ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A3D8LE79 | MTQKLKVAIQGGPASFHEVAAQQYFPQHEVASVPCQSFRQLCEVLEQRKADQAVMAVENTLAGSILPNYNLLHQFNLFVTGELWLPIEQNLMALPGQQLQDLIKVVTHPMALNQCMEFLTQQPQLQLQESHDTADSAKEIREKGLEGVAAIASKQAAALYGLEMLAENIEDRRDNFTRFLVVNREQPQERETYINKATLLLQVSHEGSLADVFSQLHTHDIHVALIQTLPATARSHAHYMVIELEGTSSENLKETIDTLKPLVEYQRLLGLYQKTKYPEHPNPKKKVNSLLQH | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 293
Sequence Mass (Da): 33119
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A0A5N9EEI6 | MIENYLPIVVVFVLVAGFVFVSLVLTHLIGPRVYNPVKMMPYESGVDQVGETRIRFSIRFFLIALLFIIFDIEIIFLYPWAI | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 82
Sequence Mass (Da): 9525
Location Topology: ... |
A0A7X2KFH0 | MDYRPYYPYPLRLLSQLVDLLLIGFGASIVTIVFVNAALRGFGGFDLAWSLELSAFLMLWVTFLGCAAAAARGIHMRVTEIIAFAAPKAAQRMIALLIDIGVIALLITLIWHGINISIHTWAQQTTVLYWPVGLLYASMPAGITLTLLFLIWNIVVQASHLKQPPDDGSRPLPPESHEGLA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 181
Sequence Mass (Da): 19881
Location Topology: Multi-pass membrane protein
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A0A5N9EEC0 | MTEIVSVAQTDLKWPKYTGKVRDTYDLGGGFLLIISTDRISAFDVTRAEMGI | 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-(... |
A0A7X2FW47 | MTTTRKTASARSIIRQFGEQEYAGELCAVTSFGTESAVLLHLVADIDPALPVRFIDTGRHFPETLTYRDLLVGRLGLKNFVSLHPSPAVIDRSDREGQLHMLDPDLCCRIRKTDPFAELSRRFRAVLTGRKRHHGGERTTLPMVEVVDGLVRIHPLADWTAGDMNRYRLLHDLPPHPLAARGYSSIGCAPCTTRTVQGESARAGRWRGVTKTECGIHLPPVSTGK | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate.
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
EC: 1.8.4.10
Subcellular Location: Cytoplasm
Catalytic Activity: [t... |
A0A5N9DTT5 | MAPNLSDLLISISRRKNLVNQRLDFGDVCLVCDKSLSESMFFKQYHVCEHCNFHYTMDARQRINWISDPDTFQESDKLVYSADPLEFKTRLTYKKKLSGDSERTGLTEAAVTGVCEIGGVPAQLIVLDFGFMGGSMGCVVGEKVALALERSYKKKIACVAVITSGGNRFQEGVLSLMQMAKTVTVANQLKTKGIPFISILSNPSTGHTFASFPNLSDIILGEPGAMVGLQSLQVVRKESLDVLPDSANTSEFHLKHGMIDAVVERPKLKETVSNILDLLSSEYKISRKVNRSTRSTRKVSINKLNNNVWDIVQIARHDSR... | Pathway: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.
Function: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase ... |
A0A2A4SBF3 | GDPSPRNIRKNAFDVGEYGIGNLANSLTLGCDCLGQIYYFDAALNDSRGKAVQIQNAVCLHEEDFGILWKHVDWRTGKAEVRRSRRLVVSFISTVGNYEYGFFWYFYQDGHIEFQVKLTGIVNNAAVDSQEFPKYGTLIAPQLAAHIHQHFFSIRLDMSVDGLNNSVYEVNTKADPKGPGNPQGNAFYAEQTLLATELEAQRTVDPLSGRYWLISNPSVQNKLGQLVSYKLVPRENILPFAHPESTVSKRAGFMRKHLWVTPFKPDEMGAAGPYPNQHPGGAGLPEWTKEDRAVDDTDIVVWYTLGHHHVPRPEDWPVMP... | 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: 354
Sequence Mass (Da): 39730
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A0A3M9XP88 | MDGGRRILRSLRESFSARHSLVPIVPGDAPYALASAAVATIPPAAVPAAAAAVAPRASARRTRGERLLSRLALLGRPGVGALATLALFAAIGAAGFVENGGYAALVASEGELYDIAARVAGFPISAVTITGQSRLTERELLDAAGVGPRNSLPFLDATAVRDRLMQVPLVKSARVMKLYPDRLVIAIEERQPSALWQRDGRVAVISEDGVPIDELRDQRYLGLPFVVGEGAQKRLLEFLMLMTKAGDLAHRIKAGVLVAGRRWNFEMTNGVTVKLPEIGPSGALETLARLQREARILDKDVMFIDLRIPDRVSVRLTEEA... | Function: Essential cell division protein.
Subcellular Location: Cell inner membrane
Sequence Length: 338
Sequence Mass (Da): 36104
Location Topology: Single-pass type II membrane protein
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A0A0M0BQF1 | MDNPYYIEKQRRIPIVHDVDVAVAGGGCAGTMAAVAAARNGADTLLIERYGFLGGAATAQYVPLLALWNLSPWADEEKPLIGGLAQEICERLDEVGGSIRPEEAFKAQKRGDFPSIWFHHDFELMKLVKQELCEEAGVNFLLHAYIASSIVEDDTVRGLIVENKSGRQAVMAKVVVDATGDGDVAARAGADFEQTKGSRIVDGVERGVMVVSNKAILANVDVAKLRGALKRNPNLIRDLMAEKVPDIIDDTVFYPPYGDKPPVYKGPRPGKLPEPYQSDPKYYAVTRPGEGAIGLINSYGRDVTDAEDMTEAELEIRSKI... | Pathway: Cofactor metabolism; coenzyme M-coenzyme B heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide: step 1/1.
Function: Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B).
EC: 1.8.... |
A0A7X2KEE3 | MQELPKIFENLRQTAFDVFSTILNYLPDLLGAALLVLVGWFVAKFARRGMRRLGDLINRGLDSFLTKGSLARFRLSVAAISLLANISFWLVIFIFFSAATNVAGLDAFSSWLDDIVSYLPTVLAGIMIVLVGFLVSTFVRDLTVSAAATARFSQADLFGSMAQGITLLIATVIGLDQIGVDVTFLVIILAVAFAAILAGFALAFGLGARDLTANLIAAHYLKEDVEPGQQVRIGKIEGVVIEITPTSFVLDTEAGRTVIPATLAQNSTVTILAGDDSDE | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A7S4RTP0 | MRPRKRRRAAAAAATSDHEEEEEEAPAPADDAAEQGKQGKQGKWKPVEMDLELMQAFESEGGVFLEETTEAAVMYGDSLIGDEPGAAPERPEAALEQGGRKGKRGKKRQAPEEQAAGASPKQPEAAPPDGKKVGKKKIKAKRRAAAKPPAGAAAPPKEAAPAKSLNFEHGTSGAQEEVSQEALAEKLPAWAPFGLHPLLLAGLLQLQFEKPTEVQARCLTPALLQRKDIVGAAETGSGKTLAFGLPILHHTLSNMDAPGAESAAGGGHLPSAARQLKAVVVLPTRELAVQVQSHLNAVAQRTPLRAQCVVGGMSAHKQRR... | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 791
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): 86502
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A0A1H0YXA4 | MAEQRVMSSGGAKRPGGAGSGGGKDDAGDDAGAKKGGKKKLLLVVAAVLVAAGAAWFFLKPAPAEAEAEPEPVPGEVLALEPVSINLADGHYLKLGLALQLVEGAGAHAPIDGSKALDSAITLFSGRSVEELADPVHREELKTELGHTLEEAYHHEVIDVYLTEYVTQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 168
Sequence Mass (Da): 17374
Location Topology: Single-pass membrane protein
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A0A0M0BLR6 | MHLRAHEYWLLLKPRILLAMVALYSTSYIASFASLGQAPFDFPHFVIGFVAVSLAVSGSNALNCYLDRDIDALMVRTRRRPIPRGVVEPKVALVFGLLLLASAAAISLYLGVVPFLLLIIEGAGFYLVAYTILLKRRTSLNVLATAPSVAAPSWFGWFMGGAPFNAQALILGLIVAVWGPLHLWTIAYTFAEDYLRGEVPMLPSVLSPGRAVYSIVVSLLVLVSSTYFLAFLAGSILFTLAVSVINIPLLFVGARFYVTPSKRRGWWIFKLTAPYIVIVLSAFMIDKYLSV | Pathway: Porphyrin-containing compound metabolism; heme O biosynthesis; heme O from protoheme: step 1/1.
