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stringlengths 6
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stringlengths 16
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A0A7C5RY21 | MNIFFNLFKIVFLLFLLFTLPEIVFCQLQSEAIILDGLHKFSAGDKIEWAKTEFDDSKWGKIKVPESWQSQKVKSDKGMGWYRIHLNITDRFKNIEPAILLGRIGDIDEVYFNGKKIGGLGIIGNRYVEASKIQRLYKIPENLIKYNSENIICIRVMNTYLNGGLFDENIAFGDYKILLIEKMKREKFTLAIEYSLFTFFLMFFIGCLFFYLKGLREREYLFFWLFVTLYGIIFTLNSVSFYNTGLKNNLVQQIISSISILLPAILLMVLKNVFKEKLTKFIKSLLLIFVLLSLTIFFFPYYEIRQIVYAIWKLCFAIIAVILLYFALKAFKRHYYESGSTMLGIAGLITGFILESIAGVDFLQSTGFFLWDYSTVFFMTCVMYALAARFTRIKELQTTSIRIFKAHEEERKRLAREIHDRIGPSLTAIKLQIQMIAKKTKEGIFPEEETVNELVQEITHSIEDMRAIAMDLRPSFLENIDIKNAILWHARKLQERSGIIINLNIEDIANINNDIKEALYRIYQEAITNVIKHARATIVDIILKRDGKFISMEIKDNGKGFESPHYKDRNKGLGLDTIRERVELMEGIITIKSNRNVGTALNIRVPAK | Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cytoplasm
Sequence Length: 608
Sequence Mass (Da): 70592
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A0A8J1TSB5 | MKGDARANDGVKINVIVAMMDHNNGIGINNQLPWPKIRTDYEYYTGLTQRVTKPGNVCINMKGRLTFESSGEQERMNPLRHNVVISSTLKECPKGVGFIAPSFDAAIEYASEYANAESIWVMGGYSVYKRALQSPLCHRVHLTRIFHKAEADAFFPIDCLEPSIYKKIDLPEVPSDLIKENGVEYQFEVYERR | 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: 193
Sequence Mass (Da): 21906
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A0A8J1XSN3 | MLMLLLLVFCGVISETVWAVHILLIPYTQGTNSRLMNMEKLADILIQDGHSVSLMINNRYDEENRPISKDVKIYKFKIPDDAWLVTDDAVVAKAHNTSFIEMASLVKHLTISYCEALLKSGILHELKKIKFDLVLVDYVEECARLSIDYLDIATVTYSNEGGLVNTYFGHLNHPAPWSFVTPFVVGFPDDMRFSERVQSTLINSVIQYVYYTMLLDMDTLRIKYKVNASLSTMNTLSRKTSLHFSNNHFVLDYPRPVMPNHVNIGGMYFQPPNPLSGHIDNIVKNASPGGVIIVSFGSIFNPTHGTLEYVTEQMASAFAGLTYTVIWKYPKNSKPPKSLGKNTHLVNWLPQNDLLGHPKTKLFITHCGVSSTYETIYHAVPVITIPIAVDQFKHSTQLTKRLKMGIELRMDHREITNTSLVEAILSVLEDPKYKENAKIASRLIQKNINKPRDVFLFWINYVIETNGAKHLVSKPLQDLSFFQYFMLDVLIFLAVILAVIVTIIFIIIRWIFRCVMCLFKNSKQKDD | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 527
Sequence Mass (Da): 60103
Location Topology: Single-pass membrane protein
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A0A7C8JEY0 | MSALLRPTVLASRRLALPAASRTLASKATKSKKTPAHPPSAPPTPAKGGPPAVAAEPPTDATTSAYSPSHTVIPEEHIPADVIPAGAVSGAPLDLQSRTVRIYKPTKNAMQSSNHRGGLWRMDWDVMAKGHRWENPLMGWQSSADYLQGTHLKFRTKEDAIYFAEKQGYNYSVQEPKERVIVSKAYASNFAWSEKKLKKIHTK | 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: 203
Sequence Mass (Da): 22237
Location Topology: Peripheral membrane protein
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A0A1L5YAY6 | MSVPSWLYHRILQHGGNIPFHQYVDWVLHDQDYGAYGAGSLQIGLKGDFVTSPSLGSSFAYLLALQMEQWLNSFGEEPLSLIETGPGEGHLALQLAQILYNNAPNFRNRLEIILIEPNKGMSQRQKNYLAKSPLPLRWSSLEQLSRNPVKGIILAHEVIDAFAVERLTYYKNDWYRQRVALIPDRMNKKEGKLMLIRGERWDYCIPNAEGLGLHKKNTFPMKSGWCTELHTETLQWLNSCKKSLSQGYLLVIDYFIEASHYYSARYSQGTIMTYKDQIARIDPLQDPGKLDITCHICLETLLSAAAKGGWSFIGQALQGEALLALGLAEQLYWSKNRDKKNINSIINERENILRLVNPLGLGNFRWLVFNSNMKHSYPLFLNEPNGSSL | Function: Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Catalytic Activity: L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine
EC: 2.1.1.320
Subcellular Location: Mitochondrion
Sequence Length: 389
Sequence Mass (Da): 44365
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A0A0R3TM44 | MIHGNFDLKQINNCVEKTYQKIQCKQDSLNNQLASSSKYLDDALKKLCALKASLNAIELGSQPRQENKTLREYLKALKKSLSSMMKGFESQMKGEVNCPLKDSLLRYTHLFHHLLFGDSANLIAVFGRIIFHPGYLKLGTYNSSFDTLASCKRPGSYIFRISSSKSGFWSVAYVSSNLEILQAMSYDWLIIFSINYGHQQGLYLYPRGQDSIDDFSDLCKQIAPSIQNPSGETCRKCFKNSANTRMEPCGHSCCRACYKEILSTSGPPGQPTEDNGGYRHAGEVSSDNDNEAFKAAQANKGETKEFINAVEKITNIGGCEKNIVEANLRTLINMGKFPFDDSVEALIEAKGNREVAYRLLKQKKAS | Pathway: Protein modification; protein ubiquitination.
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.27
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: 366
Domain: The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
Sequence Mass (Da): 40895
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A0A0N4WIG3 | MTVSYNLDISSVSAFSFLRLLFRWRGSIWKSMSTELFIWLCGYYIVFFVYRNLLTIDNQRQFEKVAMYCESKLSYIPLTFMLGFFVTIVVDRWRNIFVNMGWIENLALTVATLLRGDSKEAVLYRRSIIRYAVLCQVLVFRDVSMRVRRRFPNMESIVVAGFLHENELRDLENIKMVYNKYWAPFNWALTICTRAYKEGCIENIPAMVAIQNEVKLFRTSLAQLCHFDWVPIPIAYPQVLFFAYSLYFCTQISRTTIELLSSGKMPLNAELKALSQVVFLAVRVYFVICTVSRQFILSADAKNRSALFRVAKPEEHVKMVAVDVGKHEEGDPPKSHKPSLADKIADICCVPKRRTSVYPVSQSAVHLVHYGDSPRQAIRRQPRATQADAKTNHKPTTDNGETRKLSNAGLTTISEESDSRKSSAESEVKMNDMSRH | Function: Forms chloride channels.
Subcellular Location: Cell membrane
Sequence Length: 436
Sequence Mass (Da): 50194
Location Topology: Multi-pass membrane protein
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A0A8D0S0V7 | MQFLLSNARWSGWPDASTELAGGAVAPGPTLNVAITLSLVERLVSPGRTCAEASFRYPRPLPAPLCLLCPGSSSPATVPHPLKMYACARFVSTPALIRRTSPLLSRSLSAVVLKRPEALTDESHSSLAAPRLLTTSLIPSRSFQTSAISRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM | Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
Subcellular Location: Membrane
Sequence Length: 225
Sequence Mass (Da): 23528
Location Topology: Multi-pass membrane protein
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A0A1V3WP35 | MKTSYRTAVHDGIRDALSNDPHVVLMGEDVGRYGGTYAASKGLLEEFGPDRVRDTPLSELGFVGIGIGAALNGLRPIVEVMTVNFSLLALDQIVNTAAALRHMSGGQFSVPIVVRMATGAGRQLAAQHSHSLEPWYAHIPGIKVVAPATIEDAYGMLAPRWPTPTR | Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
EC: 1.2.4.1
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue acetyltransferase] + CO2
Sequence Length: 166
Sequence Mass (Da): 17744
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A0A7C4WGW4 | MDVLDDLYTYAVNSLATSVYTVVRRRCANIGLDDVLAIVEEPARRDYGDLSLPLYRLSRMCGFSLNELEIALNELQLNELFSRFQVVNGYLNAFLDEVNYARLLAEVVRNKGGRYGYVENEKKLNVIVEFVSANPVHPLHIGSGRNAVLGDFLSRVFEVRGHRVQRRYYINDLGRQVAVLVYGYIKLGRPKIPDNVKPDEWLGFIYAVTNTVIDIIELKKEILNAGMDRDVIMAKQSELDELMAILSELRSRDEAVVDRLLDSIAEDADPGKSVEELMARYERGDPDVKEVFRYVVNMVLTGINLTLNRLGITFDKWDWESELVFSGLVKEVIERARRCEYFTLHKGVPALEFKSLQEDESIRSLLRLPKSIEIPPLILMRSDGTTLYVTKDIAYSIMKFRDFNADLVINVVGNEQTLAQAQLRLALYALGFRDEASKLLHYSYELVTLPGIKMSGRRGRYVSVDQVLNGLEARVENIMRSRGTVVDDHVKKVMAVGAFKYMMLAASPSKVINFDSEIALNLNRNSAPYLQYTYARAFNVLRKYGRELEWGRIDFTSASKPLRRELAYHLSKFPYILTKVSKDLDPELLTTYLNRLADIFNSWYDAEPIIHEPDEGVRNFKLFLTYTTGIVIKNGLYVMGIDVLEKI | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 647
Sequence Mass (Da): 73997
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A0A0N4WN39 | MSLGKLSIDKVDVKGKRVLIRVDFNVPQKDGKITNNQRIVAALPSIKYCLDNGAKAVVLMSHLGRPDGKKNPKFTLAPVADELKKVLGKDVKFLNDCVGPEVEAACADPAPGSVILLENLRFYIEEEGKCTNEKGEKIKAKDEDVEKFRASLTKLGDIYVNDAFGTAHRAHSSMVGVKLDTRACGFLMKNELVYFGKALSDPSRPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAFTFLKVDKNVEIGNSLFDEEGAKIVKDLLAKAKEKNVQIHLPVDFVIGDKFAEDATAKTVTMEEGIPAGHMGLDVGPKSEELFAAAVARAKTIVWNGPPGVFEFDKFSHGTKALMDAVVKATSNGAITIIGGGDTATCCKKFKTEDKVSHVSTGGGASLELLEGAFHIVVLFILKVDVKDKRVLIRVDFNVPQKDGKITNNQRIVSALPTIMYCLDNKAKAVILMSHLGRPDGKKNPKYTLAPVAEELKRVLGGKDVKFLNDCVGPEVEAACADPPAGSIILLENLRFYIEEEGKCTNEKGEKLKASPEAVEKFRASLTKLGDIYVNDAFGTAHRAHSSMVGVKLNTRACGFLMKNELLYFGKALSDPARPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAFTFLKVDKNVEIGKSLFDEAGAKIVKELLAKAKEKNVQIHLPVDFVVGDKFAEDATAKTVTAEEGVPAGHMGMDVGPKSEELFATVVARAKTIVWNGPPGVFEFEKFSHGTKALMDAVVKATAAGCCTIIGGGDTATCCKKFKTEDKVTHVSTGGGASLELLEGKVLPGVEALSPAP | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5.
