPISGDLMEDNLGLNQHDMQKICDQVSIVIHSAATVKFDEELRVAVEMNVVGTMRLIALCHKLKQLIALVHVSTAYANCDRAETEEKVM | 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: 169
Sequence Mass (Da): 19229
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A0A813T0N8 | MTESGDSFQLCFQLDNICTDPERFLSAISTYVNKVHVLNKRVSTAILAKSLSKQDFKFLQSIYPQITANFYIDKRQLLSKNSQLYSDVEEYILYDHLSNNVTFFPVNKEITISFPHETSRRPCSPLIPYCIELTNENNLRLLVSSTSECDNKTMEWFKQILLKKLSTWCQLKDACSSEQTTLKLINITQYQKQYEYLKQKYGKYLIENWQELTDPQKHVHEDIGKIICSVLGIASYLITYWNENACRNEKPTFVDFGCGNGLLTCILNSEGYRGIGIDMRKRRSWKLFDSSSTSYYRELTIDPHNTILFNLLLEQKFSYIIGNHSDELTPWIPVMAQRLNINFFLLPCCFYDFGGKKFTTKKHENQNDAYLNYVEQICQVLNFDVQRDKLRIPSTKAICFIGRRKNINMTGHSNDHQESISTYNARDQILKHFGIDLDCVTAEKETKQSSLMINKKTILQKTVKSDIALILFKYILQNGSISIPDAYNILPMNLKEQIKSEPGGLNSIIKSYKEIFLLSNNNIHIADPLENDMKQKLSKNGGNDQVMKNLKTKICFFHFYHPDGCPLNRKNCKKHTLHKVSQYKKGKDSVHVQGKRRYDMKQQGFGGQKKPVFHKKAKTTKKIVLRMECTECKYKKQLPIKRTKHFELGADKKKKNQVINY | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 661
Sequence Mass (Da): 76884
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A0A6L7LW95 | MLVDVFEVLYLSLGLVFLYAGVAKVKDFQELLLAIEHQQFIPEFMTKNVALIVVGIELILALGFIFGVFLSVTLWTSLVMIIGITILSRIFQTGEKQNDCMCFGQDEVLLKSWKSWSRAILMIAGVCVGIVLFYLLPEVDPLSMSLDTLLISLIVLLLLSWVTDIAEVKNHAIDP | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 175
Sequence Mass (Da): 19551
Location Topology: Multi-pass membrane protein
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A0A6L8F9T6 | MIFILITVFIDMLGIGIIIPILPELIREFVGGSSALAGRWYGVLAATYAVTQFVFAPLLGALSDRVGRRPVILISLFGLGIDYLIMGFAPAIGWLFVGRLIAGVMGANVTTANAYIADVSKPENRARNFGLIGVAFGLGFIFGPAIGGLLGSIDLRLPFFASAGLALLNWLYGFFVLPESLPAEKRDVFRWRKANPVGSLHVLRTYPLVAGLTAAFVFVILAQRGLETVWVLYTGHKFGWDERANGLSLALVGIMSAIVQGGLVQPVIKRIGERRAVLYGLIWAVVAFLGYGLATAGWMLLVVIVVGSISGVAGPAIQSLVAGSVPPEDQGKVQGGIQSLMSLTSIAAPLIFTAGLFSYFTSASAPVQLPGAPFLLGAVMYALAFWSVLRLFRRMPG | Function: Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter.
Subcellular Location: Membrane
Sequence Length: 397
Sequence Mass (Da): 42217
Location Topology: Multi-pass membrane protein
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A0A814QTV7 | MQFVESGKFFVARLIDKAGVDRESHCALNSTCKKYDDNYRLTIDYFDGSLNVSDSKMLVESVGKYFDENGVLCYKRFCADLKKIYDSLRLQTRKQQ | Function: Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Enhances the enzymatic activity of SPC and facilitates the interactions between different components of the translocation site.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 96
Sequence Mass (Da): 11169
Location Topology: Multi-pass membrane protein
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A0A947IP91 | MKSGAIFLVGPMGAGKSTIGRLLADTLRFDFRDVDREIEDRSGVDIPWIFDMEGEEGFRDREESMLAELSDAAQVVISTGGGAVLRGDSRKLMVAKGTVIYLKTSVDEQIRRTARDRKRPLLQT | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
EC: 2.7.1.71
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 124
Sequence Mass (Da): 13762
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A0A8B7NX57 | MLQTTLLKGLRRLCLPRLQPCCHMSYVVLLPEDPVDTAENNALLRTAHGDLPNFEEITGEKCHAGVGKLALDLETGVWEIEEKIRDKPKSVSFDTVLKPLDALDAQLNFGWSTAKVLYIARQDKLPQKTYLGLHERARKARVQKFQSLPIYKACKVISEQEAPSLDSNKRRVLQKFLLESRLNGMDLSPTKADQFLSIINKLDQKKQQYRQKVQVSTSRFAYEITDPNIVQHFPPHLLERMSPSGSDTTRGPWHVTLKSDVYEGFMAHCSKRALRWNTWQAYNMRATRFIDPQLDNSVNIEEIRASRNDLARILGYSNFATMSMETKMAGSVENVLSLITSLMAKAVPKQAEEIASLTAFAKERDFSEDALQAYDVPYYSRLQRQHLYGEGEKLRQFFPLDHVLTALLQLSAELFAVQFEELAPGPELKAWHPSVRLFNVLEEDGAPIASFYFDPYRRPGEKLEPTSGSGWFASLRSRSTLSDRPVAALVFNFPPPGSDAQHDSDETLLTVSDVVTLFSKFGEALQHMLTTVPYGEVSGLTNIEWDAMALTQHFMANWVFVPEVLSSLGRHYDTGAPLPPDVIADIISSHNHMAAHNLSKHLYLANLDLLLHTTKDFWKSIMTGLWPQFLPYELDKKDYHPCSFTASMCDVWAAAYYSHTWARVMAADCTKSFIDDERSHWRSTGLRFRSTFLSLGGGEAPAEVFRKFRGRDPSPDALIELYGIGGAK | Cofactor: Binds 1 zinc ion.