Function: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + ... |
A0A7X2KDY9 | MFAALDHLLDRLSMLYLRLSQLLLAGLVLAVFAQVIWRYAFEKSFLGLEELTALALVWVVFPMSVILHRRGRHICVSVLSDLFGPGLKRLAGIIISLGVILLVLFVLYQLWQVWPYLRLKSPVFGIPDIAFKVAPAFAFIPIALQELLHLAGRRSDARPPAA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 162
Sequence Mass (Da): 18174
Location Topology: Multi-pass membrane protein
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K2KFV4 | MLKSISLAATIAIGGLLSSSALAQQLPVAHQQQVTAQGKPLTLLGHAVKVGDQAPTFTVVDQSFKPVSLSDLNDKPLLISVVPSIDTGVCSIQTKHFNQAVEELPKAVTLVTISTDLPFAQKRFCGAEGIESMQVLSDAVWRSFGESYGVLIKDMGLLSRAIFVIDQQGKISYQELVPELGQEPNYDQALAALQKLL | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
EC: 1.11.1.24
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxi... |
A0A7S4VYF7 | MASTDMKSLLLAAAGGVAVGALLMKLSKKAPSGFLGKVEEATAAVGQDNLLSPKSAKAFLDANPGCLYLDVQDPGSPSVPGTHKASLGTLIFKASTDLADFKDPKIADLPKGHPILVTCALGGQAKVGAKLLVDYGFTNVKVVEGGCVAWKKEMPYPIEAVCEVSPQGKPCGGGNDTSICTGTITLKQTSAEECSISYEIRGLTPGKHGFHIHEKADFSDGCNSAGPHYNPFKKTHGAPSDEERHVGDLGNIEPGPDGIARGTIVDKLVKLSGETSVIGRSFMVHADEDDLGLGDNSQPGPPPVNGKASKTTGNAGARIA... | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
EC: 1.15.1.1
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Length: 330
Sequence Mass (Da): 34055
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A0A0M4KCG7 | MRIAIHDILWLDQPGCDDPARVGGKAANLARLAARCPVPPGFALTAEAHLRSAGDSLPDDLARAVADAYATLGARCGAPDPAVAVRSSAVDEDGASASFAGIFASYLNVRGLDEVLAAIVRCWRSAADPRVVAYRRERGGDSLGVGVLVQALVAADTAAVVFSVNPTSGAADELVINANWGLGESIVGGLATPDTWILRRPALSTIRFRLGDKTQMTVRADGGTHEVPVLRTLRARACLSDAQVHELGGLALRLEDAMGWPVDLECAYEGGRLYLLQCRPITALRRPGP | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
EC: 2.7.9.2
Catalytic Activity: ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate + phosphoenolpyruvate
Sequence Length: 289
Sequence Mass (Da): 30395
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A0A1H1MNM0 | MLLGVIQRRTGPFKEEKLAEMFDAGRNKGSVRELPCHLVDPEVFFAEQPADVEYAKSLCMSCPIQEACLASAQDRREPWGVWGGQLIVQGEIVARKRPRGRPRKHPLPEPEIAPAVARRWELPRERRGHGRQVRSGGERAA | PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO).
Cofactor: Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Function: Acts as a transcriptional regulator. Probably redox-responsive. The apo- but not holo-form probably binds DNA... |
X8JMQ6 | MPPEALPQSNDPDASSKPRNGSPSLYSLRTIPIASASHSPTSPRLEELTHGSNETSSLLSGSGNQRSYTGLAKYMPALDPDARKLVFRAGLKVLLLFIVGSIVLGGTLWVALPTLDEADRPMLRIPKSFAQLQDLNTLLKKYRDVYPYRIFVCYTITYLYLQAFSLPGSMYLSILGGAVWGVPRALPLACSCVATGATLCYLISAALGPALLAVPSWRARLDAWSEKIEAQRDNLMSYLIVIRIAPFPPHWVVNVLCPHVGIGIPRFWISTFLGIMGVSVIHTTIGGKSNFAPLFHFFFLPMGMGCRDGRIRQTERFVDL... | Function: Golgi membrane protein involved in vesicular trafficking and spindle migration.
Subcellular Location: Membrane
Sequence Length: 353
Sequence Mass (Da): 38893
Location Topology: Multi-pass membrane protein
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A0A7S4VYN2 | QRQALQQFCPLRPNRRSQAASGSWAASSIDAQDLRDINLPCAPAGSPVPEENNLKMAASSPSSLALAMEVVPVPVANLSLTNRVYASRAAAERLWPTTPFASANWRRVTVNGFTFSLDELDIPDGQLAMNRLQRRYMRLGVGTSVRVQKREASAHAGLAAITMSVRRWTGSRETEARIDRDAFARQVRAQLNGQVLAPTQELALEWESGWMTLTVLSASSSSGGGGGGG | 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 p... |
A0A024W9T3 | MSTQTRTKGWEKESKINPDYEYERLLKLEKKFHIKAWINKGEKEGYLYNIVPTTMNVVAKNSNKSHKKTGVHMYFVSDNNKTWRLTLFYRPYFYLKTKNIHNYEQVTKFLKKELDKYNVEIDYVKKEDLSLYDHLNKKRSYLSNIFFKLSYDTIENLMNARDFLVKIIERNKKQNKNYNNSNNDKHIFNNEDLSYSQLEFSYKNEYSYNKYDDQKENTQKQQFTTNITEEDDKKRILNAKSNDNNNNNNNNNTHNSNNNNNILNMNDIIVTTKKQILSKEEIMNEIIEIYEYDVKYLTRICIDKNIRCGLWYKVKREEDE... | Function: DNA polymerase II participates in chromosomal DNA replication.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
EC: 2.7.7.7
Subcellular Location: Nucleus
Sequence Length: 815
Sequence Mass (Da): 97376
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C4KYP9 | MITLPTGLIVSCQALEGEPLHSEFIMGRMAIAAVQGGAKGIRANSARDIQEIKKHVTVPIIGIVKRDYEDSDVFITATMKEIEELMEVGVDAIALDATKRPRPGNLSLQELVHAIRSIYPNQLLMADCATLEDCIEADRLGFDYISTTLHGYTDETKGSLLYHDDFKFLKDVLDHVTQPVVAEGNILTPEMAKRCMDLGTHAVVVGGAITRPHQITARFDAALTSSVKSPL | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
Function: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
EC: 5.1.3.9
Catalytic Activity: an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-... |
A0A5N9B2R0 | MDSRTIIDRCFTDNIATIEKVRNQNTQEIESIADMVYRTFNNNKRIFFCGNGGSAADCQHMAAEYVGRFKKERKGYPAIALTVDTSIITSVSNDYSFETIFARQLEALAVPGDLLIAYSTSGNSKNIIEVLKKAKSMGITSIGMTGQSGGDMNKLTDTLIKIPSNITARIQEAHLLLGHIVCEIVDQRLN | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1.