EC: 2.7.2.3
Catalytic Activity: (2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP
Sequence Length: 821
Sequence Mass (Da): 88131
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A0A894JJ27 | NWLVPMMIGSPDMAFPRMNNMSFWLLPPSLMLLLLSSTIEMGCGTGWTVYPPLASNLSHNGAAVDMAIFSLHLAGASSILGAVNFISTIFNMRSNNFSMSTLPLFVWSILITTVLLLLALPVLAGAITMLLTDRNFNTSFFDPVGGGDPILFQHLF | 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: 156
Sequence Mass (Da): 16955
Location Topology: Multi-pass membrane protein
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A0A8J1TQP1 | MSEDYNNKVLKFLFRYIMGDLPALTDWLKTKPWVLAVPSWILRAIGAPIFLNNPISGLLILIGMFIANPWVAICGITGLISAIATAFLLGQDHGAISNGGCTFHGMLVGIVVSASIDKPDWYPWTVFPVVFLAMLSVYVNSGLGGIFSSWNIPAFNLPFCLVAFVFLAALPPNNPNFPPRIKAAPNETFAQASIDWGQIFLAIPCSCAQIYGSNQAIVGVLILLGLLIGSPILFLHAILGPFMSVFTALCVAAPPEQIYTGEWSYNAMLAATSLGGFFWVLSIQTHILALSAAIFSTIVYGAMFNTFSNNNIGGLVLAFPFVLTASIFLAFTSESKAIKRVPLDRISYPEMHWKLFNNKQTITPDGSGTLTQ | Catalytic Activity: urea(in) = urea(out)
Subcellular Location: Cell membrane
Sequence Length: 372
Sequence Mass (Da): 40309
Location Topology: Multi-pass membrane protein
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A0A099J2F9 | MSTLSLVTLAQTASPRRVRLTLVAVVVVVFAMSVATLLVSRNAEFISAWWPAAGVSVIAVLLARRNRVGMALAIWAAASGARLAVGQPLAPALAYGFANALEAWLIARILEGSDAPHSLDDVRSVGRFVIAVAIGALTMAGLAALIIGVQGGDAPGTFALVAPSHASAILVIAPFLMVARVRVPARLRTELIVQSGLLAIVLALVFLPGQSSQWKFLTLPVLIWAALRFGSWPATGQMLALALTATAIVDLRQAGAVGEPGPGSIAQEYAVLQSYFVVYAASLLVIAAGRTERLRLADEMLMRDRLLRGGIVGSQIGLLLLRENALGAVTIVDGNAVAAGLLGVTVEARGESAGAVPTDGPLASAIATVRGDTVAFRDWSGEVEIDHAERRLQVFIARVHSTGADALITVQVIDTTARYVAEQAVTAALGNEQATTSALRELNRQKEDFVSSVSHELRTPIMSILGFSEELADTKLSPLAADYLSVITRNAHRLADLVEDLLELSRMSDQNDRTVRPLEVTALNEVIRNCVEELGAAARSGGVTLVFIPVDDLDVAGNSRDVTRVLINLVANAVKFTPRGGRVAVTCSRAGDVVLVEVVDNGVGIPPDEIDRVLERFYRSSTSVSLPGTGLGLSIVTGLLKQLGGTLQITSDGLTGTQVRVRLPAAPAPVPVADTGERPAASVTTAVDRT | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 690
Sequence Mass (Da): 72347
Location Topology: Multi-pass membrane protein
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A0A8J1XRE3 | MDQGFVEAIGASLIREYLSRKGFKQTLAMLDNESPRSEQSISNRPTLMKELHLEKLMKRNKEEGQPFRTMIEVMTKHFLEQVNERHSRTSSAALENNKTKPVSPKKEYHGDIIVDDDVEGETLLGDGKSGLMDQQIPDRPMSSRSNRSRGMSGPITSSLDPRDKRLRSAKKKHVGPGTLHGPMKDVLRSEDSASPSPVNTPERQHSAGATRKEPNHLSIDLKPLTAALEEEPQRKPSASRRRTSNSEIPVDPPETSVVSKPQEKPKNITPSEFRGDKKTSFEDSLKKLKENRTKRRDKEKVEIVTPQSEATQGVMPRPSTGRRKVETDESEGYSVLNSSLTSDRPPSRGRLVEQPSKLSKDNTPNTAESENNNATQKEESDVDTEPKLPPPQLISKSINSRPMDLKTAVQLKTILFGTAMENFNDEWRYQSLTFCDIPKLQYGIVQKKGGPCGALAAIQACMLQKLLFTDKSYRTSWQNPTKEIRSKCLAMAISNILWRAGEFSRAILTLPSGRTLFTGIGRFKADQLTETLTINEFDNYDTLYGFVTQHIGHLEMDGSGGVILVVYSAILSRGISQIKKDMDVPDQGKLMGQHGYCTQEMVNLLIKGQAASNVFDNTMELDGGLVLKGIVGRGDIGLLSLFEHYNSCQVGTNLKVPKNPIWLICSESHFTTLFCTRKELMSDWKAERRFDLYYYDGLAKQDEEIRLTIDTTNRFYEPPSAEDEMVPPLELCIRTKWKDAQIDWNGTEPFL | Function: Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins.
EC: 3.4.19.12
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).
Sequence Length: 751
Sequence Mass (Da): 84430
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S5X650 | TLYFIFGIWAGMVGTSLSLLIRAELGNPGSLIGDDQIYNTIVTTHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSITLLISSSIVENGIGTGWTIYPPLSSNIAHSASSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFVWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | 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): 23746
Location Topology: Multi-pass membrane protein
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A0A0R3TIJ8 | VDWIVQFDPPDDPKDYIHRVGRTARAGKSGSALLILRPHELGFLDVLRSSRVTPVEYEVASNKVADVQSALEKLISTNYLLASSAHEAFKGIVRSYNSSKLACFNVNELDLSALAKTCGLTVIPKVDLGVEPSKKLDAKRMKRKAFGAAAASSFQTKKRKIYQKIN | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 166
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): 18277
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A0A8J1T4H3 | MANVPNQSTLAFFEVLGIFLGLSGCLLLKVTHVQNGPYMDEIFHIGQVTKYCKGLFEEWDPKITTLPGLYLLSSSLMQSLSWFFGYRVADLCTVFWLRGINVILATGNFCLLFALLRKLHGGNKGLSSTWYLLNTATLATFPVLYFCTFLYYTDTGSTFFTLAMYLMHLHGNSKMAAGVGIAAILFRQTNIIWVIFVAGLTVEKVINDYIQPEKKEITQEDIQNPKYIGIILLRIKNDLQNNRTGITQLIMNLIKAVWMYIIVGLGFTTFVIINNGIVVGDRNNHEACLHFPQIFYFCCVVVGFSIPHFLNAQTILGFLKFVLKHPFVTILGSGLCFLGVHFFTYEHKFLLADNRHYTFYIWARIFRRHWLIPYMLIPGYVFAIWTVSSFLKCKGILWKLVFLVCLVTATVPQKLLEFRYFIIPYLIFRLNMKPSSSFQTFLEFLLYFVVNALTLYMFLQKPFSWPNTDGVQRFMW | 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: 476
Sequence Mass (Da): 54925
Location Topology: Multi-pass membrane protein
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A0A1L5YCJ0 | MELTYRPRRLRRTSALRQMVRQFHLSPLDFIYPLFIHEGAESEPIEAMPGINRWNLDGLMKHVGVVWELGIRCIVLFPKIKDDLKSEDGIECCNEGGLIPRTIKHIKQEYPEMMIMTDVALDPYSSDGHDGIVNQAGLVLNDETVSILCRQAIVQARAGADLIGPSDMMDGRVGAIRKALDQEGFQDVGIISYTAKYSSAYYGPFREALDSAPRIGSTKKIPKDKSTYQMDPGNAREAITEAHLDQQEGADILMVKPGLAYLDIISQLRKQVNLPIAAYNVSGEYSMVKAAAQRGWIDEKSVVLETLLCFKRAGADLILTYHACDAAKWLLAD | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 333
Sequence Mass (Da): 37102
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A0A2Z4WX88 | GTLYFIFGIWSGLMGTSMSLIIRMELSHPGMLIGNDQIYNSIVTAHAFLMIFFMVMPMMMGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSLLFLLISSFTDYGAGTGWTIYPPLSSNISHLGSSVDLAIFSLHLAGISSTLGAINFISSIINMRPKGMELEQMSLFSWSVFITAFLLLLALPVLAGAITMLLSDRNFNTSFFDPAGGGDPILYQHLFW | 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: 221
Sequence Mass (Da): 24358
Location Topology: Multi-pass membrane protein
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A0A0N4VVY7 | MRFKEEEMVTGEERVISVMDLSQMTSIRKEDVISTLQHLNLYKYYRGQYVIVITDELKNAYRRMCEKITVRIDPSKLRWQPKDWSRRKL | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 89
Sequence Mass (Da): 10872
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A0A349CJ13 | MIKPGPLEIGLVLVIILIVFGVGKLPQVGAALGKSINAFKKGTKGEDEEEQAAQAKTKKKAKKKKATNKKASQATEGASEGETKPAAEETPAKQA | 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: 95
Sequence Mass (Da): 9870
Location Topology: Single-pass membrane protein
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A0A1L5YCY6 | MRLAKTRAALAINSLVCSIISLNNLMDLRLALVSAPILLALGWAGFNIGRAAVGQLQLMIKRSRR | Function: Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
Subcellular Location: Cellular thylakoid membrane
Sequence Length: 65
Sequence Mass (Da): 7046
Location Topology: Single-pass membrane protein
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A0A7C4WIF1 | MVKCSSIRRLSGGKTVKVDLEVFDEEIKEIVISGDFFLYPEEYIHTIESELRGRKISEVTKILNTFKDRVEVVGASIEEFAEAISDAYNSCVSG | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 94
Sequence Mass (Da): 10566
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A0A4X1U4N8 | MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSSSRSTEPSHSRDASPVGIKGFNPLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVHNCIQKENKDSLHSNTANRRTTPV | Function: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state.