EC: 3.4.24.70
Catalytic Activity: Hydrolysis of oligopeptides, with broad specificity. Gly or Ala commonly occur as P1 or P1' residues, but more distant residues are also important, as is shown by the fact that Z-Gly-Pro-Gly-|-Gly-Pro-Ala is cleaved, but not Z-(Gly)(5).
Sequence Length: 728
Sequence Mass (Da): 82346
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A0A183BD43 | MEKTDISKRAFGTAEEELSYYAPRGIMMWGETVSEALNMGRLAVRAVGENDVETYRPLTLLIEGPPKAGKTALAVEIAKLSGFPFVKILTSHKMIGYTETAKCAAMKKVCRSVVSVFKSFPHCYASKATVEQVLIFL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
EC: 3.6.4.6
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 137
Sequence Mass (Da): 15069
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G8H0K5 | IKLFTKETSMILKSNYLYFLISPVLSMMVMLMLWYNIPMFSNIMTMKMNLLIILCILSMGVYSMMVAGWSSNSLYSLIGSLRSIAQTISYEVSMILIMLCLILLIESFNLNNLSKYQYFQWFSLMNFPIMLIFYVSFLAELNRTPFDLA | Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 149
Sequence Mass (Da): 17397
Location Topology: Multi-pass membrane protein
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A0A101E638 | MLTTVLMVMQVVVSIFLIVIVLLQKGKSAGISGVIAGGAETFFGKHKAKTLEGTLERLTVIGATLFIVLSIILTILMAR | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 79
Sequence Mass (Da): 8386
Location Topology: Multi-pass membrane protein
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A0A0B0HE01 | MLQTIFWTIIAIGLLVTVHEFGHFWVARKLGVKVLRFSVGFGSPLWKRTARDGVEYVVAAIPLGGYVKMLDEREGGVDEAELPKAFNRQKLGVRTAIVLAGPLANLIFAIFAYWAIFLSGETGLKPILDEPIPESAAAAAGFRSGDEIVEVGGESANSWERVIYQLVEYAVDGEAAPVSVVGEDGMQRELFLPAESLLVLTESQGAVSQIGLVQKLPHIPAVIGEVVTDSPAEAAGFQPGDRVTGVNGKPIQDWHGWSREIRENPGRGLEVEVERNGRLQLLQLIPGEKGSGDSVIGFAGVSYTDDVDFGRYRSEIHYTPLAALERAAQETWKMSALTLKVIGGMLSGQLSVESLGGPVTIAKAAGDTAEIGIGAFVRFLAMLSVTIGILNLLPIPVLDGGHLVFYLIEFLAGRPLPDSVQARAQGIGMMIMLGIMLLALYVDFGRFFG | EC: 3.4.24.-
Subcellular Location: Membrane
Sequence Length: 449
Sequence Mass (Da): 48241
Location Topology: Multi-pass membrane protein
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A0A1X1T7H5 | MSATSTVNVINGPNLGRLGRREPAVYGNTTHADLVSMIEQEAAGLGLSVSVRQSDSEAELIGWIHAAADAGEPVVLNAGALTHTSIALRDACAELGAPLIEVHMSNVHRREEFRHYSYLSAVATGVIVGLGVQGYLLALRYLASAQRRFSGGVAGSVPPP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 160
Sequence Mass (Da): 16743
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A0A099UCT5 | MDRIILGIDIGSTKICAIIAEIKDDGIPHIVGTGMHKAEGVRKGSISNIEQASTAIRNAVNDAKMVSGEQIDKAIISLSGAYVKSIRETAIINAPKNEIGLTEIRRVMQTAIYNADIPDDHTLIHALPYEFRLDGQSYAEDPMGMSASRLEAFVHIVAAKKTALENLKRAVSEAGIEIKNIVLSAYASSIAVLSNEEKELGVACLDMGGQTCDLMIYSGYSMRYCDFLSVGSHNITIDLATALNAHPSIAEEIKAECGKLILSEDDKTKSVKVSMMTGENVEKFVPLEVIHAVIFARVEETLRLLAKSIEKSGLKDKIGAGITLTGGMANLEGMQECASSIFRKPVRISKPIAVDGLFDRLRGTDGATAVGLILHGAGRHTNYEMNHERNLLYKSNIITDSADIHSLELPKSAIEEPSIGSRITQIEDLSEIRTSNGDKRNNLFVRFREWASQLF | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 455
Sequence Mass (Da): 49542
Location Topology: Peripheral membrane protein
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A0A6I3DGE2 | MFRSGFVSLVGRPNVGKSTLVNNVVGRKVSIVSDKPQTTRTKIRGVHTTSSSQIVLLDTPGIHRPRTLLGERCNERSVQTLREVDVVCLLVEADSPIGPGDRFIANLVKESRTPAILVVNKVDLADAAAVAKRLSDSSGLADFAAFVPISALTGDGVDLLVAEINARLPEGPEYYPGGVVTDQPEAVLVAELVREKLLAIAREELPHSIMVTAEAFEEEEQESFNRRGRKVEGSEEGSEEGGQDGESSAPEKEEILRFRVTIRVERDSQKGIVIGHKGSVLRDAGTAARVEAEQLLGARVYIENKVKVDPNWQRRGHALDRLGL | 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: 324
Sequence Mass (Da): 35197
Location Topology: Peripheral membrane protein
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A0A3N4CY86 | MTAHAVTRHEIFQTSLISALAQGVYEDEMTLAELLGHGSFGIGTFNGLDGEMIILGGVCYRLRGDGSVSVPELTERTPYAVVTNFVPSLSRSLTGPMTREEFSRAIDAFVPSSNYMYALRVTGRFAWASARTVTKQDRPYRPMIEATDGEEIARHEDFSGTIAGFRTPLYESGISVAGCHAHIVDDDRTWGGHLVDFVLEEGEAELCLGTDFHMRLPLTEEFRTADLSEDMTEEIRRVEHH | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 241
Sequence Mass (Da): 26765
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A0A7K0VAP5 | MADLIEIKGIKAFGYHGVFESENIAGQDFYVDIFMELDLTRASVTDDVNDTVNYAEITDLVVEEITGERVSLIEKLAARIADRITAAYPQIAQVSITVHKPQAPVSAQVKDISVTIKR | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4.