Function: Catalyzes the isomerization of sedoheptulose 7-ph... |
A0A455V779 | MSQLMTRTRIKFCGLTRPEDIAKAVALGVDALGFVMWPKSSRSITPEALRVLAAQVPAFVTRVGLFVNQPAELIEQCLPHLDLIQFHGDESAAFCQQFGRPWIKALRMRDDIDLHEAAKSTRRRKRCC | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 128
Sequence Mass (Da): 14466
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A0A0P7WYN8 | MAENELNTPKPGEPDASASSGSGKSSKFLAFGKYFLLLAAVVFQIGAAYTLVDENYERIYVSVFGGLPDFSAEYPMEDIVVNPARSNGQRFLVIGMSLELYHHDHIPLLERNLTNIKENLMRIAASRSVNELVAFEEREVMREEMINEINEITGVSSVRNLYFTRYIMQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 169
Sequence Mass (Da): 19077
Location Topology: Single-pass membrane protein
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A0A0P7Z9R1 | MDLAAILFYVFALVTIGSAAVVVFSRNIVHAAFSLMFTLMGVAALYVLLYADFLAATQLLVYVGGILILILFGVMLTSQGYTLNFREATVNVVPAGLLSVAAAILLIYAFSTGGWVITEVDERTDTVYDLGMMLMTDYLLVFIVAGVLLLVAIIGAIVMSTRLSVNTED | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
A0A8H2VIF4 | MNKLAMGNKPKLHTFIYRLNRGNSRWQHTSSIPFRDRIELHNRKYIMKRHNFFSKHDSRYNGNIQENLLTYDPILTQCIARWLWLNYKITDYPYYDLNILNIFTDLPQSIYFMKQIMKYYHETLPFESFDKINYYLFPLYKCNNINKQSLLDDIPGNVHIMEDTTLFPINKNINFNEQTSNMYINDPVQILMFNDVLGKLAHDLVRYNPYKQSLEQCYVEENGNINKKQYSSKLDYWCELTLRQLHNNDHDHFSINENILGNNTYPMDEVSIPSQFIQLLEQLKFNAPDLRLFMIDSPKIVTKPIIQKLKRFFSRRKRYL... | Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subcellular Location: Mitochondrion
Sequence Length: 431
Sequence Mass (Da): 51217
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W4IUH1 | MVKKKTSVNVKSILETKNKREKKDEDDDEDNKTNKLYNNLYKRNKSIRINILDKNENNGEGISLSSEKQKVSFKKKNNNYDINESDGVGDYGDDECEEESEIENEDIINNKNNTNNINNINITNNINNTNNFDNTNNIDNTNNIGNTNNIQINNILERNSKEKSLYKEELTTNIQNGENNTVQFFNFKKYDYNPDRKKTRDDLNDDNENSCSSFTRRGKYNKTKTIKKSNKLKLTNTHENLLSDHHDYTSLKVNYKINKKSNYDKTKKRPFLSITFNEKQNRPVNRSSVCTDNAKFLSFLNDYERKTYLIKNRKRFNEKK... | Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
EC: 3.4.21.105
Subcellular Location: Membrane
Sequence Length: 694
Sequence Mass (Da): 81815
Location Topology: Multi-pass membrane protein
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A0A510J5L1 | MSFLERALPERWRGALILQALCGLIVLGLITWYGGKLAWQEYQWESLSPGLGLPQWWYLVWLPILSAAMLWRLVQQTRDRLKGELTSDA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 89
Sequence Mass (Da): 10329
Location Topology: Multi-pass membrane protein
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A0A2Z3YNT4 | MTNSVTGTGSGATPPIAFVVAGSEATGGAGFQVDLKTFQQLGVYGVGALSCIVAFNPADGWAHRFHPVDPVIIAEQFEAALAAHSPERMNTAKVGMLGTPATIDVVAEKLAGRDWKNLVLDPVLICKGQEPGAALDTDNALKEKILPLATVVTPNVFEATSLSGMDHIDTVDELAEAAKRIGEKVPYVLAKGGVELPGEDAVDVLWDGHEITRFTAPKIGEQRVSGAGCTVAAALTAELAKGSDILTAVDTAKKMVTRGIEHRVSANTPFDTVWQGA | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3.
Function: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P.
Catalytic Activity: 4-amino-2-meth... |
A0A455UWZ0 | MSHNTNQDPNGLKDDVLAASSTPESIADGVDEEVVEPNRRLFVGWQFLLFAALAIAYSGFHLFSLNVYPMETWSFRIVHIAGALILGYGLFAGARFAEDDQQASPAWLKWVSYALLVPAVYSLVQVFLMQQAINGGAMRIDPAVETLHFGYPLMATTAGAIVLSWFYRQARHRLNPADLVLMVCALASAGYLLMAFNTSMRMSTGTSFAPPGISWAAIAGSLLILELTRRVAGLALVVISAVFLTYVFAGPYLPGFLGYPGLSVQRFFSQVYTDAGILGPTTAVSSTYIILFIIFAAFLQASKVGDYFVNFAFAAAGRAR... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 406
Sequence Mass (Da): 43304
Location Topology: Multi-pass membrane protein
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A9HJD9 | MTPSRLIASFGGCGFSPFAPGTVGSLAALACGLGLLAHPLALAVAIVLCCAIGYVATARASGGVDHGWIVIDEVAGMWITMFPLSLPPTPVHPWAPDRIGVLWLVLAFALFRLFDITKPGPVGWFDRRHDAVGIMGDDIVAGLIGAFILAAIRCLIVMT | Pathway: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
Function: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate... |
A0A7S4VSF2 | MAVEWQQFFRQVRGKLAGAWGRHPLVLAKGEAALRGRLTLADVAPLVDSGLLPAGCAALGAGARDWRSVPLSGPLAEVLPSATAYANNAGLYLSTLAEVCLAAVQVLGWPTTCNAYLSGSGLAVSVPPHTDRQDVLVLQTSGRKRWTVFAPPAVGPVDPLRRGKDGDAMLEAELGEHLMDVTLSAGDALYVPLGFPHSTSTLLGGAGADEEPSVHITLNLDSLIWGLSYRMLWIVALRRARLRRGMSDPPEEGRGTEGMTWQRYAALQAPLPLGFVEEEAAGACVQGLAGDLSRRVADWTGGEVPQSEELGEGDVEAALA... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 374
Sequence Mass (Da): 40252
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C4L431 | MYHIKTFNQIAAAGLKRFEPSEYVINASDQADAWVLRSHQVHEEDIPPYLLAIARAGAGVNNLPLDQLAKRGIVAFHTPGANANAVKELVLASMILSVRPIVKGFNWVNEQTTASQSQLEEAMELQKRQFLGAELRGKKVGIIGLGAIGASLANDLLQLGVDVIGYDPHLSVDAAWNISKHVTRAKHLSEVLGNVDLLSIHMPLTEETRFSIDRSWFERMKPGMTVLNFARGELVKDDDLLKAFHHHVGLYVTDFPRHTLIGHPQVMALPHLGASTKESEVNCAIQAVETLKLYLETGNIRSSANFPNVELPYTGKRRLG... | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3.
Function: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydrox... |
A4ZG61 | GLFLAMHYTADTSMAFSSVAHICRDVNNGWLLRNLHANGASFFFICIYLHIGRGVYYGSFLFKETWNVGVVLLFLVMATAFVGYVLP | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membra... |
A0A351KRL9 | MRSSQKAIGIAPLTLRAAWGREPWQLLLLGFIALATRFTGLGYPATVVFDEVHWGRYFSSYFTGNYYFDVHPPLGKLIYAGWAWLWGFRPGFAFESYAAYPEDWALVLRILPALIGSLLPLIVYRLGLDFGLRKGCAFLAGFLVAIDGALVDISRFVLLDPLLLTFGFGALLAHRHWSRTKAVRWLLLSGGLAGLTFSIKWTGATFLALMVIFELSSLWRWREVTLGVPLLWRLLGLVLIPATLYILQFWLHFSLLDHSGTGDAFMTPAFQATLRESLYAKDPVLEPPDFWEKFLELNRMMYQANAGMTAGHPYSSKWYS... | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A6H0JPU2 | GLTTNLLTMYQWWRDIIRESTFQGHHTSAVQKGLRYGMILFIISEVXXXXXFFWAFYHSXXXXXXXXXXXXXXXXXXXLNPMEVPLLNTSVLLAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXISXXXXXXXXXVATGFHGLHVIIGXXXXXXXXXXXXXXXXXXNHHFGFEAAAWYWXFVD | Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... |