Subcellular Location: Membrane
Sequence Length: 323
Sequence Mass (Da): 35962
Location Topology: Multi-pass membrane protein
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T1FNW6 | MKNIEPGSHCTISVVEDPLHEGEYFFEGTEKLLEIWFSPSSPSSASGSVQGGRASLRDINRSEWELLLKNVNCEILSSRHSTTMDAYLLSESSMFVSKDRIILKTCGKTTLLEAVKPLLGLAKEQCGFDNIVDVFYSHKNYLRPDLQPETYRHFDQEVAMLDTLFEDGAAYVLGKLNKDCWYIYTLDRFNITEPDQTLEIMMMDVNQDVMNMFTQSYGLTASQLTEKTGILDILPGAIIDDWLFEPCGYSMNALLPNGRYFTIHITPEDEFSYVSFETNVPRDSYNDLITKVTDIFQPNKFIVTLMANEASPAYKLCLKMDGPVKPFRRTEHQACEMKNYNLNYALYERPPTSKLIPYK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Pathway: Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1.
EC: 4.1.1.50
Catalytic Activity: H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-(methylsulfanyl)propylamine
Sequence Length: 359
Sequence Mass (Da): 41058
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T1G001 | MKRQGNRDVVGYGHNGQAVYEDRPEFPAPAIRFKENSKEVLALREKEKGDWKNLTLQDKKALYRASFCQTYAEMDAPTGNWKQVMAIVLAGMTLTLWINYFIKKFVVNDLPHTITREWQEKQLENMIKQRIGHIDGLSSKWDYENNRWK | 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.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 149
Sequence Mass (Da): 17565
Location Topology: Single-pass membrane protein
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A0A220DNB1 | SQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAITQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLL | 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: 169
Sequence Mass (Da): 17911
Location Topology: Multi-pass membrane protein
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A0A0F5LWT9 | MNACAGSPLGALVLVVGPSGVGKDTLISGARTALEADKRFVFVRRVVTRRADIELEDHDSMDHQQFAALEAAGRFALSWDAHGLRYGLPLSVDTDIALGRVVVANVSRHVIAEARAKYPACAVVMICAEISLRAERLTRRGRESRDQITARLARESAPVPAGIDPIIIDNSGSLAIGVTAFVMALRKIADE | Pathway: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route II): step 3/3.
Function: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP).
EC: 2.7.4.23
Catalytic Activity: alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + ADP
Sequence Length: 191
Sequence Mass (Da): 20442
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A0A1S3AV32 | MDFSHIFLFFLFFFPTLITAQSCSVSKCINDDFAIRFPFRIPDQQPARCGYPGFNLACNKAGVTTVNLSASEYFLVRGIDYATQQIQLYDSDDCLPRRFLQGLNKLNFSNSPFIPLFSQNITFLSCPPQFTMSHFPIIGCLSNSTNSILATSSTSFVKSMSTSCTIMTTLPVPVSNPDETNQFSTNLNGDLVLTWYSPACGICETEGRLCGYKSNSGQGIACFDKYTSEENNGLRVLRIICVVILLPTLMCVIGLGCFICMAKWSYSLTDGRGNQVQHRQQVNPAGSDLEAPSRLSGLNESTIESYQKVILGESRRLPGPNGTTCPICLGEYLTKDTVRCIPECKHCFHVDCIDQWLRVNSSCPLCRNSPNPSPSHLTPIS | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 381
Sequence Mass (Da): 42142
Location Topology: Single-pass membrane protein
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T1EF37 | MATCAVLGGGISGLATAYYLNKFGGNLVKKIILIEGTNRFGGWMRSVKYEKDLLFEQGPRSIRGVGRAGFNTLEMVEDLELDDEVLPIPRSHVAAKNRFIYVNKQLCKLPSSLKAVLTTQPPFSKPLCLYGLMEPFRKKGELDDETVDSFFSRRFGPEVAKYAANSMCRGIFAGDSLKLSMRSCFPLFHEFESKYGSIVKAALMRPRTKRRENSELINKFVSENWSMWSLKNGLEDLPRKLLATLQKEDKVKVMSGSKVNTLQFDDVKVKLVTSANGEIMTVDHVFSALPSFDISLLLLPTYANISSLLNDIRFASVGVVNLVYPSDVTTPQVGFGHLIPSFEDPAVLGVLYECHTFPHHNGRDNKTRITLMMGGAWFEECFGSPETADKCKFEEMALKAVSEQLSIKQRPEMVVVNVQKYCIPQYKVGHHKLLEEAESLISKNNLQLSLVGSSYRGMSINDCIFNGKLQVQQYLGIRRDDE | Cofactor: Binds 1 FAD per subunit.
Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
Function: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
EC: 1.3.3.4
Subcellular Location: Mitochondrion inner membrane
Catalytic Activity: 3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX
Sequence Length: 482
Sequence Mass (Da): 54048
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L1JHI4 | MESDTRRDILPANILPHLDLVANFRLHGDIPNTLETIHQDIDIGTPRLIEKSGKIIHHVTVTYTPGNLEMYRLQEKQQRSRKMFAAYLVSNCGRPRDAFIARLMSALGDDRLHSYGRCMNNRKFPEEKEHGSNSLSLLKMYKFTIAIENYLSHDYVSERFYQPLLAGSVPVYLGAPNIEEFAPGVNSFIDIRNFPSPEALASYLISLADNHTAYDSFFTWKLDGPSPEFLRMMNMSMTRGNVISFLVVVLRVLTAFFYPQVDLNRLHTSMCKKLVALTRREMKCGA | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 286
Sequence Mass (Da): 32712
Location Topology: Single-pass type II membrane protein
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A0A183P353 | MPFKLNTLNALSWCEFVKLANKSPDPSIRDIFAKHLMQIPGCTGPKITSIMEKYPTPCILMDAYDKQPTMSGKSNMLAQLKPADSNRCIGTALSQSIAFAFNTL | Function: Interacts with EME1 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks and nicked Holliday junctions. May be required in mitosis for the processing of stalled or collapsed replication fork intermediates. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI).
EC: 3.1.22.-
Subcellular Location: Nucleus
Sequence Length: 104
Sequence Mass (Da): 11469
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A0A8J7YIY1 | MVYQLGADEAGRGPVIGPMVLCALLGDTEKLVSIGVRDSKQLSEERRNAIFRSLGSISSWRISVVWPEEIDMAVAHSSLNRLELLHFASLIRHFDSEVAFVDAPDVDCKRFSAEMCRITGRKVVAEHRADIRYPAVSAASIVAKVTRDRIISEIAEELGEDIGSGYPGDSATIDFISSYVRKNGVLPPYCRRSWETSKRIISFIRIKNLNEFG | 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.
Subcellular Location: Cytoplasm
Sequence Length: 213
Sequence Mass (Da): 23702
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M5C4C8 | MATDFCPVYAPFFSALGCTSAIVFTCIGASYGTAKSGVGISAMSVIRPDLMMKCVVPVIMAGIIAIYGLVVSVLISGEMQPRMALFTGFIQLGAGLSVGLAGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALIMNTSGKVDDINKLCPLPSV | Function: Proton-conducting pore forming of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments.
Subcellular Location: Membrane
Sequence Length: 169
Sequence Mass (Da): 17310
Location Topology: Multi-pass membrane protein
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Q5U3T2 | MAPVPPGIRFLASFNRDQWYKAFTFALTFLLYTSFHLSRKPISIVKSELHKNCSHAVEAPTEISSSSQQPGHHPEFDCSWKPFDRNNYKQLLGAMDYSFLFAYAIGMFLSGIIGERLPIRLYLTVGMLTSGLFTCLFGLGYIYDIHSLGFYIFVQVANGLVQTTGWPSVVTCIGNWFGKGRRGLIMGLWNSHTSVGNILGSLIAGYYVSSNWGLSFIVPGVIIAAMGVICFFFLIEHPNDLKTASTQSSAPSSQKFHKSCNGVNGHKDLYLQYKPGAKAQSWDTELLLGQESIGVCVPVQQVVVVKSEAEPSAISFMGALRIPGVVEFSLCLLFAKLVSYTFLFWLPLYITKAAHLDAKKAGDLSTLFDVGGIVGGILAGVISDKMHKRATTCAVMLLLAAPMLYGFSMMSQFGLGPTIGMLLVCGGLVNGPYALITTAVSADLGTHKSLKGNARALSTVTAIIDGTGSVGAAVGPLLAGLLSARGWDQVFYMLMTADFFALLLLLRLVMKELRYHRNRPGIAVELKEH | Catalytic Activity: D-glucose 6-phosphate(in) + phosphate(out) = D-glucose 6-phosphate(out) + phosphate(in)
Subcellular Location: Membrane
Sequence Length: 529
Sequence Mass (Da): 57507
Location Topology: Multi-pass membrane protein
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F1Q7U1 | MEETANTDVLFIELRQKLQSGLLFIRSDVIGGGADVKIESKPDSILNVQTPDSSFQVTLTPGVSLVETQKQKSPANSEQGSHYRLRLKVEQPTESPCSVIGQLRVDESYSVLCQSCGSRVLQHRSFGRVLPLPNGNWNALVDDWCCHPDPFANRKLLPRAGDCLLGDTFILLLRDDGCDESLTRAAAEKRVLVSCRRCSTALGEEITAEVLKLYITEISVKPSEDGECDLTQLSLEPKSESVRQRFLEQTLASRLVELSAAQSIFRFSIQSPDGKAEILLWLLNTDTLVASFPAPAARADGFISVGDSHPRMHQSCQAVAAVKVLYILCSDSKLRDVVDVWEKDISVHPLPLPQRSCEELKTLLTSSTFRLPAFLRCMNSFQVAYMRM | Function: E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.