Function: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
EC: 4.1.2.25
Catalytic Activity: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde
Sequence Length: 118
Sequence Mass (Da): 13026
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A0A0K2Y4N6 | MVRTYQQSGVDLDKAQALIQAIAPLASQTYNESVLQGVGGFFGACALPSGYKEPVLISCTDGIGTKLKLAKEAHQLYNLGLDLVAMNVNDLICAFAKPLFFLDYFATSKLEPAQTLALIEGMAFGCKESGCALIGGESAQMPGVYKAGEFDLAGFCVGLAEKSDLAKKDKIKAGDILVGFKSSGLHSNGFSLVREILKSKPKNAPSLATLLTPTRLYTPLLALKDKIHSLAHITGGGLKGNLLRILPAHLSAQIELKALPRMPVFNWLLEHIDFSECLRVFNMGVGMVALAPLESLGALMRAGGFYLGALHTGGQSGAQEITFVE | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
EC: 6.3.3.1
Subcellular Location: Cytoplasm
Sequence Length: 325
Sequence Mass (Da): 34546
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A0A7M7HG44 | MEAGSLDIQHGLEEVNQELQHVEKQIERLLTKQQRLLQRKEQLEVQTSRLHELSLQTGSTDWEKSDYPWSAKLRSLCETVFGIKKYRPLQEKTMNASLSGRDVILLMPTGGGKSLCYQLPALVSKGFTLVVSPLLSLMEDQTMALEEIGVNATVLNSNTPPESVKDVHRQMIDARSELKLLYVTPEKIAKSKRFMACLEKAYKANLLTRIAIDEVHCCSQWGHDFRPDYKILGLLKRQFTDTPILGLTATATMDVLDDVKGILGLQGCQVFRAGFNRPNLFYEVRPKPSKQAEFVEELIKLINGEFKGQSGIIYCFSRKDTETMAENLKKGGIQAHPYHAMLDAQYRSQVHRNWKENNIQVVVATVAFGMGIDKPDVRFVIHHSISKSMENYYQESGRAGRDDEPARCIVYYGIGDVFRQSTMVVTEQTGQQKLYNMVAYCVAPATCRRSLIGQHFGERWEGQARCNRMCDVCQSGAQVVEKDMLPHLQRIYTILDHKAKSDNRITALKLTDELLSKKGVAALDKGTYQAKKMTGRDYEYLIAHFLLEGYLREDFHFTPYNTISYIIPGPKARLNTATPQRAVTVPFKMEDGQRSKVRGQGVKGQGGARGEKEKGRGRPPRRRPRRTRGRRMEMEE | Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 636
Sequence Mass (Da): 72290
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A0A7N0U2M5 | MVDAHTARSIVGIIGNVISFGLFVSPCPTFWRIWKNKSVEEFKPDPYLATAMNCLFWVFYGLPFVHPDSTLVATINGIGLVLELFYLTLFYIYGDNKQRKKMSAVLAVEAIIMAAIAAVTLTVFHTHAKRSTFVGAFCVAFGILMYASPLTVMYKVCRDKSVEYMPFWLSFTSFANGIVWVAYALLQFDLNILISNGTGAVLGAIQLLLWTYYREIYPKCCAGDARQTDIEIMAATKVQDQV | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Membrane
Sequence Length: 242
Sequence Mass (Da): 27082
Location Topology: Multi-pass membrane protein
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L0AGU6 | MTGYTATVTVRLKHGVLDPEAETTQQALERLGFELEDLRSADRFEIDLEAESAEDARERADEMAERLLANPTIHDYDVEVDER | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 83
Sequence Mass (Da): 9465
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A0A6J3KZK7 | MVRKMTDRKVLFACLVLITLLHPLVHMVSGEECTTPNNQTGNCLNIKTCNPLQEILQTQGHTATDFLRQSLCRYEGHAPIVCCPNDPNKEKRGILIETVYKYVPLRPPYCGFSNGEHTRVVDGKPAKLGAWPWIAALGFHNPQNPDTEPEWKCGGSLISARHVLTAAHCAIRSDLYVVRIGDLNLKRDDDGAHPIQMGFESKLIHPDYTPNIHNHDIAILRLVEEVPFSKYIHPICLPIEESLRNNDFVGYNPLVAGWGALRYRGPRSDVLMEVQVPVVSNAECKTAYSKFPNAPITDGVICAGYAQGGKDACTGDSGGPLMIRQQLTFYLIGAVSYGHACAVAGYPGVYTRITSYLDNFILPALQ | EC: 3.4.21.-
Subcellular Location: Secreted
Sequence Length: 366
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): 40424
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A0A075P7Z9 | MKEFDLIGRYFSNGGYKRKDVIIGIGDDCAVTKVPENQQLAVTTDTLVGGVHFLSDAPAKSVAYKTVAVNLSDLAAMGAEPAWISLSLSLPEVKEDWLAEFVDGLYELTQYYSVQLIGGDTVKGPMSMTITAQGFIPPGSELTRSGANPGDWVYVTGTLGDAGAGLDILQNTLEVKGEARDVLINRHYFPTPRVAVGTALRRIATSCIDISDGLLSDLNHILTASGCGANIHVDRLPLSRAITSAVDNDTAIEYALSAGDDYELIFTVSEEQKGNLETSLASTNVKATCIGQLSGHSSNLSLFKGEKPYTPKRDKGYEHNF | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine phosphate: step 1/1.