A0A0A6ZCD1 | GGFGNWLVPLMISSPDMAFPRMNNMSFWLLPPSLVLLLSSSLVESGVGTGWTVYPPLADNISHSGASVDLAIFSLHLAGASSILGAANFISTVLNMRPSSMHMDMMSLFSWSVFITAILLLLSLPVLAGGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
D5JK70 | TLYFIFGIWAGMVGTSLSLMIRTELGTPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLILLISSSIVENGAGTGWTVYPPLSSNIAHSGSSVDLAIFSLHLAGISSILGAINFITTIINMRINNMSFDQMPLFVWAVGITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFW | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A0M0BL17 | MTVILDGRETASTVMEELKEQSERLKEKGVTPTLALVLVGDDKYSMRYVKMKMSRCGEAGVEAQLHHLQETTQEELLNLIEKLNEDDAVHGVMVQLPLPEGFDELSTVEAISPEKDVDGLSPATLGKLLMGEECFPPAGVEAIIELLRRHDIAPEDKHWVIAGLSTIVGKPLAALLTNMNVSVTCLQADHPDLARYAREADVLVVDVGRKWAVTADMVKRGAVVVDNGNNYEGKKVYGDVDFDGVKEIASAITPVPGGVGPLLIAILIKNTLKAAARSSV | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate +... |
A0A5R9NZ38 | MRKSILLATSALALLASGAVASAADAVPTPEAAVAAEGSSYVRVCDAFGTGYFYIPGSEACLRVGGQIEFSAGYDSFQDEGYTATEARIDIETAQDSEFGAIKTKLRISSDVNLDGYTIPSAWGAGVDRDTQLEIATISVGGFYVGYAETLINTDVLYGDMLDLETFGDLNSTAIGYLSGDLGGGVYAGFAVEDARRGGGADFARFGENDKPDLAGRVGVKQAWGTFDVSGLYGTENENWFVKATADLDVVENAGFRLTAGYGDAGKDSSDDAWFVAGAGKYNFTQSILGFAGVGYGEENDFDGVSANAGAVWTPVAGLD... | Function: Forms passive diffusion pores that allow small molecular weight hydrophilic materials across the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 347
Domain: Consists of 16-stranded beta-barrel sheets, with large surface-exposed loops, that form a transmembrane pore at the center of ... |
G8EXH4 | MTESTSEYGLDRPRRVAVIGVTGSVGRQAVEVIERSPRLEMVGAVALRDAGGLAAAGARLGCEHLALIETATDDRRSWADPTPERFLHAVKPDVVLNAVVGVAGLAWTLAAIDAGHDIALANKESLVAGGRVVNERLAASSSRLLPVDSEHAALHQLLEGHRHHAQTLTITASGGPFRGRRWADLHDVTVEAAMAHPTWAMGNKNTLDSATLVNKGLELIEASYMFDWPQERIEIAVQPRSVIHAAITLRDGTHVANVSPPDMRRSIAYALHHPECVDIGLPHVPLAGLGTLELEPEPEDFPGLALSRAALRAQDHGGTA... | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
Function: Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
EC: 1.1... |
A0A1B8QVV2 | MKKTLAALIIGAFAASAANATVIYNNEGTKVELNGSLRINLEKSNQDGINKSKTTKRHSHSGLQNDGSRFEIKARHDLGDGYYALARTEVRFDGDEKGLKKKDNDGFGNLTTKRAYVGLGHKEFGQVTFGRQVTIVDDVVTAEDKTYGLIEQGDYVSKEGKSVVRYDYYGIEGLQLGVGYQFAEQRKDNNEVLEGSVQNSNQFGALYEKDGIIAKTAFGRTNYKTGNTETKEHRDGVVASLGYEFNGVTLSVDGGYAKTKFKDTDKKETRFFVSPGFQYQITDLSKVYGNYKYEQIKGTDSSKDKQHGFLLGIDYKLHKQ... | Function: Forms pores that allow passive diffusion of small molecules across the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 360
Sequence Mass (Da): 40147
Location Topology: Multi-pass membrane protein
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A0A7S4Q8N6 | ATPGHAPGGRRARVGPGGEMGDTTPDICEVGGGGNILPLFGDAEQNWPMALRGILYLLGLGWCFMGVALIADVFMGAIDKITSQKTRVENPDTGRKITVPVWNPTVANLTLMALGSSAPEILLSVIELMSNSFFSGALGPSTIVGSAAFNLLCISAVCVVTIPDKEKRTIKEVPVYCITASFSIFAYLWLLVILLGTSKDVIEIWEGVLTFLFFPIMVILAYLADRGYFSKVLQVSRSSREGLLGGAHGGGIILGSHTNKEELAELTAAIRRRHGADLPDEKVAKLVAREFGSRPTRAQYRVQATRGLTGGKRVAMGAQS... | Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Subcellular Location: Cell membrane
Sequence Length: 858
Sequence Mass (Da): 92529
Location Topology: Multi-pass membrane protein
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A0A8H6S5X3 | MPLIGTSFDAHPGAYFTTLEELDTWANTPHRKHGVLMYHPRPVSTDERAKLLVCHDYKGGYNESPIALGYTFNFWSAVDTFIYFSHHRVTVPPPGWITTAHRQGVKMLGTLIFEGSGENDCLRLLVGRLPQSKSGPASQPTDFRSLPLSPHYARVLANLADERGFDGYLLNFECPLRGGIEQTRSVAAWITLLVSELKSKIGAHAEVIWYDSVVVNGQLAWQDRLNGFNLPFFLSSTGFFTNYTWPPSHVTRMKQYLTTVASTSLSAQDIYVGIDVFGRGSHGAGGFGSYKALEHISPAQLSTAFFAPGWTWENTQDAPS... | Catalytic Activity: an N(4)-(oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc)-L-asparaginyl-[protein] + H2O = an oligosaccharide-(1->3)-[oligosaccharide-(1->6)]-beta-D-Man-(1->4)-D-GlcNAc + N(4)-(N-acetyl-beta-D-glucosaminyl)-L-asparaginyl-[protein]
EC: 3.2.1.96
Sub... |
A0A1X7FWC6 | MRSRALDRIVDAYFKLLEFILFLCMTGMVVTVFGNVVLRYGFNSGILVSEELSRFLFVWMTFIGAVVVLRERGHLGMDTVVNMLPLAGAKGAKAISDLLIIACCIYIVSGTWQQHDVNMDNLSPVLMIPMEYVYSVAYISGFSMMAITTVSLVSTFLPGAGDPRQSMFVDAEEKAALNSVGTVRGESDP | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 189
Sequence Mass (Da): 20753
Location Topology: Multi-pass membrane protein
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A0A519K9U4 | MQTTYIETQQISFQDFKNQILEDYKLGRISREMSYLGRREVLTGKAKFGIFGDGKELPQLAMAKVFRNGDFRSGYYRDQTFALAVDALSVESFFAQLYADTSVEREPASAGRQMNGHFATRSLNEDGSWKDLTAQKNISSDISPTAGQMPRLLGLAQASKIYKTVKFDGSEKFSNEGNEIAFGTIGDASTAEGHFWETLNAACALQVPMIVSIWDDGYGISVPTMKQRAKADISEMLSGFQRKEGENQGCEIIQVKAWDYPALLDAYAKAEHFARTESVPVVVHVIEVTQPQGHSTSGSHERYKNEDRLSWEADFDGLVK... | 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... |
A0A8H6SN03 | MHQLLKDWKFTQIGGGKGTKEGEWLPVSTFPTTVHVELLKLKKIPDPFLGLAEWDVQWVGESKWAFKTDFVVEPTKAANVDLVFEGLDTFSAILLNGVELIKTNNQFVSYRVPVKDHLKEGGNELVINFDSAFVTGRAIEKAHEKLNLWNGDSSRLHVRKAQYNYGWDWGPILMTTGPWKPISIHTYDNRITDADIRAQVTDSLAANLSATFSFSGEQEAFASFVLKGPDGSTEFSDDKPARSLQDGRVDISISFPEGKIKLWYPVNYGEQPIYTAELTVLDAAGNVLDSIVQKIGFRNVKVVEEPLVDQEGLTFLFQVN... | Pathway: Glycan metabolism; N-glycan degradation.