EC: 2.3.2.26
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 388
Sequence Mass (Da): 43030
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A0A183P4E3 | MSGFSSSADVLLDPAAFPLLICPMDILISSIVRGVTFVERRVGAASMSGGSSGKVGAGTNANLALAKSEKIKTMKPVRDREYTVHFAADTHSLMKWNFKPSQKALRIVPGETALAFYTAENPTDKPIVGIATYSVVPFEASKYFHKIQTSHFSTSSTKSYCQQIIFGMKAAGTKSCFCFEEQRLNPHEKVSVHYRFTRKVFYIYEINQSPCI | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 212
Sequence Mass (Da): 23425
Location Topology: Single-pass membrane protein
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A0A7J9TCD6 | MSKLVGAVAIAGGGIAGIQSAIDLASSGLKVYLIESSTTIGGKMAQLDKTFPTLDCSMCTLSPKLAEVARHPNIELMTYSEITGITGEPGDFTVTVKKKATYVDYDKCTACELCVSKCPVKVPDEYNEGQNNRKAIYLAFPQAVPRVFTIDANHCLYLTKGKCGNCQKACENDAINFEDTDKEVDINVGSVILNTGFEPYDASNLEQYRIDHPNVVSSLEFERQLSSSGPFEGHVTLADGSHPKNIAWIQCIGSRSPEIGRNTCSSVCCMYATKEAMVAMEHDLDLKTTIFNIDVRAFGKGFEEFYQKAKNEKGIRFINSRPSGVEVDPVTDNISLKYEAEDGSGIKREEFDMVVLSIGLTPSESSKNLAKIAGVEMDDNDFVKTKIDSPLETSKPGIFVCGAMQAPKDIPDTVADASGAASKASSMLSSERGTLVTEKEYPPEKDMGDEIRTGVVVCRCGINIGNIVDVPDVVEYAKTLPHVVLAKEEVYACSTDSLEGIANLVKEHNLNHMVVASCTPRTHEPLFRETLMEAGLNPYLFELANIREHCSWVHQNNKEEATKKAKDIIRMSVSRANLLQPLYQEKIEFNKDALVIGGGIAGMNAALDIGEKGFKVTLLEKESELGGMLLKFTHLQDGRTTKEVLEPIIQKVESNPNITVHKETELTEQEGSMGNFKGHIKGANIDEDIEFGVAIIATGANEFEPEGYFSYGEYSNIITESQLEQMMEEGVDAKNVVFIQCAGGRNDNRPYCSRACCTVAMKNALRLKESDPDRNITVLYRDIRTFGVWEELYTKARELGVVFMRYTEDKEPEVSEKSVRVFDHLMNMDFEINYDLMVLSAPMVTPETNELLAPMFKVTLDANRFFLEAHIKLRPVECATDGVFLAGTSQAPKLVDESVSQASAAASRACTILSRDFLETIGNVSVVDSELCIGCGRCTLVCPYKAPELKEVTVETEEIVYITKKSEINPAVCKGCGCCAAECPTGAITARHFTTPQIMAVIKAYGEGI | 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.-.-
Subcellular Location: Cytoplasm
Sequence Length: 1009
Sequence Mass (Da): 110598
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T1FRK7 | MASSRQDEEVQSTNDDAVNSKFSAVKLGYWQDPYIQFFSKFSSAIDRKPPELNRGYYARVKGVEYLLKQFLKKTDLKCQVVNLGAGSDTRFWLLSDQNLVPLKWVELDFEPVVNKKIRIIKSKKSLMCKLQANNHDGSSDSIPDVQIKPTEIHSNIYHIVSCDLRDVCQFKSCIDRCSIDCTIPTAFICECVFIYMDPHSSSCLVRTISEMFSDIFFINYEQVNMNDRFGEVMLSNLQNRGCALLGVQHCLNFQTQFDRFLKCGWNGIDGGDMLQIYHGLPQDDVQRIEKIEFLDDIEMLTQLFTHYCIVWAYKHSTKNTTTTTATAAAATTTTNAVTDFSTVTNDISTIPVSSIAKSIAAATTSATTAVTTNITTSTSLLDDSGHSSSGSGSSSGGVVVSQLSGKLDFSDISLFIYK | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 418
Sequence Mass (Da): 46564
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A0A2K3N9T6 | MEDYGYSDNDDDYHFSDQEDSELELLQNDLHNFQFSSSKAPIAQVITKESLIAAQKEELQRVMDMLSIRQQDARTLLIYHRWDVDHLFEVYVEKGKEFMFAQAGVSVDEYHDSDSPVSAVVMCEICIDDVPSDEATRMDCGHCFCNSCWTQHFLVKVNEGQSKRIRCMAHKCNSICDETVVITLLGRRHPDMAEKYERFLLESYIDDNKKVKWCPSTPHCGNAIRAEGDDLCEVECSCGEQFCFNCLSEAHSPCSCLMWELWQHEHQDEVESDNWIIIHTKPCPKCHKPVEKNGGCNWVGCICGQPFCWLCGGATGLQHTNYSIAGHDCGHYKEPEKTVDHEKRDLYRYKHYYNRYKAHKHSFKFESKLKGSIQEKIPIFEKKHSQRNKYQLGDYSWVNNGLSRLLRSRCILSYSYAFAFYMFGDDLFKEEMLEAEREIKQNLFEDQQQQLEANVERLAEILPEAFKSLQYGKVMKRRMQIITLSTVIDDLCKKMYECIENDLLESVNLGSIHIIAPYKSKGIERAS | Pathway: Protein modification; protein ubiquitination.
Function: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
EC: 2.3.2.31
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Length: 527
Sequence Mass (Da): 61285
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A0A1S3CJV7 | MAAAALDPSSLQFTSTWAVAAVCFFFISLSLFLEHLIHLLSNWLKRKRKAALFEAVEKLKSVLMLLGFMSLTLTVTQQPVSKICIPNSVAYTMLPCQREIQITASKNLEMEKFQSNQSFSWLTEKVESSSSNDDSSSSSSSSSSSSDYCSAKGKASLMSQGGMNQLNNFIFVLAVMQILYSVLTMALGRAKMRRWKAWEEETNTLDYQVANDPNRFRLTRQTTFGRRHISSCATPSFLLWTKCFFRQFFRSVAKVDYLTLRHGFISTHVPGNTSFNFQKYIERSLHDDFKVVVGISPFMWLIVVIFILVDVHGWNAYLWVSFLPLIIVLALGTKLEVIVARLALELQNKTDVVKGAPMVQPSDDLFWFNHPKFVLTLLHFTLFMNAFEFSFFIWVTLQYGIKSCYHENVVVIVIRVVLAVTVQVLCSYITLPLYALVTQMGSQFKAAALEEHTAKAIKKWHKDVKQKRKKHSHHHDLDSSQHQEGSSHFASERPSSRVFEGSSRTLNSDQEMSSSHHRALSFSELNGVSIIECDEIVEEKLRDTVVTKDESAVSNKVIKIEIGEISEIHEEKITLSTPQNERRIS | Function: May be involved in modulation of pathogen defense and leaf cell death.
Subcellular Location: Membrane
Sequence Length: 585
Domain: The C-terminus contains a calmodulin-binding domain, which binds calmodulin in a calcium-dependent fashion.
Sequence Mass (Da): 66494
Location Topology: Multi-pass membrane protein
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A0A0B8NEB3 | MTVFTTMASPVGELLLVGEIQDGETILTAVSMAGGKSVLVEADWVADAEAFANVVPQLAAYFAGNHTGFDLRFGEGGTEFQRRVWRALDEIPYGRTTTYGEIARRIGAPRAAVRAVGSAIGANPLLIVRPCHRVIGVDGSLTGYAGGVERKQRLLELERVAWAPPPLCHRCGPDGSPSRTGRPWPGSSTSMGTH | Function: Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated.
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Cytoplasm
Sequence Length: 194
Sequence Mass (Da): 20629
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U3JB19 | MRRPSLKNKTPISIIKNLDAFPKVPESYVATSAFGGTVTLTVFILMALLTISEFFVYQDTWMKYEYEVDRDFTSKLKIKIDITVAMKCERLGADVLDIAGAVVASKEIKYDSVSFDPSAQKKQWYQILQQIQNRLREEHSLQDVLFKSALKGYFSDPAPRVDPTPESQNACRIHGKIYVNKVAGNFHITLGKPIETHKGHAHYASFIKDEVYNFSHRIDHLSFGNDVPGHINPLDGMEKTTLEQNTLFQYFITVVPTKLHTSNVSVDMHQFSVTERERVVSNEKGNQGVSGIFFKYKLSPLMVRVSEEHMPLAAFLVRLCGIVGGIFSTSDLLHRLIGSFVDIICFRFRLANKDREVLNRVSQSE | Function: Plays a role in transport between endoplasmic reticulum and Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 365
Sequence Mass (Da): 41460
Location Topology: Multi-pass membrane protein
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L1IYU7 | MAAVVRGVSAGMARAIRRGGDAPVYSIAVEQHRKYVDAIAQRVRSVIHVPARDDLPDCCFIEDTAVAVGKKILLTRPGARSRREETKDVELTIKSEISRFKSAYSVVSMAEESNEDVTLDGGDVLFTGRHCFVGISSRTNEAGFEFLRKHFASEFAEGAKSIHAIQVKDDLHLKSLATFAGNDQIAFDDSVGGDHFVQEVERLIGATHGYSMHRMSVHEATNVLRVGDALLVSKGCELLPEMQKLAEMAGVKRQDIVGVENSEFAKADGAITCRSLILPHLF | Function: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation.
EC: 3.5.3.18
Catalytic Activity: H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline
Sequence Length: 282
Sequence Mass (Da): 30798
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A0A352PP53 | MMRLADLGEFGIIERISRLLPATPKDVVVGIGDDVAVLDTSGPNYLLATCDIQVENVHFLRHGISPQQLGRKVVAINVSDIAAMGGRPRWALVSLGLPSDLSVTFIDELYHGLNAQAQVSGLSIVGGNLSQIKGPLVIDLFLLGECDKECFLRRDGARTGDAVLVTGDLGDSRAGMELLMHPELQVPEEVRTQVLAAHLTPHPQLAEGQLLAASRRVHAMLDVSDGILSDLGHICESSGVGASLDLAKIPISSACRQVAEAAAASPEEWALTGGEDYQLLFTADPTEVEAIQALVSQQTGAAVTVVGRIVAAPGMITVIEPDGTMKTPSGASGWDHFKQRKQP | 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: 343
Sequence Mass (Da): 36268
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A0A0N0RFS0 | MEALGLNLNFWIAQVVNFVVILVLLRMFLYRPILNMLDQRREKIRESLQAAEKARAEVVASQKAYEEELAKARREAQEIIERAREAAERQRAEILAEARQEAEQLKKRAQEEIAYERQQMLAQLRDEVAQLSLSIAQKVIGAALDESKQRELVEKFIAEAGDLK | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 164
Sequence Mass (Da): 18933
Location Topology: Single-pass membrane protein
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A0A069AKH2 | MLTYKESGVDIDEGNRAVDLIKGKIKGTYDGNVVGDLGNFSGLYSLKDFVGMKEPVLLASTDGVGTKLKIAQMMDKHDTVGIDLVAMCVNDLICQGAKPLFFLDYIALGKLVPEHIEKIVGGIADGCKMSGCALIGGETAEMPGMYGEDDYDLAGFSVGIADKEKIVSGNNVKSGDVLVGISSSGVHSNGFSFIRKIFLETYNYKMEQYVEELGMTVGEALLTPTKIYVKLALDVLAKHDIKAIAHITGGGLIENITRVIPKGLGLDINKKSWEKPPIFKMIEGFNAVDERELHKSFNMGIGLVLIVDKENADDVVNFINNRENDNAAYVDKKYSELLEDKAYIIGEVVDSHEGVELC | 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: 358
Sequence Mass (Da): 38874
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L1JSZ3 | MAEEESAASRKFVRKVIPSDNSCLFNSIAYCMAPVDNIHQTSSALELRELISAVILSDPEEYCEAVLSKSNQEYSHWIQQSSSWGGAIECSILAGHFQVEICAIDCQTLRLYRFGEGRGLSRRMYLMYDGIHYDAISELEGRKEVTLFRAEELAIALVKTFRDKRQFTDTSNFSLRCLVCGQGIQGSDGAQKHAAETGHGNFAEN | 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: 205
Sequence Mass (Da): 22904
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A0A1S3C4S4 | MEPKCSNLWCVLVFASLMATLSSGSLSAKYYASTCPKLLSIVRSEVVKAVDKEYRMGASLLRLHFHDCFVNGCDASVLLDDTSNFTGEKTAIPNKDSLRGFEVIDSIKTLVEAACPSVVSCADILSLAARDSVVALGGPSWVVGLGRRDSTTASFDNANNDLPSPFLDLPDLISAFSNKGFDTKELVALSGSHTIGQARCSMFRVRAHNETTTIDPDFAASLRTNCPFSGDDQNLSPLDLKTQSLFDNAYFKNLVQNKGLLHSDQALFTNSSADSHVSSYISDPKAFFSDFAAAMVKMSNLSPLTGSDGQIRSDCRKIN | Cofactor: Binds 2 calcium ions per subunit.