Function: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.
EC: 2.7.4.16
Catalytic Activity: ATP + thiamine phosphate = ADP + thiamine diphosphate
Sequence Length: 321
Sequence Mass (Da): 34400
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A0A4W2HGF7 | MRRIRWTRRGLLCAGVYIRVLRLRATRAGWGRSGLLGVGCFSCSSVGRASGSTGLNLSWKLCVTIMRLVILDNYDLASEWAAKYICNRIIQFRPGQDRYFTLGLPTGSTPLGCYKKLIEYHKNGDLSFKYVKTFNMDEYVGLPRNHPESYHSYMWNNFFKHIDIDPNNAHILDGNATDLQAECDAFEKKIKEAGGIDLFVGGIGPDGHIAFNEPGSSLVSRTRLKTLAMDTILANAKYFDGDLSKVPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTIFVCDEDATLELRVKTVKYFKGCQTWDNLTLTFTNLITPLIIRSRLVMILMPVEIFMDLEKLGINFDHIWQKTLTVLNPMKPADGSIMNETDLTGPILFCMALGATLLLAGKVQFGYVYGMSAIGCLGIHALLNLMSSSGVSYGCVASVLGYCLLPMVILSSCAIFFSLQGTFGTVSALVIIGWCSLSASKIFTSALAMEGQQLLIAYPCALLYGLFALVTVF | Pathway: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
EC: 3.5.99.6
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Length: 523
Sequence Mass (Da): 57704
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A0A2G6DWP3 | MPEVDYSLYLVTDPAMCAAHGLRHVVHRAVSGGASIVQVRAKNASTAELIAQVQMLRATVGVPVLVNDDVDAAAHAHGVHLGPSDTDPLSARQALGPSALIGLSVSSADQAQAAAQLPAGTVDYLGVGPVWATATKPNAAAPLGPAGLPAIVRAAAGLPCVAIGGIDTARVGQLRGLGLAGICSVSEICTAQDPGERAQALLRAWQGPHTPAGPARPASRTDPA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 224
Sequence Mass (Da): 22418
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A0A173XP32 | MEFYNSEENNRIRHVVNWIVDITVVIAFAWFIVYAYGTQIPIAGHSMTPLLQSEDVVLMDRLSYDFGKPDRFDVVVFEREDQKMNVKRVIGLPGETVQIKGGQIYINDELIEQPEGAGSISLAGIAENPVKLGEDEYFLLGDNRDSSEDSRFSNVGNVSGKQIQGRVWIRIAPLANLELIRSK | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Cell membrane
Sequence Length: 183
Sequence Mass (Da): 20662
Location Topology: Single-pass type II membrane protein
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E7CCA5 | MSTLAPLRLLREPWNASEGNQSNATAGAGGAWCQGLDIPNELFLTLGLVSLVENLLVVAAILKNRNLHSPMYYFICCLAVSDMLVSVSNLAETLFMLLMEHGVLVIRASIVRHMDNVIDMLICSSVVSSLSFLGVIAVDRYITIFYALRYHSIMTLQRAVVTMASVWLASTVSSTVFITYYRNNAILLCLIGFFLFMLVLMLVLYIHMFALARHHVRNISSQQKQPTIYRTSSLKGAVTLTILLGVFFICWGPFFFHLILIVTCPTNPFCTCFFSYFNLFLILIICNSVIDPLIYAFRSQELRRTLREVVLCSW | Function: Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular Location: Cell membrane
Sequence Length: 314
Sequence Mass (Da): 35440
Location Topology: Multi-pass membrane protein
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A0A2E4R5A1 | MSWNSAADFFAMGGYGLYVWGSVGVTVAALILELFVLGQRRKSALSRIKRASTTERNDDNEKQT | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 64
Sequence Mass (Da): 7085
Location Topology: Single-pass membrane protein
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A0A0U2UHD1 | MFVTNWIKRWIRRSLFVKILMYTALLSLIPYVLFSIYFLIEVKALTKKMIHETSSNNILQASVSLEERTRRLNEQWGGKTDKASRELLAGELLDIAVYGYKPMAYILDTNGAVIAKARNDLEPEVHIDLLEAHHSTILDHKSGHVTVNAPGEKVHLLYMSLDKAGWFIAYLIPESRLMSIAAGQAEDYADTQVYKLVQRMSFFLFIGMLLILFFSYFFSEFFTTPIRQLTSALIQRAKGFEIDPLHTKRSDEIGELIHTFNYMDSTIQKLITELHSRSNQLEENVQKRTRDLQEANDLLQQTYSKLKRSEKSRSELIVQVSHDLKTPLTSMKGFLEILNKYALPQEQKKELIDQLLVQTNQIIQLIEGLFDLSSLDAEELTFQKEWINIEFIMDHALKTVFSDGEHANITLNTYYEDHLPLVFVDPKKIYRVFINILNNSIKYASNQPKIHIKITVYLNNKDIVIKMQDNGMGIQKENIDKVFVPYYRETRSVEKEIQGSGLGLSISKKMIEAHHGDIFIESEVNQGTTVYIMLPVVDTGAMMSGVSDMSAG | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 552
Sequence Mass (Da): 63425
Location Topology: Multi-pass membrane protein
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A0A1Y1MPY7 | MTAVTSDVRFRRIITLHSICTSIYTSFIIFILVYTHKIYEIGKRSSLPVIGVLIVGECLKVVFRPFTSETSTKEKQNKPKKFNLSSKLKCALVLCTSIVIYYCLAVLFGAPFLSSHEETFMFALLLTVLTVLPSCLAVGADVTIAILIDLTSFEGDIITETIKQNICVTLVGAWLGAVVIPLDWDRPWQAWPIPCSLGAVIAYMCSNLFNIVGMSSKTLKKKTGRYNL | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 228
Sequence Mass (Da): 25299
Location Topology: Multi-pass membrane protein