Catalytic Activity: Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
EC: 3.2.1.25
Subcellular Location: Secreted
Sequence Length: 872
Sequence Mass (Da): 99080
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A0A843ARZ1 | MIRVDIHTGKAASGRPSMETPFHTGLYRARPEVGAVVHLHPPSSTTLAVIGRNLRPAITPEGVLVLGERVPMIDYATPGTGALADNIVTQLGSCNACLLRSHGALAVGKDIMDAFGRMETLEYIASLQLGCETLGGLDDLPPQEIARMLSKD | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 4.1.2.17
Catalytic Activity: L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone phosphate
Sequence Length: 152
Sequence Mass (Da): 16114
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Q55DA4 | MTLLNNNKPINYIIGSGASEEGSVSDDIKLKQQYSKANQAEVTQLEHDNNNNINNNNNNNNNKNKEDYKVNSRKKDDKIQQEQQQQEQQQQEQQEQQSSFKATSEKELYNTSKEDKAKDLKNRYTSTKRTTEIISVTLFSIFLAISVYRMLTLLFIKNIWIFLSSTVLAMFLADFFSGIVHWAADTWGSLDTPLVGNSFIRSFREHHVVPTQMTHHDVIETNGDNCMLTVPILAITALGNITMDSTYNMFLMSFLVNLCFWVSLTNQIHKWSHTYNVHPFVGFLQKSGIILSKRDHAIHHRNPFDKYYCITNGWLNPWLA... | Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Membrane
Sequence Length: 354
Sequence Mass (Da): 40736
Location Topology: Multi-pass membrane protein
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A0LNQ9 | MKRPLLLCLRLATGTIFIAASIDKIIHPGAFAQIVYNYQVLPNGMINPIAIVLPWIELVMGVLLLAGIWLPGVALLSVLLFLTFFGTLVFNLARGLNVHCGCFTTSPADNPQTTWYVIRDSLFLILGISLCYQVFRRRNG | 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: 140
Sequence Mass (Da): 15520
Location Topology: Multi-pass membrane protein
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A0A353RAS3 | MPEEHHLSFQGKYKKNHRIFVCMIEFHDALHIVLDHAAATGTQGISLDSACGRILALDVNAPSDLPPFSKSAMDGYACRKEDTENGMEVLEVIAAGKLPVHQIVPGTCSKIMTGALIPRGANAVLMVENATLHNRRVYGPRPGSDNIIRQGEDLKAGEPVLRAGTLLQPQHLSLLAMCGITTV | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 183
Sequence Mass (Da):... |
A0A7D4A896 | MPLATELVEVGAEWVGAEPGPPPGPGPALLLTGIAQPGPLRSYLESQGYTIMHHEALPDHHAFQPADLAALQKYWQPGWPVFTTEKDATRLSERTAPGLWAGRPGGRCASTRFRCA | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A7L3D1R0 | IDFKGVNMVINYDLPTSAVEYIHRIGRTGRAGHTGKAITFFTEDDKPLLRSIANVIQRAGCPVPDYIKHFPKLQSKQKKKFIKKPLKRESIRTTPQCFLKKAKRKM | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 106
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): 12199
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A0A7S4V5I0 | MLSTPPVRPPSPDAGLGPGFVCLPDAAEGSPLQGDSHSAPARAKRPAAPLGLLQWRVELADGAVVSLPGVAESLLLQLDEVAWEMSGVRCRGVLFLTDFRLVLQPCGAPIVGLHDAALPLEIPLGAAAECKAERSAARLYAPSGDYSVDQVLIRCHDFRCVRIIAPRRPGRGVAAPLDALVGALQPRLLRPPLAELPGLPSRLFVASMGQPTAQWGLLDWAAEFLRQGADSKRWRPCRINLQFEVCDSYPPLWWVPVGASDDDVQLAFACRARRRGPLLTWHHRGSGSALLRCAQPLGPASDSQYLERARRAVHEDARLV... | Catalytic Activity: 1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
EC: 3.1.3.48
Subcellular Location: Cytoplasm
Sequence Length: 716
Sequence Mass (Da): 79489
Location Topology: Peripheral membrane protein
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A0A840RAM8 | MFYSFSVKKIQLAPRPFSWSPVRKSALALGILWPLTATSGVSSYPDPLPTDRDLSPVPALADVISSDMACTLAPPGSALTLYQAVERALCQSPKTREAWAAIKSQTAQVGISKSALMPHVNASVQWAKEHTYTEVPNSPDLSSGGGTHFRSDVLALEWVLFDFGARYEEMKSAQQLLVAAQQTHAATLQQVFLQTAADYYEAIAAQAAALSTREMEHAAKQSLDTASARVRGGVAAVSDQLQAQTAYAQANYARVKAEGMASTSLGTLALDMGLSPDGHFELAETQDGPLNDISFIKSLSTLLTDARQQHPVILASQAAV... | Function: CyaE is necessary for transport of calmodulin-sensitive adenylate cyclase-hemolysin (cyclolysin).
Subcellular Location: Cell outer membrane
Sequence Length: 498
Sequence Mass (Da): 53660
Location Topology: Peripheral membrane protein
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A0A800GIP0 | SQASVHIGALLMLMALSFVMGGVIERAGLLSDIPTSFSSVWLTLSFLGLALVAIGMIMDPFGAVVLVTGTLAQIAYNNGIDPVHFWMIALVAFELGYLTPPVALNHLLTRQMVGHEEVAKSVLKEGHFWYRHEKILLPMATMATTLLLVAVIPVLIGLWR | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 160
Sequence Mass (Da): 17380
Location Topology: Multi-pass membrane protein
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A0A7S4RFM7 | MAGSGARANTGVKRARSVQKARGGSAAPRLKGRPAGRLVAKPGKARAPRLRPLPPSLPLGPVRPRGRGGALVIGADEAGRGPWAGPVVAAAVALGPVVRGLERGVTDSKRLAEAQRERVYEALTGNPGVHWSVALVGPARIDKVNILRASMEAMARAVRRIPGRVHKVFIDGPHVPGELAEHSCEAVIGGDRKNFAIAAASIIAKVTRDRLMMKLDRKHPQYGFKSHKGYGTAVHHKAIKRHGVLREHRRSYEPVRRLLSQGRGGRQGPGRGSSA | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Seque... |
A0A1Q3EHZ2 | MKAVCFLLLLGAAVQAVKLSVDSVKYSIISAKGEPTTKSLSPTEKSSSEVVTIFQDQTLKLSFQVVDKVTGKGVQPEQAFLRFYDEQSGEEGIQPVRVTSSGKAKFDLSLAKPPASLPPTSSAPLKVTLLLGASSYAPAKLELFNLHIPASHPAPTHPEEAKFHILPELAHTFRPDPKLPARAVSALFAGLVLVVPWTILLGLWFSISPRVPRLFSPNILPFTASLGAFEFLLYRYWVDLKLGDVLTYGAMLGDLVIKNNYVAPTPVDKYTMNLEQERRVWGIERSDRDMNSTFRY | Pathway: Protein modification; protein glycosylation.
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus m... |
A0A2T2XA23 | MPSQHREGFVLWFTGLPGVGKSTLAQGLSARLKAEGHRTYVLDGDILRTGLSQDLGFSASNRHENIRRAGHVAKILVDAGVIVLAAFITPFADDRKMLRRLFSPKQFSEIFLDCPLEICRQRDPKKLYRKAESGLIPEFTGISSPYEEPTQPDLRIPTHLMSAEQSLQVLWEFIQTHYDGNSG | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 183
Sequence Mass (Da): 20536
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S6CES5 | MLEALFWIVRRDVTIALRRRTDVFTTLIFFLIVVSLFPLGIGPELDTLRLIAPGVVWVGALLASMLALEQLFLADHRDGTLEQMLLAPQPLPLLVIGKVIAHWLITGLPLVIMAPVLGLQYDLSAEALTVMVWSLLLGTPPLSLLGAIGAALTLGLRSGGVLVALLVLPLYIPVLIFGAGAVEATTSGLGGGAHLSMLGAILLVALLGTPLATAAALRVASE | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 222
Sequence Mass (Da): 23258
Location Topology: Multi-pass membrane protein
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A0A0A1HA87 | MGDAPRGDVPTRFPPRETAWFFDIDGTLAEMMPTPEMVQVAPGIAERLTMLFGVSQGAVAVVSGRSLASIDALLAPLVLPASGQHGAQRRNADGAVRAAGAATASLAAVRQRIAAWVGENPLVRVEDKGHAIAIHYRAAPEFADAVQGFAQDLAAADRNLRTQPGKMVVEILDAAHDKGAAIRAFLAEPPFRGRRPVFIGDDLGDEPGFEAVNRAGGVSIKVGTGPTAAQYRLPDVQAVQAWLAALVA | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Removes the phosphate from trehalose 6-phosphate to produce free trehalose.