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
EC: 1.11.1.7
Catalytic Activity: 2 a phenolic donor + H2O2 = 2 a phenolic radical donor + 2 H2O
Subcellular Location: Secreted
Sequence Length: 319
Sequence Mass (Da): 34414
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A0A914B411 | MDMKSSSSIDLPDIFSPDDSVSSHGRPGGRVFGGAGRSHPSSVKSAGPLRNLSLQTFFRLMALTVVCTTTFALYYINSGVIRNTTPTATTDRGDIARQVLKNPAATNKPTDRIAPPLNHPSGVQNTSTAKLTSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGVQNISPVNIPSGVQNISPAKLPSGAPYISPAKIPSGVQNISPAKLPSGVQNTYPGGVQNASPAKIPTGVQNTSPAKLPSGVQNTYPGGVQNASPAKIPTGVQNTSPAKYPSGVQNISPAKLPSGGQNTSPANPSGSAKATQLLGDSRKTCPELKKIPNLSGAAKELHLEETPMTTVESQVFGNMRDKILHLVEEGNRQMRAPSLQTPSTGGTGSYDRLLGSLIPLEAMLDNYSYLPGGHWRPMHCTPRWKVAIIIPYRHREYHLPILIRRLVPMLQKQLLQFAIYSVNQENNMPFNRAMLMNVGFLESLKFSNWDCFVLHDVDHVPLSDLNDYGCTNMPKRMLSGSDRWNYRIPYHNFFGAVTGMTRENIRTINGFPNVYWGWGGEDDEIFERVRARNLNVYRTTGPENYYKVITHHHMSSPAMKERFDLLRSFRSRYQQDGLNNIRYTRPLIELHTLYTNISVNIQKV | Pathway: Protein modification; protein glycosylation.
Subcellular Location: Membrane
Sequence Length: 747
Sequence Mass (Da): 80720
Location Topology: Single-pass type II membrane protein
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Q7ZZ56 | MAAIIKEFVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKDHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDKWLSENDNHVAAIHCKAGKGRTGVMICAYLLHRGKFKKAQEALDFYDEVRTRDKKGVTIPSQRRYVYYYSYLLRNKLEYKPVALLFHKMVFETVPMFSGGTCNPQFVVYQLKVKIHTSNPAHTRREEKYMFFEFPQPLPVCGDIKVEFFHKQNKMMKKEKMFHFWVNTFFIPGSEESTEKVENGGLVKDLDGIQTAERGENDKDYLILTLSKTDLDKANKDKANRYFSPNFKVKMFFTKTVEEPSNSEASTSTSVTPDVSDNEPDHYRYSDTTDSDPENEQYDEEQITKV | Function: Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4.
Catalytic Activity: 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate
EC: 3.1.3.16
Subcellular Location: Cell projection
Sequence Length: 399
Sequence Mass (Da): 46828
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A0A6A6LJU1 | MRQFHHQRKKEPLLTSLGRCTISCILVLLTQFALSLVPRFFSASSLLIQLALSVVVLLLVVGFGKWCRRLLGVFASAPAFVFCNIFFVWAVYFVIVRQAIPFFIDAVFNGEVAMLFIGSSSLLKRVRYCKICKAYVKRFDHHCPAFGNCIGQNNHVLFMVLLLGFLSTEASYVMCSFQYWSGWKFGYQYIAIHSSPSTMAGGVYGMAYILYVL | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 213
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 24123
Location Topology: Multi-pass membrane protein
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H1XU80 | MLRTLLAYVFAVLHTLFCSLAAIVFGLFNPYSKIVDKIIRLWARGLLKAAGVKVVVHGQEKLRKDQPYIFMSNHQGAFDILAGVVAIPVTMRFIAKKELFRIPIFAHSMRTVGMIPIDRGNSAEARKSLEEAARTLQNGVSVLIFPEGTRTRDGNIKPFKKGGFVLALKSGLPIMPMVFTGSLNIMRKNSLKLHKGTIHVYFLDEVDTSQYSFEQRNELLKEVRKRIVDFYETVRLE | EC: 2.3.1.51
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Sequence Length: 237
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence Mass (Da): 26841
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T1F274 | MLFLIGLGLGNADDITVKGLKLLQQSSKIYLENYTSILSIGKNELEKVYGRELILADREMVEQNADVILDEAEREDVSFLVVGDPFGATTHSDLLLRAKERNIKTQIVHNASICNAVGCCGLQLYKFGETVSIVFWEIDWQPESFYDKILANKERGLHTLCLLDIKIKEKSVENIIKNRNIYEPERFMTVNVAIEQILEISKRRNCQVITPQTKGVGLARIGADNQLIKYGSLEELKIFNFGPKLHSLVIIGDLHPLEHDLLCNFSS | Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
EC: 2.1.1.314
Catalytic Activity: 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + 4 S-adenosyl-L-methionine = diphthine methyl ester-[translation elongation factor 2] + 3 H(+) + 4 S-adenosyl-L-homocysteine
Sequence Length: 267
Sequence Mass (Da): 30162
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F2Z4T6 | MAAPLGLHLEFGGGAELLFDGVKNHHVTLPDQSNPWDMKQLLAWIRGNMLKERPELFMQGDTVRPGILVLINDADWELMGELDYQLQDKDNVVFISTLHGG | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3, then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
Subcellular Location: Cytoplasm
Sequence Length: 101
Sequence Mass (Da): 11340
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A0A0R4IUS5 | MSTTVTQRKRRTSTTCSRRGNSKRNRAQMSQTVMETIDVLENDRTNSEDVVDLTCEGSEPAVVDLTNNDSIVVVEDGVQRRVGPCTESYVLSSDEEEESSLRLSPGLLSSLRDSSRARSTPGAISCPVCMDVYSEIMDSGRLMVSTKCGHLFCSQCIRDSLSRAHSCPTCRKKLTHKQYHPIYI | Pathway: Protein modification; protein ubiquitination.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Nucleus
Sequence Length: 184
Sequence Mass (Da): 20459
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A0A6G7QLK7 | MIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGVGTGWTVYPPLAGNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMKPPATSQYQTPLFVWSILITAILLLLSLPVLAAGITML | 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: 145
Sequence Mass (Da): 15416
Location Topology: Multi-pass membrane protein
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D8J4X7 | MKTEDLVQAAREAHAHAHVPYSEYRVGAAIETVDGTVFTGCNIENANYSNSLHAEEVAVSQAIATGHREFSRLAVSSDRRDGVTPCGMCRQTLAEFCEEAFPIVCDRGDDWTEYTLGELLPDTITQHHLE | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
EC: 3.5.4.5
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Length: 130
Sequence Mass (Da): 14354
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Q6PFK7 | MVSRRSLTIDTEKATKTTYVLGTTLTVNLIRCAPPQSKSFSIRCTPNVHYKITPPITDKNALPYPLGPNTILLITMDTVSETAFDSKLSVRYYGEKTETLGDAILHLTAVEISLDVDADRDGVVEKNNPNKASWKWGPNGHGAILLVNCDSESINNKKPDNENSDIGKVSDLKDMSKMVLRTNGPSQLPEGYKLSMHISQSTSESVRVFRPRTNTKTENLWKYQLLKLFLKDFLMVVGTDTLTQEVPYLGGSSELEFHVEGLRFPDKDFDGLVTINLSLLEPCGKGFPETPIFTDKVVFRVSPWIMTPNTLKPVEVYVCSTEDNYSFLKSIRNLVEKSGYKLKICHEYMNRGDRWMQDFPYDALLGPDFGYVTRNALNEEVSSLDSFGNLEVSPPVTVNGKNYPLGRIIIGVAFPTARKGRNMTKVVQDFLWAQKVQEPIALYSDWLFVGHVDEFMSFVPAPDRKKFRLLLASPDAGYKVFKSLQNSGLGKAEMFPGKEEAISVNDLLSDKKLQAENRYVQNCIDWNRDVLKKELGLDDEDIIDLPILFKVMEEKNEDSVPRAVAYYPDMVNMIVLGDQLGVPKPFGPQVKGVCALEKEMCSLLEPLGLKCTFIDDFAPYHKLLGEVHCGSNVLREPFTVRWWNLEL | Catalytic Activity: H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4(+)
EC: 3.5.3.15
Subcellular Location: Cytoplasm
Sequence Length: 647
Sequence Mass (Da): 72890
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A0A183IL52 | XXXXXXXXERNIINFLEALHRAFSVFSFNNHDELLLQQRARSKLTFPGLWTNTCCSHPLHCPAELENTPFAIGVRRAAIRKMSQELGANDINIDSLCFMKRILYRAKWDETHGEHELDYILILRQELALQPNSDEIERIRYVSKEQLRSMLGNQQEYRFSPWFTLIAEHFLFRWWEHLEHIDRFLDYSIDDFD | Pathway: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1.