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A4EAH2 | MHNKRVLVAMSGGVDSSVTAYLLKSQGYECVGATMRLTCPAPDPTTGMSKVDRDIADAKAVAERLGIPHHVLDLQQTFDRNVIERFVNAYQEGLTPNPCIICNRHIKFGALLDAALDMGCDYIATGHYAKTSQAADGTWQLHRGEDPKKDQSYFLYSLTQERLAHTIFPLAGLDKERDVRRIAAEQGFTNAQKAESEDICFIPDGDYADYIERRCGHTAAPGDIVWRDGSVVGRHNGALRYTIGQRKGLGVAMAHPVYVTGIDAANNTVHLGEAEDLTAVALTADEWIWSAPDARMEAELDAGGIRVGAKYRYRQKDQAATLTRDEDGQMLLTFDEPQRAIAPGQAVVVYRGDIVLGGGTVTGAIK | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Location: Cytoplasm
Sequence Length: 366
Sequence Mass (Da): 39909
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G9J027 | AYSSIAHMGWMTAILAYNPTMTLLNLTLYILMTTTTFMLFMFSSSTTTLSLSRSWNKMPLITASILVMMLSLGGLPPLTGFLPKWMIIQELTKNDSIIMPTLMAITALLNLYFYMRLAYSTSLTMFPSTNNTKIKWQFEPTKRMPCLAPMIIFSTLALPLAPMLSVLN | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Membrane
Sequence Length: 168
Sequence Mass (Da): 18914
Location Topology: Multi-pass membrane protein
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A0A1Y1MYG6 | MRTFLLLLAATFINAENSSTSIAFVERQINLEINETKKLSVTVTNLNNSGVLLSFDVLQEDLVYVYPRKILLEAGNKTYHFTIEGISPGHSDILAITNDSSITIPQEHFSVNVYKKKILDIVSQIIGWIFIISWGSSFYPQLYSNYERKCVIGLNFDYLALNIVGYISFAAFILNLYFNLEIQDEYYERYPRGQIPVKLNDVVYILHGTLAIFVTIGQCCVFERGHQKVSTTAKSLVTLIVSFYITCVALERLKFLKWLDFLYYCSYVKLAITLLKYIPQAYMNYKRKSTSGWSIALVFLDLNGGLFSILQMMLDCYNYDDWVSIFGNPTKFGLGILNALFHSFFIIQHFVFYKDSAYTMI | Catalytic Activity: H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in)
Subcellular Location: Membrane
Sequence Length: 361
Sequence Mass (Da): 41513
Location Topology: Multi-pass membrane protein
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A0A1S1L9K8 | MSEKLKLVSRVSAINWNRVPDEKDAEVWDRLTGNFWLPEKVPVSNDIPSWNTLTDHEKQLTMRVFTGLTLLDTIQGTVGAVSLIPDAITPHEEAVYTNIAFMESVHAKSYSSIFSTLCSTRDIDDAFRWSEENPNLQRKAEIVMEYYRGDEPLKRKVASTLLESFLFYSGFYLPMYWSSRAKLTNTADMIRLIIRDEAVHGYYIGYKFQRGLERVDEAKRAEIKEYTYDLLYELYENETDYTEDLYDEVGLTEDVKKFLRYNANKALMNLGYEALFPREETDVNPAILSALSPNADENHDFFSGSGSSYVIGKAVNTEDEDWNF | Cofactor: Binds 2 iron ions per subunit.
Pathway: Genetic information processing; DNA replication.
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
EC: 1.17.4.1
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Length: 324
Sequence Mass (Da): 37397
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A0A1V8U1V3 | MAARFSYPRAVRRLILAVTVPAAAAVAIQDNLYEITPVTGTSMSPTLSPDYNLTGRCDRVLWSKVSPSANLVRGELVTYRSPQRPDRTAVKRVVALEGDTVILDPRRRPGGVDRSSGREEADRTQAESWDQMGPKFEVPFGHVWVEGDNWRSSNDSNNFGPISKSLIIGHAPTIVYPWERMGTKPWEDRRRIGTRVVYGKQGVPPEGFRDMFE | EC: 3.4.21.-
Subcellular Location: Membrane
Sequence Length: 213
Sequence Mass (Da): 23870
Location Topology: Single-pass membrane protein
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A0A537VVW3 | MPAVGILGLGVSFRRAPVELLERLAFDDADLTKAYLHAQDLDGLDEVVILSTCNRVEAYGNVRSYHSGFIALKRVLVETRGIEHEELTDPLYAHWERDATDHLFSVAAGLDSMVLGETQIQRQVREALRRAETEGAAGPMLDAVFHAAVRAGRRVRQETGLGAAPDAYVAIGTDLADEALGGIAGRRTVVIGAGGMAELAVHHLRGRGVGPVRVLNRSLEHARALAERTHADHGGLDALPDALEDADLIVSATGAAGHVIARGDLVRAAAGRAGRALVVLDLAVPRDVEPSAAGLDGVRVIDILSLRERIGDHSPQTVEDISRAHAIVDDEVRRWVMRRRGDELAPVIRALRSRGDRVVRAELDRWASRLVELTVEERDAVEAIARGVAAKLLHDPIVVMKERNEPGTDRAHAKLLAELFGLDPDDQR | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH
Sequence Length: 428
Domain: Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence Mass (Da): 46296
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A0A958HWU8 | MMLRNKIVKLAVAVGVLTVTLLFTTCSDSEDNITNGEHEAAHWGYEGEDGPEHWGDLDPDYAACSNGIHQSPIDIDTAAVIHVDLPNVQINYQASTLNVVNNGHTIQAKNSAVNYIEVEGTRFDLLQFHFHASSEHTVLGSAYPMEMHLVHQNAAGALAVIGVLITEGLENPVFNPIWDNLSALTAEDFPLANPLNLDDLLPMDQRTYRYTGSLTTPPCSEIVSWLVMAAPIEMSPAQIQAFEAIHDGNARPVQALNGRYILFDASMN | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 268
Sequence Mass (Da): 29290
|