EC: 3.1.3.12
Catalytic Activity: alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
Sequence Length: 248
Sequence Mass (Da): 25972
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H9UAK8 | MPNLYFCIPKDDAVYFDEHEVTHMKVMRLKEGEIIEATDGNGGKYKVVVKKIDKYSAVGSVISYEFVESPEGRLVLFAPSGRWERLRWTIEKAVELGVDEIYVFNNERASRHYEDKQEKLELVVREAAKQCVRYNFPVIKPIEFLDIFSLAPESTYILDFKGRKIPKRISKNVGIIAGPEGGFSQKELLLLKKRFRSICLGKKILRFETAIILATGVFSMKLGKI | 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... |
A0A380CJY2 | MKLKFTKALLIIGLGCLSLSAFAKETKEPKGSLFIIGGGAKDQQLIRSMVDAAALSPSDYIMILPMASTVADASVADIKEQLQEVTDHKITAINFSKADASDLRLVDSVRKAKLIYITGGDQNRFMAVVEHSPLFDAIHSAYQQGACIAGTSAGAAIMSDQMITGEQAQDSTYRATFNRLNKDNLVTAKGMGLIRTAIIDQHFIKRSRYNRLFSALAEHPDKVCIGIDESTAILIHNKKAKVVGQFQVVVASNPVKLEVNKEGRIIWDDIRLSIYDNGKTFPIQ | Function: Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
EC: 3.4.15.6
Catalytic Activity: [L-4-(L-arginin-2-N-yl)aspartate](n) + H2O = [L-4-(L-arginin-2-N-yl)aspartate](n-1) + L-4-(L-arginin... |
A0A4R0NRJ3 | MIAQSIHYKESRPRAKVLEFVNLKDLFSKYLFHWPLFFIVLSMALLAAIFYTKVSKPTYEIKATLLIKDQKKAPDQQSALHEIDMYNSSKIVENEIEILSSKKLSQEVVNDLRLWIGYEKVNGFMSSTDLYKASPVNFNLLGASGNYAPEGLDIVIKNDKTFLLKMPSGELKEMGFSKNYTTELGEWRLDATNNLNQYINSTIKIKVMDPDQVAIQYQKGINVILPNKLAAAIDLSLNDTNAERGKDVLNRLIYHYNLAEAVEKNRETKSTLDFLDRRLASLTGDLTNAEKGIEDFKSTRGLTDLSSDSKISLENMQAND... | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Subcellular Location: Cell inner membrane
Sequence Length: 788
Sequence Mass (Da): 88570
Location Topology: Multi-pass membrane protein
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A0A453RRR0 | LRVRKFSKHCRSCDKCVDGFDHHCRWLNNCVGRKNYFTFFALMTTSLLWLAIEVGVGIAVLVMCFANTNAEKIIQDKLGNGLTRLPFATIVGIFTLLSLVACVPLGELFFFHMLLIRKGITTYEYVVAMRAMSEVPQDEEEDERANIIYSPTNSATSGFSGGSSLGLHYKGAWCTPPRIFVDQDEVIPHLERGMAPSTVDPDATGHAERPNKAKRQVKISAWKLAKLDGNEAMKAAARARASSSVLRPVGARGPGSTGNSHPQSIASQDDYETGTQSASSLSSPVHIHKLAPRTQMNVPPPRPPEGPGFPTTQATTNPIM... | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 468
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 50350
Location Topology: Multi-pass membrane protein
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A0A0S8HNA9 | MRILLVNDDGILAPGLAALRAAVEDLGEVTVVAPDSPQSAAGRSITLHAPIACQRVHVDGRFWGYGVSGRPADCVKLAVRELMEAPPQLLLAGINPGANTGVNVFYSGTVAAAAEGALLGIASVAFSLDRGGEMDFHRAGRLCRWVLDALLAAGLAEGELVNVNLPALSADRPRGVKVVPQGTAAITESYRREEQAGGSALFQLNEQYEHGPQEQETDVEALAGGFITITPLKSDMTDRARLPRLQGHTWGLPPEGNG | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
EC: 3.1.3.5
Catalytic Activity: a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 258
Sequence Mass (Da): 27103
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A0A1V4QN95 | MPALAPKIILGRVVGAHGIRGELKVWAEAEGAETFLQIGEVELAGRGYQVAGARPHKRYLLLSLAGICSRNQAEALIGQEVWGAAELLPPLPEGEYYWDEILGLAVYRMDTGAYLGRVTEIIPTAAHDVYVVREGDREYLIPARVEVIQEICLEQGWMNIDPNVGVLETRAV | Function: An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but ... |
A0A2X0VL42 | MFNIRPCFIIMQDKKDITLALDLTGSTLPDNDIAGALNFAHTLYPSLKVHVFGSDSLKEAMQRGKIDEKFYVFHNARALDTTKKPQQSASDGNCATALALLMTLNKESMATVSMSDGTYLSAMSRHIVGAYSETLSLASKIPTGAKSYLLMLDMGANVAVGADDLLKFAILGSACARVYLDKEAPRVRLLNALGDDVRLNPMAYDANIYLKKDSSIRYDGFIAPDKIFLTDANVIVSDANTANTALKAAKGIADAYDSGSSISRFLSKMMRPDWLTPWQYNASVILGLKENVIACHARQGKDALALAVVEAVLACEHNLA... | Catalytic Activity: a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]
EC: 2.3.1.274
Subcellular Location: Cytoplasm
Sequence Length: 333
Sequence Mass (Da): 36165
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A0A7G6E5N8 | MVMDISQFRVKVKETIEQYNLIQSGDLVVVGVSGGPDSLALLHVLKTLRPELSCELHVAHLDHSFRGKQAEEEARWVKELATHWGLPVTIAKKDVPALAREKGLSPQEAGHLARYEFLSGLLKQLGAQKIALGHQADDQAETVLMHLFTGSGLEGLRGIVPVHGPIIRPLLYVTREEIEEYCRAHALEPRRDPSNEKDIYLRNKIRNRLMPWLLENINPNLITTLNKTAQILWAEEEYLEYVTKKKAKEYLAHEGDYEKLSLRRWEEIPLALQRRLIRHAYSFRGAAQGLYFQHVEDIRELAQRGQVGKLLHLPGKIIVE... | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34)... |
A0A0A1H6S0 | MSVITAVILAGLGLYAAAMASGRLPTDFALFLLLCTVVSGVYYVAELVVLKARRSERAKRELAEFDRRNGEAGAIAPEPVARERRALEERLAVRPWWVEYTAGFFPVIVAVFLLRSFLFEPFRIPSGSMIPTLRIGDLILVNKYQYGIRMPVWDRTLIPIGHPQRGDVIVFRFPLDPSQDFIKRVVGLPGDVVDYRDHVLRINGKVVPEAPMAPFFDASRLQTYRQYEETLGTVRHRVIWGGGDGIAAYPVPQHNDPGACVYSTDTDGGVRCTVPSDSYFVMGDNRDNSEDSRFWGFVPDRNLVGHAVFIWMNFGNVKRI... | 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: 324
Sequence Mass (Da): 36451
Location Topology: Single-pass type II membrane protein
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A0A7V8IQM3 | MRSMSKFDRAFLDQVLQRTSIIDVVGRKVTWDKRKSQPARGDMWACCPFHSEKSPSFHAVESKGQFHCFGCGEHGNAFDFVMKTQNIGFSEVVEQLAQTAGLEMPKLSRDSVEKAGKTTRIMAALAAARQLFEEALIKDEGKIARNYLQKRGIDSKHWPEFGIGVSPNSRNWLKDRLTAAGHLVEDLLDAGLLRAPEDGGAPYDLYRGRLMFAIEDGAGKTISFGARTLNDDVQPKYLNGPETSVFSKSYTLYRYKSARAKTKKSPLIIAEGYMDVIALELAGFAAVAPMGTALTADQLNLAWRAHPRPVLCFDGDEAGQ... | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
EC: 2.7.7.101
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Length: 634
Domain: Contains an N-termi... |
A0A8J5FT25 | MPKRVVFAFELLESWGKCACSGLRMFDERRTGNMRSYFHLELLCNIELPKKKKEPLQQTNPPSIPVDELFPSGEFPEGEIQQYKDEELLSSNLWRTTSEEKRELERLEKPMYNSVRRAAEVHRQVRKYMRSILKPGMLMTDLCETLENMVRKLIKEDGLEAGIAFPTGCSLNWVAAHWTPNSGDKTVLQYDDVMKLDFGTHIDGDASWRIVDCAFTVAFNPMFNPLLEASREATNAGVKEAGIDVRLCDVGAAIQEVMESYEVEINGKVFQVKSVRNLNGHSIGPYQIHASKSIPIVKGGEQTKMEEGEFFAIETFGSTG... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
A0A7C6J1B0 | MLITKLYPNARHLHFVTGIKSKSYNCTPGDIFVAIPGSTVDGFDYVDQAIALGAKTIVTERTDAFERLPNFKGNIIIVDDAKRELSRIAKRFYKKWLRGITVIGITGTNGKTTLSTLTYQYLRSINIGVILIGTNGNYINDEYYETVNTTPNILEIYSLLRKAKKDRKKIKYLIMEVSSQAIKEMRVLGLEFNIVLLTNLGRDHLDYHKTIDDYKYSKGLLIARMKQKKNNYVILNRDSPYYRFYHQLSLANIKTFGLYQADYQADIQYESLEGTKIKLKINGVLYDLYTKLLGRFNVYNILAIIAILDSIKLFSENVIK... | PTM: Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the addition of an amino acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosyn... |
A0A524JUJ8 | MRENRKRSKRQRVMPVLPNLFTTGNLFCGLLSIMTSIEVIAAVSGGGASEEWVFRRFWWAGAFIVISAFLDMMDGKLARFINHESKFGLSYDSLSDLVSFGVAPGVLIYSWVLMGSGKIGLMAVLFYVVCTALRLARFNVQSGNEEKFSFTGLPSPAAAGLMIAPVMLLTALNIVPDSRVLWFFLIAAPVIGLLMVSNVRYNKRPYFNFGGPFNALVVAAIILAAIITHPEIMFIFIVYLYALVGLVLYVIKQLKSKPKLSDEAETPNSSS | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
EC: 2.7.8.8
Subcellular Location: Membrane
Sequence Length: 271
Sequence Mass (Da): 29864
Location Topology: Multi-pass membrane protein
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A0A1F8V7I3 | MDFKKDKTPILYMAPMAGVTDRAFRRLCLECGAKIVVTEMVSAKAVQYGDKKSYELGKLFESDQPAIIQIFGSDPIAMAFAAKEMTAFNPIAIDINMGCPVPKVSGSGDGASLMKNPRLAGEIINAVVSAIDVPVTVKIRSGWDSKNINAVEIALIAEANGAAVVTVHGRTKVQGYEGYADRNVIKEVKQTLKIPVIANGDIVDGASAIDMLEKTDCDGLMVGRGALGSPWVFTEIKAVLENKPYIPYSPGQKREMILRQLDMMVIDKGEQLALLEIRKHIAWYIKGIPNAASIRASVFLTHTKEKLIEIIKNIDFL | Function: Catalyzes the synthesis of 5,6-dihydrouridine (D), a modified base found in the D-loop of most tRNAs, via the reduction of the C5-C6 double bond in target uridines.