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
EC: 5.3.3.2
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Length: 193
Sequence Mass (Da): 23075
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A0A1U9KMN6 | MHILGLTGDMGAGKTYVANLFRRRGWPVFDADATVHRLQGPGGEAVAPIKALWPEAVPGDAIDRTALRHIVIGHPDRLKALEAIVHPLVRQERQRFLRRMQARGKRWCVLDIPLLFETDAYRACDRILVVTAAESTRLRRIMRRRGMSEEQARNLLARQIGDAKRRRLADVIIRTDLSRAATFRQLRRLQHDLEAMR | 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 Length: 197
Sequence Mass (Da): 22594
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L1ISN7 | MCHSFFSTELPYVSHCLLCTAAWQKKYFNPFSQGLSKKPETSVSPPPAHAPPVESLKGKDLYQALEQLPSDWRDFLADETDKEYFKDLNDFYVDEVSKGATVYPPTRDIFGAFCLCPLDQVSVIIVGQDPYHGPGQAHGLAFSVRQGVAPPPSLQNIFKELESDPAVSFQRPRHGCLEGWAKQGVLLLNTCLTVRAGQALSHQAKGWEKFTDAVISKLDKQCDGLVFLLWGQPAAKKCSSVDESKHMVLKAPHPSPLSARRGFFGCKHFSLCNEYLSAQSKKEINWQT | 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: 288
Sequence Mass (Da): 32050
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A0A183J610 | MVSAYDKGELPPLTAEQRKEQQVAINKLQEIVKEIRKEHPDFGKLQFKTRHGPVPHPGPFPENPLWKYLDGQIWQKRPMAIGCGKPFKSLQCRAIISNNCNSILLKFMEFKAFVAISLFNNTYVVLFQETCLHPTDDKNILSLESFVCYHLVVVIWTSRILFIPAHTMLSHAKSMYPISNALAAAGHEVVFLEFQYERNGSFRQETEVPAGVANALGPDRGRRTVLPLWDDHCEGKQRSCXXXXXXXXXXXXXXXXXFDTSKTWIGSHEAKGTMWSRSLYPLYRVAVSRKPSSSFEERTINFWTLILFDLTMKITYRLMPFWIGFSGADHLERFYARSLFSMSMLPTYLDSETPMALDVFCSKLNCPPAAALSAEYESFVNNPDSMGTIVMALGHYISWDKVPIEAFDSFFLAFSKLKRYRFVLQCNVNLINKFTVPEHVMVRDWLPQAALLNHPRTVLFISHVGLKSLIDALCARVSIVTLPIFAEQHVNAMIVNARGIGVDLDRHSLSTEKVESAVVRVVTNGSFKRNVDRLSSMLQDNLLQGHNEQFFHFQFFMRHHRQMNFIRQRSTRLGTLVLYLVDAMTLSFIMFFGLLKFFY | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 599
Sequence Mass (Da): 68736
Location Topology: Single-pass membrane protein
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F1QH81 | MRNMAREILAFILCTSGWVLISSTLPTDYWKVSSIDGTVITTATFWSNLWKTCVTDSTGVSNCKDFPSMLALDGYIQVCRGLMITAVCLGFFGSIFALIGMKCTKIGGPDKFKARVVCFAGFNFACTGLCSLTAYSLYAHRITSEFFDPMFVAQKYELGAALFIGWAGSTLCLLGGALFTLSMADGSSKKSSPNRRVASLMSGAMPQSQTSHTRRTLPEYSSTPQHFDKNAYV | Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular Location: Cell junction
Sequence Length: 233
Sequence Mass (Da): 25382
Location Topology: Multi-pass membrane protein
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A0A818Y3X1 | MSNGAITMTKRLGSDVSGFEYDKRTGKGYFMNATGYDQQGQGGSWAKMYILDCNTQVIDSAKRGDKTYKALVYEAGNKLVWPDMHSGYIEMLNLANNVIDSVHIGVTLDEMDVSPDNNSLFIACRLGGSDIIKYDINTLGTTKFKAGSWPCVVRTDSSLNKVFVLNHFQSTISVINPNTNTVTATINLPLAEGRADAIAVMCYDKFLQKIFVSFPEFGNIVKINAVTNVVESTTPIPGFTFNPDGGGSNFNMSRSIKAPTGTTLSCKNWITEAAMRMLMNNLDADVAERPEDLIVYGGSGKAARNWECYDKIIETLKVLNEDETLLVQSGKPVAVFKTHTNAPRVLISNSQLVPAWATWDEFRRLEALGLIMYGQMTAGSWIYIGTQGILQGTYETFAACAIKHFGGTLAGRFVLTAGLGGMGGAQPLAATLNGAAFLGIGNSIHSGMVIVADGTPEAEARLERCLTYDPGMGIVRHADAGYDLAIEEQKKFGINMPMLK | Pathway: Amino-acid degradation; L-histidine degradation into L-glutamate; N-formimidoyl-L-glutamate from L-histidine: step 2/3.
EC: 4.2.1.49
Catalytic Activity: 4-imidazolone-5-propanoate = H2O + trans-urocanate
Sequence Length: 500
Sequence Mass (Da): 54204
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A0A948AM70 | MRLALFGGSFDPFHNGHLAVVRELGDRGLCEQVLISPARISPGKPAPLAAGHHREVMAVLGAAEHAYVSVLDLELRRPGPSYTVETLAELSRGRPGDEWLLIVGADAWRDFRTWHDPDRILELARIVVFPRPGIDPDPASSTPRVTLLEDFLVPVTSTAIRRRIAAGESVTHLLPGRVLDYIRLHGLYGCPCAADDGG | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 198
Sequence Mass (Da): 21577
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L1JMB6 | MSASQPLPFDPTSGSLSQKKPFDVDVSKLQDPSKVQEGCNPVVLLACGSFSPPTVLHTRIFETARDYFRETAETNKLQVVGGFISPVHPSYGKKGLAAPEHRVEMVKRALETSDWIACDEWEVKQNEWTRTRLSLDRMYQELNKDRGGQEVKVMLLCGADILESMVTPGKWRERSEERRGMILSRGIVCIKRSGSDPERLIQENDLLYERTRPFNSLIVCQAREWVENNVSSTAVRRAIKRNMSVKYFVADPVLDYIKDKRLFLD | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
EC: 2.7.7.1
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 265
Sequence Mass (Da): 30270
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Q503F4 | MSWGALYAQLGGVNKHSTSLGKIWLSVLFIFRICILVIAAETVWGDEQSDFTCNTQQPGCKNVCYDHFFPVSHIRFWCLQLIFVSTPALLVAMHVAYRKRNMKKKSILAKRGGNGKGDDLESLKNRRLPITGPLWWTYTSSLFFRLLFEAGFMYALYYVYDGFQMARLVKCEQWPCPNKVDCFISRPTEKTVFTIFMVGSSAICIVLNVAELAYLIVKALLRCSARAKGRRSFVHQEKMSTEKAHLQNEKNARLLSSASDSSSNKTV | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 267
Sequence Mass (Da): 30323
Location Topology: Multi-pass membrane protein
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A0A945CCT2 | MSDFLDYVEIQILSGNGGNGLASFRREKFIPFGGPDGGNGGNGGDIVFVGSNNLNSLRDFRNKRVFKAQNGTNGGSNKRNGKNGSNKVIRVPLGTEILELNTNKKIADIVTEDLEVVLLEGGKGGLGNTFFKSSTNRAPTKYKDGKKGEKLRLALNLKTISDVSLIGYPNVGKSSIIRKITNSKASVGNYQFTTITPNIGVLEAKNKDFLIADIPGLIKGSHSGKGLGHQFLKHIERSDCLIEVLDTSCLNIEELQEQHDTLLFELKEYNIKIISRIKLIVLNKVDACKFRDELSKFKPLKNCSTILASSLDGFGMEDLKREIEAI | Function: An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
EC: 3.6.5.-
Subcellular Location: Cytoplasm
Sequence Length: 326
Sequence Mass (Da): 35664
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A0A2H1JJG8 | MTAVSAATATTDLYPTRSGETTEVLPRTGPIVFGSPEDGPLEAADLKHFEDTGYLTIDQLITSEELTLFTDELQRLSRDPEVKADERTVVEAESDEVRSIFDIHRTNEIFRKIANDPRLVDRARQILGTDVYIHQSRINYKPGFVGKEFSWHSDFETWHAEDGMPTPRAVSLSLSLTDNYSFNGPLMIMPGSHKRYISCVGGTPEDNYRKSLIMQGAGTPDRQTLSDFADEYGIDVLEGAAGGAIMFDSNCMHASNGNVTPFSRSNIFIVYNSVENTCVEPFAAPKPRPEFVGSTDFTPAGR | Function: Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine.
EC: 1.14.11.55
Catalytic Activity: 2-oxoglutarate + L-ectoine + O2 = 5-hydroxyectoine + CO2 + succinate
Sequence Length: 302
Sequence Mass (Da): 33416
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A0A379LNX0 | MSLLTPHLSDMLLPLWLSIKLASITTLCLLLFATPMAYWLAKPSSSTLIARVKIMLMGVIAMPLVLPPTVLGFYLLLLLSPNFALGQWLMAHNIGALAFTFEGLVLGSIIYSLPFYVQPVYAQFLRIPKSVSDMALLLEPSRLRRFTAVSLPQAKTGIILGSLISFAHTIGEFGVVLMIGGSIAGETKVISIAIYEQVEALNYEMAHTMSLLLVVLGIVLVGLIASINRQVNEGFASRPKSKSMK | Function: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell inner membrane
Sequence Length: 245
Sequence Mass (Da): 26647
Location Topology: Multi-pass membrane protein
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Q5TYP2 | MVASQCVLGFLLLVAVFSARPQARSFDQRMIMEGPHLLDNNFRGYWDQLQSPVKVESLRAPLASNLVSSVQSKQEMLSPVSSKVDWRFPLVREEPAQLDVNFQLRQPQTPNTVAVQCLENGVHVEVKQDFFGTGHLLEPSSFSLGGCGVLNVDTAAGVLIFQSALQDCGSQLVMTDDELVYVFTIDYKPAVLPNIPVVRSNSASVNIECHYSRKHNVSSSALLPAWTPYAATAVAEDVLVFSLKLMTDDWMYERPTNVFFLGDIFNIEASVSQYNHVPLRVFVDSCVATATPDVNAAPLYSFIENHGCFTDAKYTGSASKFLPRVKDDKLRFQLEAFRFQKEISGFIYITCLLKATVATQSLVNEHHKACSFIKNGWVSADGGDQVCACCDTSCGPRTAFTASQAGIQYEGRAQVGPFQIPSQSSGIKVVSF | PTM: Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular Location: Zona pellucida
Sequence Length: 432
Domain: The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Sequence Mass (Da): 47528
Location Topology: Single-pass type I membrane protein
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L1I7G2 | PERPYQAREDIQKISVVHWGQRKLFVAEMSFLSAHYTPSITTVVYAGAAPGTHLVELMLKFQKLSWVLVDPEPFHHKLRDFYSSSVTLIQDRFTDAFAAQFAGRNDVLFISDIRTADHNRDNKEENERKIAQDMQNQKRWFRIMNPVAALLKFRLPWDNRMTTYPMGKIQYPVWGRVSTTETQLIVLQNAPDTVYDNKRYESKMFYHNTIAR | Function: Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase OPG063 that creates mRNA's poly(A) tail. In the presence of OPG102, OPG063 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.