A0A097RN14 | MSLFTTIMASSMSLLGLGRLTALNTARRILLNPTRSTSTSTWRLSVNKGTDTLLVPENQKLDLSPLSGVPEEHITTRKVHIFVPTKSAMQSGINGTKKWKMDFDTRDRWENPLMGWASSADPLSNMVLTFSSKEDAIAFAEKNGWSYDVSEKKSSKPRVKSYGANFSWDKRTRRSAK | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 177
Sequence Mass (Da): 19834
Location Topology: Peripheral membrane protein
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A0A8T6S0X6 | MPPDTGGPTVHKFGGSCLATPELTVRCARIVTESASAPNGTLIVVSALKGQTNLIREMLDRLLAGGNGIDNFMEEVRARHQYIAQSTIMDRHIRSAVMERVETLATRLERLLYGVIYTEELTPRSRDQALTHGERMSAHLFAGVLADRGTTAIPLEADEAGVITDGVFGSATADIEATSLHLGSTVQQTLERGDVPVLTGFFGSDVDGHTTTFGKNGSDYSAAVAARAIGSPVLTLWKDVSGFMSADPNVVARARLVPLISYEEAAELAYFGLEVLHPRTVEPLRPAGIPIQIRDIHNPDSPGSMISPRAQSNDRDIKSITCAKGISILNVHSASIGIRPRLLARIIAALAKADIQILGLSTSQASLGVVLRSRELEAAEEGIRSFNLPELERLEDKSGFALVGAVGAGALEDPSVVPRIMATLSELGQGVATVA | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
EC: 2.7.2.4
Catalytic Activity: ATP + L-aspartate = 4-phospho-L-aspartate + ADP
Sequence Length: 435
Sequence Mass (Da): 46182
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A0A1Y1MSD6 | MATVLYLVTIFVCIQIGYALKCYKCNSQTMDGCKKGSENLQETNCSLEHPDFNQFCLLKFVYDEQQNKDNVLSGCEIAAKSTILSTNMTQCQTDGRYRVKECIVCDTELCNYTNTGSSKKTSIFCTAVLFVLYNFLR | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excitability.
Subcellular Location: Cell membrane
Sequence Length: 137
Sequence Mass (Da): 15518
Location Topology: Lipid-anchor
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Q5BK44 | MGILGPRPLKLARSLRAPRGARLRSLTPDPDSWQASPAKKARVEQDEPATPPSSPLSAEQLVRIQRNKAAALLRLAARNVPAGLGESWKQQLCGEFGKPYFVKLMGFVAEERKHHKVYPPPEQVFTWTQMCDIRDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIFKELSTDIDGFVHPGHGDLSGWARQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNLNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKANELLQRSGKKPISWKEL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
EC: 3.2.2.27
Subcellular Location: Mitochondrion
Sequence Length: 303
Sequence Mass (Da): 33907
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A0A2Y9QTU4 | MPAKGRYFLNEGEEGPDQDALYERYRLTSQHGPLLLTFLLVAITACTALIIIEFINWDTSKLKSLLGTAIVVLVVFVALYLLVYVDCLVRRGLRALALLIWACLMTLGYVLLYDSRMKGACAWEQVPFFLFVIFVVYTLLPFSMWGAVAVGVVSTVSHLLVLSILAGVHEMPSDHIELKLLANAIIFLCGNLTGAFHKHQMQDASRDLFTYTVKCIQVRSKLRIEKRQQENLLLSVLPAHISMGMKLAIIERLKEHRDRRYMPDNNFHSLYVKRHQNVSILYADIVGFTRLASDCSPKELVVMLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCEAIKQVREATGVDINMRVGIHSGNVLCGVIGLLKWQYDVWSHDVSLANRMEASGVPGRVHITEATLRHLDKAYEVEDGHGQQRDPYLKEMDIRTYLVIDPRSQQPPPPCQHLPKPKGDAALKMRASVRMTRYLESWGAARPFAHLSHRESVSVSETPVPSSRRPRAIPLRRHRTPDKSASLKGRSEDDSYTDEMWSAIEGLTSTRFSCSRSDDFHACTCVSIFQEKGLEREYRLAPIPRARHYFACAGLIFLCILLIHVLLMPRMVALGVSFGLVACVLGLVLGLSFADEFLRCCPARGMLRAISQRVETQPLLRVSLAILTIGSLLTIAIISLPLLPLPVREPLGGNKTSVSAVSNQTSCELLLHYTSSCILGFIACSVFLWMSLELKFVLLTVALVAYLVLFNVSPCWQWACCGHGPDNLTETNDTLSSSPHPWNDLKTMINFYLVLFYVALVMLSMQTDYYCRLDCLWKKKFKKEHEEFETMESVNRLLLENVLPAHVAAHFIGDKLNEDWYHQSYDCVCVMFASVPDFKVFYTECDINKEGLECLRLLNEIIADFDELLLKPKFSGVEKIKTIGSTYMAAAGLSITSGHENQAGQWGDFSRPRVHRLCPAGPGAAARPHRHHGGVQPRPDEQAGRHQQALLQLLPPPRRKLPWRLLI | Cofactor: Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
EC: 4.6.1.1
Catalytic Activity: ATP = 3',5'-cyclic AMP + diphosphate
Subcellular Location: Membrane
Sequence Length: 1016
Sequence Mass (Da): 114400
Location Topology: Multi-pass membrane protein
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E5V774 | MVIYISNDEMEKCKKIVVVGSTNVDLIARVSHLPEPGETIGDAEYCLSYGGKGANQAIAAARSGGHVSFISCLGDDAYADTLITSFVDSGIDVDYIQKCVRHSTGIAFIFVAENGENCIAVAPGANNLLRGERMDTILPVIKEADALVLQLEIPYESVISLIEYAHTVDTKIILNPAPAKQIPSYILEKVDILILNETEAMLIAGQSLDFSEPIGIARSLLRRVGQVVILTLGEKGSVIVSDEMEKQIPSYVVNTVDTTGAGDTFCGAFVAQWVEGVDLQDCVQFATAAAALSVTRIGAQVSIPYQKEVIEFMRNRIL | Cofactor: Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2.