EC: 1.3.1.-
Catalytic Activity: a 5,6-dihydrouridine in tRNA + NAD(+) = a uridine in tRNA + H(+) + NADH
Sequence Length: 317
Sequence Mass (Da): ... |
A0A3A6P4G4 | MRRAQAEALAGQELPAGLFAGWEALSVELLKWSAVHRLTGHADPDAIYRDLLLDSLALLPLIKGTTLLDIGSGAGFPGLVLALARPELQVTLLEARAKKVSFQKQAIRVLDLAGRVRAVLGRAGVDLRGERFDIVTIRAVAGLAESLALARPYLAPGGAALLPRGARDRADARSLGLAVTEYRLPGTNEPRIIASYQA | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 198
Sequence Mass (Da): 21059
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A0A3P1SC80 | MRTSGEVALASATRTLNAALAQPGVDAMRVAEDFFGLSDLVREDARLRRGMTDPARSVDDKRTLSRGAVGSVVTATTATVLDDLVASHWSDPMDLHDACEVLGIIATMEDARRNDALETVGQELFAVADFLADYRDLRLELSDMGHGNRHERGDLAQSIFKDQLTKWTMRLVRRGVGRTSHGRLLSTLRRFAERAASMMNSVLVSVQAAAPMTDAQIERLRAVLTCKLGRDVTLTVSIDPALVGGFRFEVGNTALDSSIQTQLNDLRRALVGSR | 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 c... |
S5MHA9 | MSKVIFKISELNENIKNFVEKTNQFKNINIKGEVSNLTFNKSGHIYFSLKDNEARIDCAIWKSNTQSFINLSVKEGTEIIAKGVLTFYKPSGKFTFTISSVKIDGIGELSLIYEKRYNELKDKGLFDQQKKKTIPNIPKNIGIITAASGDAIWDVVTTIKRRFPIVNIFIFPTLVQGEEAAKDISKKIIQADNFIPKLDTLIIGRGGGSYEDLWSFNELEVIYAIEKCTTPVITGIGHEPDTTLSDYVADFSASTPTAAAEKSTPDYQTIINLLNSKLNDFGKNLKNKLDKIEDQVNNYSNKLKVDLNNKISYLKQEFRN... | 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... |
A0A8E2DHJ2 | MSYFFIPKYSSDIATVNFDSSGTTKIGKYYFNHSFMSVGLIGVVSACILGYVLSQIVIG | Catalytic Activity: (S)-malate(in) + succinate(out) = (S)-malate(out) + succinate(in)
Subcellular Location: Cell inner membrane
Sequence Length: 59
Sequence Mass (Da): 6438
Location Topology: Multi-pass membrane protein
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A0A4P7CQZ3 | MISRDFTFIVGGARSGKSAYAERLAADSGLPVTYIATAATPEGAHADAEFAARIAHHRARRPAHWVIVEAPLDLAGALDAAATRGQCVLIDCLTLWLANLLCPPESEAPLPDWRARLDAFAAACERAKHADCSVLVVSNEIGMGVVPLGAATRLYVDELGRLNQRIAALAHRATLVAAGLPLVLKAPSADAASGSGALKAPSADTASGSGEPGRSC | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 5/7.
Function: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
EC: 2.7.1.156
Catalytic Activity: adenosylcob(III)inamide + ATP = aden... |
A0A7V0TZ78 | MEAAVGMIWRQPNSYKGKQMNKARKKVKPGQEMISFEQACQLIWQHSSTLGSETILTRQAVGRVLAEAIKSPLALPPFAKSAMDGYAVRLSGKEKYPLQLEVVGIAPAGISQPGFKLAAGQACKIMTGAALPKGANTVVRIEDVKTEGKTITVKQTLTKGMNVCARGEDVKQGALVLPLGQFLRPVEIGILASLGISKVKVYRQPTIALLSTGDELVNPSVEPLPGQIRDTNRPLLLSYLTQRGLVCQDLGIAKDNQRSISEKIAKGLKADILLISGGVSMGDYDLVPQVLSSSGVQQVFHKVQVKPGKPLFFGKTDSTL... | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 336
Sequence Mass (Da):... |
A0A933Z6H4 | MIGGLGFQELLIILVIVLIIFGAGKLPSVGANLGKAIKGFKSSIGEDKPEELTSEQAAKTEQAQQTTPSGDKAGQAKPQA | 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. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 80
Sequenc... |
A0A316LJL4 | MNWRISDLLSADCGYMYGENWNLQDQDIQKAMPSIRQAVNDVETIRRDGKGPTGELVLFPHLPYILSEDLLMDEKERQQLAKLEASATSIDVVVSIGIGGSYLGNKALFDAFCGPYWNMGLASERQLPQVFFAGQNADPESLSALTRYLEVKAKTTEKQLNIVLLVISKSGSTIEPMSAFYALYPRLSAICHVEVITITDKQHGLLLSQSQEKHWMHFSVPEGIGGRFSVLSQVGIVFCALCGIDYREMIQGAKECDQACQGKDWKENPALALALFRYLATVSRGVTAEVVMPYGDRLNSFGRWYAQLMAESLGKAKNRQ... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 463
Sequence Mass (Da): 51331
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A0A7V6GNY0 | MMEWKIREEIQTRIDKFLQENTEFSRNQIQHLIKSGDVLVNDSLVKPSYLLKNGDFITLNTPKIEKEVELKPVDLNLEIVYEDEYLAIINKPKGLVVHPSNTYEGVTLVSGLIHEFDLLSNEDEPLRRGIVHRLDKDTSGLLIIGKNDEAHNKLKLMFQRRQVKKHYLAIVYHEFKEYTGIIDKPIIRHKKHRQMMTTANTGRSAMTTYEVLSQNNGFAYLKLDLITGRTHQIRVHLKSINHPILGDPVYGPKKVYGNTGPYLHAYALEFNHPITKEKLNFSVEPPKEFQIELTKRGLKV | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 300
Sequence Mass (Da): 34776
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A0A970IYE5 | MYLQTIFTFNNLFWFFFALVNFSLITLIYKLFGRLGLFTWIAIGTFVANIQVIKMVDLFGFKPATLGNIMYGTIFLASDCLTEKYGKKDAQKSVYLSFFILVSMTIIMQLALQFKPSPYDFMQEHLEAIFDFVPRVVAGSLTAYITSQLLDIYLFSKIKEKLPSNRFLWVRNNVSTIISQLIDTAIFVTIAFAGTIDTNALFQVFISTFVIKIIVALLDTPFIYLMKRIKPIKDNNTLLS | Function: Involved in the import of queuosine (Q) precursors, required for Q precursor salvage.