EC: 2.1.1.57
Subcellular Location: Virion
Sequence Length: 212
Sequence Mass (Da): 24915
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Q8JHW1 | MGDWNLLGSILEEVHIHSTIVGKIWLTILFIFRMLVLGVAAEDVWDDEQSEFVCNTEQPGCKNVCYDQAFPISLIRYWVLQIIFVSSPSLVYMGHALYRLRALEKERHKKKVQLKVELEESEALEEHKRIEKELRKLEEQKKVRKAPLRGSLLRTYVFHILTRSVVEVGFIVGQYMLYGIGLTPLYKCERDPCPNSVDCFVSRPTEKNIFMIFMLVISGVSLFLNLLEIFHLGVKKIKQTIYGSMYSDDDSICRSKKNSMVQQVCFLTNSSPQKQLHLTHTSLAMAPDGQMVPLPIYMQTAGHVVSNINPNGSVQPLRQDRLPSQPEIQVLQQLGIKERRSIPDNRLQSCSSEDSGPKGSEPPKYSQQPRASFRASHIEIPAALRKHSRVSQCKDFSEESDSVESGNYPTARKASFMSRGLSESPSESAASKSGSDTEANRITQGESPAMTPPPAAGRRMSMVRKF | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 466
Sequence Mass (Da): 52612
Location Topology: Multi-pass membrane protein
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A0A947RVD1 | MSIRPVHVAGGGLAGCEAALQLARFGIPVVLHEMRPARETPAHQGEALAQIVCSNSLKSVDPTAASGLFKAELASAGCRLLAVARACAVPAGAALAVDKELFSSRIEALLAGDPLIEIVRDEVTAPDVAGDAFWIIATGPLTSADLRLRLEALTGGAGLYFFDAIAPTVTLDSLDLDALFRAARYGKGEADYLNAPLTRPEYEAFHAALTGAARAGVRDFDRSHLFAGCQPIEEIADSGLETMAFGPLRPVGLADPRTGKRPHAVVQLRQENRAGTLYGLVGFQTRLKRAEQRRVFRMIPGLGRAEFVRYGQLHRNFYLDTPRVLDRAFALAARPRLRFAGQITGVEGYVESIASGLTTAWSLAAELRGMRLPPWPSDTLLGALLHGFLFDGTGGRLTPMNVNFGLLPPLAQPPRGRGARRQRREALSARSRESLTRHLRSPSLQRLLAADSTR | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
EC: 2.1.1.74
Subcellular Location: Cytoplasm
Sequence Length: 454
Sequence Mass (Da): 48861
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A0A6P4ZRX1 | MPEGPLCNLLALCECPGTMWEGSRLRLPCGVRVRFLYDPQGWCALGIISFIWAYNTVFIPSLVIMPMYHDNRLPLATPVFYFLMSSLTVVCLYLSVTTNPGTVPLDIQPSAVEAADWTVCKVCQIRRPPRSHHCRRCQQCVRKMDHHCPWINNCVGEENHWLFMQLLYYTLILVSLSIALAALHLYYSPPCSYCNPGIFPFSYTRPLLWFTCGQGVFFFPAAIGLVFGQTFNIILDRTTLENLADPYFRSGVPSPRAIHEAFSDICGTKNVFCWLWPLRRRRAITAQAGYSYYRHM | Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
EC: 2.3.1.225
Subcellular Location: Membrane
Sequence Length: 296
Domain: The DHHC domain is required for palmitoyltransferase activity.
Sequence Mass (Da): 33914
Location Topology: Multi-pass membrane protein
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T1FN31 | MIKCHFLIYSILITSFHLLSVNQDDVLTSDFQSCLTTSTIPDLTDPDNSNNNNCKMICTKLHEKQLVTLINSIIPPLCNKLYKGQAGKIAVIGGSKEYTGAPYFAAISALKMGADLVHVFCTNDSSPIIKSYSPELIVHPMIDSPNVMERIKPWLDKMHAVVVGPGLGTNREILKNVKEIVSYVRAKNLPLIMDADALWIVVEDSEVLRDYKKAVLTPNLVEFSRLYKSLTNTTLNDADAHEPVESVKKLSNLLGNVTIVRKGYQDIITDGVQVVISEVSQSNPRRCGGQGDVLAGLIGTFSHWAYSSTYDDPLLKQLGPSLLASYGGSYLTKLSSYQAFAKHGRSTTTSDIIEILPTVAKDNFENY | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
EC: 4.2.1.93
Catalytic Activity: (6S)-NADHX + ATP = ADP + H(+) + NADH + phosphate
Sequence Length: 367
Sequence Mass (Da): 40403
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A0A1S6H945 | MAVNHVAIILDGNRRYAKKHNLPLYRGHEFGAKNVEKLFGWAEELSIKELTLYSFSMQNFNRTKEEFNYLMKVFEIFCKKAVAKLKKNPKVQFHFIGRLNLFTRKIQILARELERKSRNNKLLKVNFAFGYGGREEIVDAVKKIVKKGLKNIDEKVISDNLYLKSEPEVIIRTGGDQRTSNFLPWQSIYSEWFFLDKTWPEFNKADLKRIVDDFTRRERRFGV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids.
EC: 2.5.1.89
Catalytic Activity: geranylgeranyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + tri-trans,hepta-cis-undecaprenyl diphosphate
Sequence Length: 223
Sequence Mass (Da): 26447
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A0A161I258 | MASPKHSHHRASAAPPASSNSNSKHMSNSKQHARATKQRPLSLRRAMLHSFVCFLVGLLTGFAPSDWTDAASRAAVHANAAATAQVFRALHAMNNTAAAGALGHLLTLQHYQSYQQQGKQQQQQPPLDLVVVVTTTTTSTGLSERERRSAGLTRTAHALRLVSPPVVWLVVESAREAGPTARLLRRTGVVYRHLTYGENFTSEAWEEERHHQRNQALAHIEQHRLRGVVLFAGLADVYDVRLLEHLRRIRTVGAWPVATVWEQEKRVAVEGPVCTTAGTGTATAAWFSVSASEEAASTSPSPPVMTDDSVHGFAFASDLLWDPARWDRFPTSEPDQSQDSIKFVQRLVVADYNKTRPIPEYSNCSQIMVWRVDTTLL | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
EC: 2.4.-.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 377
Sequence Mass (Da): 41629
Location Topology: Single-pass type II membrane protein
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Q60I71 | MANSARERNKLWIYIIVLNILPRISSGQIAFSVSEEASPGTTVGNIVKELNLNLQELEHRGFQIVGPNKRYFDVNMKTGILQVKDKLDREEICGQSLKCALELEAIVNSPLNMYRFEVNVLDVNDNSPTFPSSRLQLNVSEAAFIGERYALPNAFDADVGINSVKSYKLSANEHFSLDAQSGGEQSVSAELVLQKALDREKQPVIRLTLTAVDGGKPPRSGTVHIIVNVIDVNDNIPVFTKSLYKARILENAPVEFSVITVNARDADAGLNGEIEYSFIKHGIDKNIESFAINKETGEITVMGKLDHESNNAIEIRVQARDKGSTPRVAHCKVLVEIMDVNDNIPEISVTSLINVVKEGSPKGTMVGLITVKDDDSGENGSVKLKILDSLPFALQNTYKNKYSLVVDGPLDRESASEYNVTISAADEGSPPLSSTSVIAVHVSDVNDNAPRFPEPVINVYVKENSQIGAVLHTVSAVDPDVGDNARITYSLLESSKSGPVTSMININSDTGDLHSLQSFNYEEIKTFEFKVQATDSGVPPLSSNVTVNVFVLDENDNSPAILAPYSELGSVNTENIPYSAEAGYFVAKIRAVDADSGYNALLSYHISEPKGNNLFRIGTSSGEIRTKRRMSDNDLKTHPLVILVCDNGEPSLSATVSIDAVVVESGGDVKTPFRHAPVKEESFSDLNLYLLIAIVSVSVIFLLSLISLIAVKCHRTDSSLGRYSAPMITTHPDGSWSYSKSTQQYDVCFSSDTLKSDVVVFPAPFPPADAELISINGGDTFTRTQTLPNKEKPKVPSSDWRYSASLRAGMQSSVRMEESSVMQGAQGVLVQNWPTVSSAPDNEGGEVSPPVGAGVDSNSWHFRYGPGPGGPPHLKPGEVPPEAFIIPGSPAIISIRQGQDGDDKSDFITFGKKEEAKKLKKKKKKEKKDKREKGKDDDD | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular Location: Cell membrane
Sequence Length: 939
Sequence Mass (Da): 102075
Location Topology: Single-pass type I membrane protein
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T1G978 | MSVADFKPSNVSNGIKRRNLTDGIIEIGSFYKVRKADGRLHTAEVIEVRNDEQKDGQVEYYVHFVGCNRRLDSWITLDKFDSFTKVQDVYKDVNASMNAAKISEMEEEKNSDRKMTRNQKRKYEEMNHIPTSYSDMDPTTAALEKEHEAITKVKYIDRVQMGKYEMDAWYFSPYPEEYGKQTKIWVCEFCLKYMKLEKTFRYHLTECVVRYPPGKEIYRKMSLSLFEVDGKEAKLYCQNLCLLAKLFLDHKTLYFDVEPFMFYILTEVDRHGAHVVGYFSKEKDSPDGNNLACIMILPPFQRKGYGKFLIAFSYELSKLEEVIGSPEKPLSDLGKLSYRSYWSWVLLEHLKDRKGAVSVKELSESTSISHPDIVSTLQSMNLTKYWKGQYVVCVSQKLIEELIKSNHYKRPSLIVDRTCICWQPPPKKNFKVNRK | Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
EC: 2.3.1.48
Subcellular Location: Nucleus
Sequence Length: 435
Sequence Mass (Da): 50936
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A0A0M8KC05 | MNEQTVLTQLEAVIRQRKAERPEGSYTTTLFDGGLDRILKKIGEEAGEIIIASKNANPDEIIYETADFLYHLLVMLAYHDIPWRDVENELQRRFGNRPH | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
EC: 3.6.1.31
Subcellular Location: Cytoplasm
Sequence Length: 99
Sequence Mass (Da): 11484
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V5IN23 | MAHQLPSTLDLGNDVSLDVSTAPTTPGSNLSFSPVLQAADEQPGIPAMKPQSTSRSLSSTLFDTTARTPPVRNICCVGAGYVGGPTAAVIAFNNPHIRVTVVDKDEKRIRRWNSVHPPIYEPGLNHILRIARDGSKECTIETRSLSTTNTTSSNTPDVSDASTPASECGSQCGDNVSKPIPARQPNLFFTADVAKSISEADIVLIAVNTPTKSRGAGAGSATDMTAFEAVTNVVAQHARPGAIIVEKSTVPCRTAQFVQDTLALHRPGIHFEVLSNPEFLAAGTAIKDLLNADRILIGSSATPSGQRAAAALASVYSAWIPRSRIITTNVFSSELAKLVANSMLAQRISSINSIAAVCEVTGADVSEVAGAIGADPRIGSKFLKAGIGFGGSCFKKDVLSLAYLAESLQLPEVADYWRNVITMNEFARNRFASRVVRCLNNTLIGKKLTMLGYAFKKDTNDTRESPAVEIIRTLVEEGPREIAVYDPCCNPAQMAEDIGRYVGAEVLQRNGGPVIVYADAYEACHSSDALLITTEFDEFKNTGEPVSASAEVLAPKAAPVKAVVPDPRPFKGEEPTETELLALHTFLLQSTDAEDKEDPLHRFNSVPDCAEDCPDCFIEKETGTSGYGAGQEHVFKGRLDWRKVHYHMHKPHWVFDGRGVLEVAGMEKLGFRVESVGRQGRV | Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Length: 682