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
EC: 2.7.1.15
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+)
Sequence Length: 318
Sequence Mass (Da): 34230
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A0A0S7EDF8 | MYIDNKYYRLSTILYRVKDIVDKAISNNYFWLRAEIGQLKEDRKGHLYLELVEHKDGVVLAKCRANIWQSNAYVIKKTLGENANEILKNGAEIMCYCEVTFSNLYGMSINIHRIDLSYSLGEVERIKQENLRKLVERGYHQKNKELYLPAVLQRIALVSSKGTAGHADFIKQLEENEYNFVYHLDHYDCQVQGDGAVASIQEALSEIESDAYDVIVLIRGGGSALDLDVFNHYELAVTLATSHTPVFTGIGHETDSSLADFVANRYFKTPSAVAAYIVERTALFYTDISRMYDGIMQSYKQCITVEQHKLEVAEKEIRLYGVAQAKQKKQELDTLSNRLITEVRKRLHTEESFIESATQSISYRSQRITGKETQALKEKTKLVAYLAQQCIDVHQQQLNTSLEKLVYQAKGQLKKERVRLVTFEEITTAYDLSSILRKGFAIVMHNGQLLNEHQELNIGDELEIAIYNKKYRIILAEIKEVKQWNNLLMKKPL | 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 Location: Cytoplasm
Sequence Length: 493
Sequence Mass (Da): 56690
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A0A1Y1KVI4 | MKPIRFGVLTVSDTCFSKQNQDLSGPKLQECIRASFPDASIIATRIVPDEKEMIKNALLEWSSQGVMDVILTTGGTGFAQRDVTPEATKAIIDKEAPGLSYAIISKGMAVTELAVLSRAVSGIKNKTLIINLPGSVKGASESFGFIKNVLKHAVAHVREDRETIKCDHKHIRDLSPSKVKIHQSAYRNRNSPYPQIDVDVALAMIFEKLPIASVTECVDISKSLCRILAEDVYAKEPMPPFNASIKDGYAVKTSDGAGVRKVRNVVAAGDVPDSARPLDDDEIVSISTGAPVPQGADAVVQIEDTVLVQASSDGSRELLVEIKVAPKLYQDIRPVGSEITANELVIHKGDAITFGHIGVLATLGKVNVQVYKRPQIGLISTGNELQAPHEELKPSHIRDSNKLALLNLLRQYSYEASDCGIAKDNPDSVKKALHSALAHYDVIITTGGVSMGEFDLIKNVLEEDFNATIHFGRVNMKPGKPTTFATCNFEGKLKVIFGLPGNPVSAMVTTILFVIPALRHLENSKQKSLPMIPVVLGEQFTVDPRPEYVRVRLEAGDNVLTAYSVGNQISSKINSFINANALMLVPSKLVHPNSFKKGDILNAIMLN | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes two steps in the biosynthesis of the molybdenum cofactor. In the first step, molybdopterin is adenylated. Subsequently, molybdate is inserted into adenylated molybdopterin and AMP is released.
Catalytic Activity: ATP + H(+) + molybdopterin = adenylyl-molybdopterin + diphosphate
Sequence Length: 607
Sequence Mass (Da): 65807
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A0A6A8MNN8 | MLTQLDNLFAQSKSQNRAILIGYLPAGFPTQRKAKKIIKAMIDGGVDAIEIGYPYSDPVMDGPVIQAASEEAINNGAGVSEVFELLKTSVDFGAPSVVMSYWSPIEKYGVDRFAHEVAKNGGSGIITPDLTYEESNNWKIEAEKNSLNRIYVVAPSSSNDRLAKVTNECSGFIYAASLMGVTGARTSVSVNAKQLVERIRSVSNKPIAVGLGVSTSQQAQEVATYADGVIVGSAFIKIVQEFGAGRNGLKKIKQLAKSLSEGIKSAR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
EC: 4.2.1.20
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Length: 267
Sequence Mass (Da): 28526
|
A0A6I3D3G1 | MALDATDPPEKPGGTAPHVIVDEIDDPVMCVEDVHHLSKVRRLRNGDLVSATDGRGSWRWCAFENASLSVVGDITVEAAPSPRLTVGFALVKGSKPELVVQKLTELGIDSIIPFIAERSVVRWDDAKTERQGERLVKVAREASMQSRRVWLPTVAPVARLSDLISSEGVVRADRDGRALSSGDTTVLIGPEGGWSPAEADMTSVVGLGHTVLRAETAAIAAATLMVALRDGFVA | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 234
Sequence Mass (Da): 24952
|
J7HKL5 | MESRFKLKVESHQSCCAILERGPVIKISSTKPRTRHYESGLKKMPNSSSSKVPSIKAQHRIAKKRAVRRRRIDLDCGCSIYIHINCAKDGNGFTHMGRHHCASGREFRFYLGGSKSPLFQDVQRGGSTLHAHKDIPHSNPVQPQPEESTKSSQSVPELPSLDGIDSSFWDDIFE | Function: Strong activator of the late viral genes promoters. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. Also suppresses the host basal defense by interacting with and inhibiting SNF1 kinase, a key regulator of cell metabolism implicated in innate antiviral defense. Determines pathogenicity.