Subcellular Location: Cell membrane
Sequence Length: 240
Sequence Mass (Da): 27520
Location Topology: Multi-pass membrane protein
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A0A174J4Y2 | MIFDTHMHTIFSSDSKMSISEVINTSKSLNLGVCLTEHMDLDYPEENEFKCDIPRYLETYSNYRSDSLLLGIEIGMTQNTLLENEATSNKYDFDYILGSIHTVDGLDIYNTFHNNKLPSDDFYKRYYENMLYCVENYNNFDSLGHIDYLFRYAPFPNNEININPYKEIVEAIFLNLIKKDKAIEINTRRLSNPASLQALLETYKFYKELGGRYVTIGSDAHTPSAIGNNIKEALMLAEQLSLKPIYYKSRKINYFK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 256
Sequence Mass (Da): 29810
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A0A1G1IT46 | MKKRTAKVARKTKETNIVVNLTIDGRGNAEIKTGIGFLDHMLTLFAKHGFFDLGVAAQGDMDVDMHHTNEDIGITLGSAFKKALGNKKGIRRFGDSFVPMDGCLVRVVADISNRPSLHVHYKTKRDIENLLANLAIGDSVKYSFVNMEQFMQAFVMNAGINMHIEILAFDKDLHHLIEAIFKAMGRSLDEATQIDIRSKSIPSTKGKL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
EC: 4.2.1.19
Subcellular Location: Cytoplasm
Sequence Length: 208
Sequence Ma... |
A0A932XV12 | MPVTLRCKRFPLAAGEVARLWRAVIQLREHRDEDVTVCCVSVREMTELQARYRGRPGATNVLTFSYTAEPKPEPMHDVALCMAVINREGRRHSFNRRDYAALILAHAFLHAVGLDHERSRQQALAMRQAERFVLTRCGYGYTGW | Cofactor: Binds 1 zinc ion.
Function: Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 144
Sequence Mass (Da): 16571
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A0A1V2M942 | MSAFFAGLNTFVIGILIVFLALVLLIVLINMFGKVVSSFENKKKAIEPTPAQTAKTRVAAVTTQQPVVTVEDDCEIVAAISAVIALSLGTTTDKLVVKSLKRIR | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 104
Sequence Mass (Da): 11118
Location Topology: Single-pass membrane protein
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A0A7X7LT42 | MKLGSHVSLGGNDKFLGSIQEALSYNANCLMVYTGAPQNTSRLPLSKLKIPEAWALMAINRIEKTDVFVHAPYIVNLANPDIEKQQFAIQFLTEELIRTTGLGANVMILHPGNHLNRGCEYGIELIAQGINQLHRNTQGDSTIIAIESMSGKGTEVGKTFEELQAIIDLIEDKNRIGVCLDSCHLHDAGYDVQTGFSQVIDEFDRVIGIDKLQVFHLNDSKNIRGVAKDRHANIGFGQIGFPAICEILNHPRISHVAKILETPYVSNPANPKLSYPPYKYEIAMLKAGVFQPDLMDVIVLAEG | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-produc... |
A0A1V2M7E7 | MILGIVGGIGAGKSTVVQIMKELANIFVIDVDKIGHAILAKDALAYNEIIEEFGDKILDDEKNIIRKILGEIVFNDPIKLLKLNQISHPKIYMEVERILKSIDMKKYKYIVIDCALLFEIGLDHLVDKIIGVYASEQVRAARIMKRNNISYENALVRIRKQKSWQELQSRINYFINNDGNDENLQKNIKDILEVIL | 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... |
A0A2T2XFB3 | MQPENALIVGKGAREHALAWGLKESSRFKEIFAMPGNPGISQIAHCLPYRDTAEIVAWAMHKAPMLVVVGPENPLAEGIVDQLREAGHWVIGPEQRAAQLESSKSFAKSVMERYRIPTAHAKRFDNLQALEDAISAESEWPHVLKQSGLAGGKGVVIVETPSQAMQIAREWAAQDNLLAQGVLWEDYLDGKEISVHVLTNGKNYVWLPLTRDYKRVTPDLNAPNTGGMGAFGPVADITQDIRTVINAKILDPLMQFLQDENLFYRGVLYVGIMLTGQGPMVLEFNVRMGDPEAEVLIPLLPIDWGACWLGLAQGHLPSIV... | 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 2/2.
EC: 6.3.4.13
Catalytic Activity: 5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate
Sequence Len... |
A0A7G6E2D8 | MNKHLGEQFEGKEEYVKNLFNSIAPFYDRMNMIMTWGLLKSWQRFVLNLTNLRPGDKALDVCTGTGELAFQMAEKVGPTGEVMGLDLSEEMLSIAREKLVKQYPQRKVIFMEGNALSLPFPAGEFACVTTGFAMRNVVDIPLAVREMTRVCKKGGRVICLEISQPTIPLFRQGFSLYFFHFIPLLGRLVDKGQRIFGRLPAYTWLPESLKKFPDRETLAQIFREAGLREVKYYPLSGGVVTVHVGVK | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquino... |
R6DNK1 | MYQALYRKYRPKNFDDVVGQEHITVTLKQEISSGRVGHAYLFTGSRGTGKTTCSKIIAKAVNCPNQQDGNPCGVCDICKGIDDGSILDVTEIDAASNNGVDNIRQLREEANFTPAVTKYRVYIIDETHMLSVGAFNALLKIMEEPPEHVIFILATTEVHKIPATILSRCQRFDFRRIDPKVIAERVKYVCQQENILIDEDAASLIARLAEGGMRDALSLLDVCRSNARNPENQQEHITAEHVRSSAGLAMSDCLFSIADAVLKQDVPAILKEIDTMFLNSIDFEKMCVQLISHYRGLMMAKALKSPADFVPGLSQDIQAL... | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 552
Seq... |
D5ECH9 | MKKVFLAVILGIILFLAIFFMKSVKRPHPLEQTSYALGTILHFQIWGKDANQALEKALSRIHDIEVHMSTHDPNSDIYKVNVSSGSSFVPVHEDTFYVVEKAIDYAYKSSGTFEPTIGGLVNLWGIGTPEERLPSEEEIANAVSLIGYEEVQLDRKNMSIRLPRSGQHLDLGGIAKGYAADEVVAILKRKGIKSALVDLGGNIFVLGTKPDSTLWNVGVQNPLEPRGQYLGVLRVSNKSVVTSGNYERFFEKDGKRYHHIFDPATGYPAESGLLSVTILSDRSIDGDALSTALFVLGKEEGLKLASSIEGVEALVVTKEK... | 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: 345
Sequence Mass (Da): 38034
|
A0A847YTU7 | MILGELNNNLKTIIMIKKTRKYLSIVISILLVILISLTIKIFIFEIYDIKSSSMEYTLLEGDKILVNKLVYGPKVPSSIEEIPWLNLFCPQHAKHKQNLYRRINGLSKVQNGDIVVFLHPYNNAKGILIKRCIGLPGDTIEVRNGKIFINNYIFNDSKYINPLPAVDSNLINIHIPDKHTFLNEVNQSWTNDNFGPIIIPFEGMSINFTLENIRMYKKAIGFSENNIIKEHNGKIYLEGIETTKYTFLKNFYFMIGDNRNISIDSRDWGFVPEENLIGKASIILFSNNKDGVNIGRFFKFIN | 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: 302
Sequence Mass (Da): 34785
Location Topology: Single-pass type II membrane protein
|
A0A1X1Q5L7 | MNITYEVKDNEALTPVSVRAFLRSHCGVSHGLWRRLKWNGTILVNGEAVKATMATVAAGDKVTCILEEESAIVPTKMPLDIRYEDKYLIILNKPNGILVHPTGGDHTNTLGNGLKYYYQATGQDIDFHPVHRLDRNTTGLVVVAKLPQLQSALTQPGRRMKGNMQEHNITQKFFHRSYFALIDGIMPKREGIIDLPIARHPDSIIQRICSPDGQYAETHYQTVAVNNGKSLIKLELKTGRTHQIRVHLASIGFPLLGDDLYGGNHDIIGRQALHAYHLEVFNPLNGETVSVYSDIPQDMIQAFYK | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 305
Sequence Mass (Da): 34172
|
A0A847QF89 | MARKKQEQCIEDTISFEDALSKLEAIVKQLEQGDLSLDQSLDQYAQGVRLSRLCLAKLNSAEDKITKVITEANGKIVESNLDFQEEE | 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... |
U7UM18 | MDILKDDFNFYHFTVDKAMKNKEFLKKINLSSRYIRRSVREKNIFVNGKLILQNIDLKPGDIVSIKIEEEELNAIAEEKELDIVYEDNDLLIVNKEPGIIAHAVNVEQRGTLSNYLAGYFLKNNIKRKIRLVNRLDRDTSGLIIVAKNSNAHSQLAKQMEEGKIIKKYMAIVEGVIDRETIIEKNILRSEDGIKRIVDQRGQYAKTLVKPIKTFNNMTLAEVQLFTGRTHQIRVHLNYIGHSLVGDPLYGNPSPLIKRQALHSYYLKFNHPRTNKILEIKGELPCDMKTLIM | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 292
Sequence Mass (Da): 33728
|
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