Subcellular Location: Cytoplasm
Sequence Length: 174
Domain: The zinc finger and the transactivation region are involved in PTGS suppression.
Sequence Mass (Da): 19556
|
Q14Q27 | MLISEKFIDNYAAALMDLALETKKNDHFLEVSNIIVELFKQEPDYIKLMMNADIPKEERKNILAKPFQKVIDPLILNALFLLIDREAFCYVRRIFKRLRKLINISYDVQYGNIYSTQPLTKKQITTIETKLSKKFGYHIELVNKIDSSLLGGVRIKIKHEIIDGSIAGQLETMRQKAIHNK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 181
Sequence Mass (Da): 21054
Location Topology: Peripheral membrane protein
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A0A1Y1L6Z0 | MILIHKHEDNLYIFIRDWLIHYNYTTSTYTEFQIHQPTDVREKLSEDRNVAAVSASKDNRLIAVTLCNKQLVIYDEKLNVIANVVCKRAACALTFTDDDDLLIADKTGDVFVYKLDRQPELLLGHLSMLLDVAVSECGRYVITCDRDEKIRVSHYPDSYNIASYCLGHEEFVTHLKMYGDILISAGGDGTVRFWDFVNGRQLNVVNTNDHLPDKAVVAEFRKEMGVENADVTALPIVDLQVYKSEQSAYLGVRLLGSDSVQVYRLQNASDVRLVDVLTVPSLLAFHLGERLLVVTERGFLHYTVAPNKLTKTDVSDACFEKCEHLLKDHVSQSKSLFCNLYKRKYDNVQEYLEKKKMRIENKS | 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: 363
Sequence Mass (Da): 41524
|
A0A7C2ZRS8 | MFRLGLYKVEVIITYRKELRDPESEIIHKDLILKKGYANVKKVTTGKYFSMLVESDTKENAISTVRELCEKLRIYNPIAQEIEVFVRE | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2.
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Catalytic Activity: ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate
EC: 6.3.5.3
Subcellular Location: Cytoplasm
Sequence Length: 88
Sequence Mass (Da): 10382
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A0A6I3CH83 | MKALFVALGAGLGAPARYVVDYYVKRAHSSLIPYETLGINILGSFILGLVIDGNQNVSLLLGTGFAGAFTTWSTLSVEQHSLLKNKRYLAAVTYLIATLVLGVGAAALGIYLTK | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Cell membrane
Sequence Length: 114
Sequence Mass (Da): 12047
Location Topology: Multi-pass membrane protein
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V2YEB6 | MSDTMNLFEKAPVPQAVLKNALPAMAAMLMVLIYNLADTFFISQTRSDILVAAVSLATPVFLIFMAVGTVFGIGGTSVISRAFGQGRAEHAKKVCSFCMWGCVAVGIIMSLAFLFFMDQILTLIGASTDTWEPTKTYLTIVALGGPFVLISVCYSNVLRAEGQPNKAMAGQVLGNLLNVILDPIMILAFNWGIAGAAIATVIGNVAGAGYYILYFLQGKSTLSIHIRDFSVKDQIFTGVLAIGIPASLGSLLMSVSQIIVNARMAGYGDMAVAGMGVAMKVTMMTGMVCIGFGQGVQPLLGYCVGAKLWERFKKIMRFSIFFSLALSAVMTGLCYLLRGSIIRVFLTEPASFDYALTFTNILLTTSFLFGPFVDNLERQRQFVTDASHELKTPLAILSADMGLLEDTYGEDKWLESAKSQITRLDRLIKNLVELARTEETIKEDAVELFSISEIAQASADTFQPLAEADGKTLTSEIPDEISLKGVQDNFFRLFSILLDNAVKYCDPVGNIHLSVSVWGRNIYISVSNPCAGVDTAQLSRYFDRFYRADSSRARSTGGYGIGLSTAKAIVTRHKGRISNHYADGVITFTAVIPQMS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell membrane
Sequence Length: 596
Sequence Mass (Da): 64639
Location Topology: Multi-pass membrane protein
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A0A6I3HR18 | MTIETIVAELTAANLDVRTDVPLAPLTTYGVGGHGACVVKVTSTDQAISVGSILRRFPDVETLVIGRGSNLLVADSGFNGVVIVMSPSVTDKEVAINGDVVEANGSMLMPVLARRSVGAGRGGLEWCVGIPGTVGGAIRMNAGGHGADMASAVVDATVLSLRTGQTALVDAQRLGFFFRGSALLSHHVLLSVRLLTIAQDAAIGTNVINEVVGWRREHQPGGRNAGSVFVNPGSGDDSSGALIDSSGLRGFTIGAVQVSEKHANFIQAAEGATAADIAAVMAHVQSTVESAHGIRLYSEVCLVGFSSDLMTRFTHPSHTAVEHVAAKEELQRLLGERA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 338
Sequence Mass (Da): 34952
|
A0A673M858 | MMSLKELCAYETPSVAEMQNFMLADRRPTGHVNQVWPNVYIGNEVAARDKSMLYNMGITHIVNAASGPPHVNTGPRFYRDMDIDYYGVEADDSSDFILSVFFYPTARFIRAALSKNGRVFVHCLMGVSRSATLVLAFLMICEDLTLMEAIKAVRQHRDICPNPGFLNQLRHLDMSLVRERKKKLEAYKL | Function: Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (By similarity). Involved in the modulation of AMPK and MAPK1/2 signaling pathways.
EC: 3.1.3.16
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Length: 189
Sequence Mass (Da): 21539
|
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