Sequence Mass (Da): 73204
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A0A327KDN5 | MRNVPQIIGLATAAFALALDQVTKQIALSNLAPGVAVPIAPFFTVRLGFNEGVSFGMFAGWFSGRPLILAAIMMGIIVLLAVWLWRTPRRPQAVALGAILGGALSNVFDRLRIGAVVDYLDFHAWDHHWPAFNFADAAIVCGVAILVLGDVMGRPNDREGQRELR | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 165
Sequence Mass (Da): 17877
Location Topology: Multi-pass membrane protein
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Q1PYN7 | MKILGIDPGTLIAGYGVIEKSGAEIKAVAYGSIKTGKNQNFPERLKTIYTGVTELITIYKPDHMAVEEVFFGKNFKAAIKIGEGRGIIFLCAAMANIPIAEYAARVVKKAVAGNGNAHKGKVQEMVKAILGLPEIPQPEDASDALAIAICHGHRL | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 155
Sequence Mass (Da): 16516
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Q504A1 | MVSHSLVLPMIGFTTLWGLVGIVAPFLVPKGPNRGVIITSLVLTAVCCYLFWLVAILAQANPLFGPQLKNETIWYLRYYWE | Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular Location: Membrane
Sequence Length: 81
Sequence Mass (Da): 9125
Location Topology: Multi-pass membrane protein
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L1K448 | MSDSQDAAKSKEGSKDEQSSWQDNCHGVSALAIKRLIKFAHCKDKTLLIYGGLKTMLVADCSTGSLMELEQSHTERVTSVTVGKDKEVMVSGGNDKRLVVWQLPEMKVASKTVTDKKVVSVVLDEERRRVVFAEIAGEVFQKPIDDLDSKAEHLLGHISSLTDMRISPSGSRLLTSDRDEKVRISNFPHAFEIEAFCLGHTELVTCIETFTLAEEELLLSGGADGSVRLWSVKDGSLLDTYMIDPAGEEEEGEDGQQADSQPLAEEPKTWDRFAAGTAQATAAVSGRMRRRTNSPAVVALAYCPRLSLAACIIENQREVLLLQVSGKELKELNRVEVDQMPVGIEIDDVEHEGKAECFMLVAVLDDRPKLEAFRVEGGKECVVKKIDLKSSKEESKIISAFACLSEEMSTRQEESHKASGQDGSGQYFQKRRRHTEPGFKQYQGKAD | 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: 447
Sequence Mass (Da): 49387
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H1XT72 | MFTHLKICGITRLEEAQKIAELGVSFLGFNFYERSPRFVTTGRAREIIRQLPAWVNTVGILVRPTLRECLQILKHTEIKFLQIYDPLDFTDFNRLPAPVIAAFRLKDGVEFSYQRRGEQYVLLDAFHSGVYGGTGRTLNWLQLPAEVPRERLFLAGGINPDNILKALTAVNPAVIDVASGAERAPGVKDLEKVRAMQMTVLSFNLAKIDRAKQNGNN | 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: 217
Sequence Mass (Da): 24413
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A0A6P4ZMB0 | MSSTSPTVTELTPLACLDPQNKGVRIALIVLNQPQSLDVLAVLWTKAAVLKAVTDGGVNRLYDATRNNPESWIPDLITGDFDSASSENLQYYKDKGSEVICTPDQDHTDFTKCLQLVVQRMQERNIQVDYIVSVGAFGGRMDQVMANINTLYEARSLTSIPVILLDEVSMAFLLSPGKTLLHVQTGGEGEWCGLVPVGGTCPHVTTTGLKWNLNDQALKFGELISTSNTFDQSAAGLVTVETNDPLLWTMGVNVQRS | Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.
EC: 2.7.6.2
Catalytic Activity: ATP + thiamine = AMP + H(+) + thiamine diphosphate
Sequence Length: 257
Sequence Mass (Da): 27961
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L1JH97 | LQFHIHTPSEHTIDGEHYDMEIHFVHKTDDPKAKSKVRPKGASATRLTGRQIMVMLLPIDFADISQTVMIGSLTHRGADAFSFVPNFKNYLTYSGSFTTPPCSEGVQWVLLRNPIYVYSKDLQVIRSLEGANARPAQPLNGRHV | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 144
Sequence Mass (Da): 16175
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L1JJF8 | MLRVLYLCFYNLFGLCGWAMILFQVVSILLEGRVTNLWKELEGTVKLVQGAAVLEIMHSLLGLVRSPVSRTFVQVTSRLLTVWASMDPLYTYPYTPFPKGKGCNYSIDVVECSEEWNYYIGAMTLIAWSFAEIIRYSFYGINTVSPKSVPFVLVWFRYSGFIILYPVGVAGEMLCAYMTLPLLQKGMCPRFEGFLQTCPSYSVTLLYVFLANYVSCEDKACSAVEDGVWGLPWLYTTMLGERKKRLYPKPAPKLQGVVFPVSKNGERSTTNAAKEIFAMAMESTDAKMADKVKKEKNWRFGYTKHILNNLVVSAKSQKHQKLTKVLQGDRDC | Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 4.2.1.134
Subcellular Location: Membrane
Sequence Length: 332
Sequence Mass (Da): 37679
Location Topology: Multi-pass membrane protein
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L1JFY6 | MSLEDNKKEEKVLNGIKHPRERFVALTRELGKNLKLEKALSEKGVRTVELPCIAFEAGIDSDSLPSALKEDWEYVVVTSPEAASVFLDAWRLASQPSLQVACVGTGTKQALQEGGIEPVFMPSKATGKTLADELPGPQGNGRVLYPASAKARTEVQGGLTARGFTVTRLNTYDTVSATWSEQELQMAASAAVVALASPSAVKTWAERLGTKQYAACIGETSASACKELGFEHVFWPESPGIPGWAQAVHDALEEMESAEMSRSK | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O + uroporphyrinogen III
Sequence Length: 264
Sequence Mass (Da): 28383
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L1J5G3 | MAEAARSERTGGDDGGDEGERMAACTREKKVEALEEEDETAEQKGMSEHGALTIEDPSAGKGSIKKRLGRQWHKYCQTLPRHYKGGLMSSDEVDAKRAGQNVERRRPEKGDHHKDSHRRAGLPEHQRCSFWIEQKKRLCSRPRMERSSFCIGHQVAQGADGKEDSSEARECEFCRTRILPDRYESHLKRCNVRTREDAMRSCPYYKQDINSGSQGRPLPSSQPVMSDAEDPVGFVGRVNENYEIHVRAIEEQDSSLISNMEDKGLLNHVTDSTFIEFGAGKAMLSLSLVQCDEAVNLLLVEKDSGHMKGKADRILRLRSRGAFQRLTVDIRHLDLRAVPCGEIPLMSSVVGISKHLCGVATDLALRCLVNYHHSGGPGENQGPNAVKGICIALCCHHLCTWDDYVGKKFFVNDLQIGRGGFEMMCKYASWATGCRQHMNEKQKTGDNNVEQQDSSQHHHNAKITMSREEKVLLYI | Function: tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His).
EC: 2.1.1.225
Catalytic Activity: adenosine(4) in tRNA(His) + S-adenosyl-L-methionine = 2'-O-methyladenosine(4) in tRNA(His) + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 475
Sequence Mass (Da): 53350
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A0A174BXQ4 | MTKQKQSLIISFLIGFAILAGLDQWTKGLAVQSLKGQKPFVIWNGVFEFYYSENRGAAFGMMQEKQLFFFLIAVLVLGAVAYLIWKMPPEGRYRPLAVCLMMISAGAVGNMIDRVSQGYVVDFLYFKLINFPIFNVADCYVTVGAACLVFLIMFYYKDEDMACFSFKKH | Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or Ala) have small, neutral side chains.
EC: 3.4.23.36
Subcellular Location: Cell membrane
Sequence Length: 169
Sequence Mass (Da): 19219
Location Topology: Multi-pass membrane protein
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F6P1M3 | MADHRVAPVVGFLLFLVAPVWSGCPSACRCSFAMLQCLESDGITSIPALAAQESENVTEIYIESQPNLENITDVDLANYRELKNLTITDCGLVYISENAFQHNFKLQYVNLASNALTHISWRVFQSVTLLSLILRDNLLTCSCDIYWLQQWHRKRLNEIDSQQNCIYNGSQIPLDSFEMDNCSVPEVMIDPPTVTTQEGGNLTFTCRVTGVPTPTIHWRTEQLRSSWTLEQGIWGSTLEVVLHMRNVSSADNLHNLTCEAENRAGMGDAVVQLDIEFPVRIIYLKNPESQHHWCFPFAVDSNPPASIKWLYNNMPLTETRYAYTELIRDVYDGSQQHGCLFLNKPTHLNNGNYTIIVKNKLGRDQRTVRAKFMDNPFDPSDPEGIIPVLNDDPTAPTNQSTETEKIESRVFGVSVAVGLAVFACTFLLIMVVVINKCGQHSKFGIHRSSVLGTEDDLAVSLRFMNFGASPPSSDDGTLDSGLSSFVENPQYFCGIIKDKDMCVQHIKRKDIVLKWELGEGAFGKVYLAECANLCPDTDKMLVAIKTLKIANESTRQDFQREAELLTVLQHEHIVRFYGVCADGEPLAMVFEYMRHGDLNRFLRAHGPDARILDEMKVPPMGQLTLPQMLHIAAQIASGMVYLASLHFVHRDLATRNCLVGEGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESIMYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNSEAIECITQGRELERPRTCPKEVHLLMQGCWQREPQQRLVIKDIYSRLVALVKNPPVYLDILE | Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
EC: 2.7.10.1
Subcellular Location: Cell membrane
Sequence Length: 797
Sequence Mass (Da): 90265
Location Topology: Single-pass type I membrane protein
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L1JUK2 | KLEPAVQNYEWGVRGGGQSSLVARMANAQVAEEKPFAELWMGTHPKAPSVVLEDGWSGMVLGEFLRLNEVFMGSKAGMFGGDLPYLFKCLSVAKALSIQAHPDKTLAKLLHARDKPNYPDDNHKPELACAVTEFEGLCGFRKLDEIVENVGAVPELKELIGQDTVKLMESSLDKDAQSRAEALKQAFNMVMSSPEDRVKHQASKMVDRLKSSQKLRDVEELVLRINEQFPLDVGLFNIFFLNHVKLRPGQALFLGPNLPHAYLSGDCMEIMATSDNVVRAGFTPKFKDVATLCSMLDYERSGPAEIMEGEAREGMRVYAPPGHDF | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
EC: 5.3.1.8
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Length: 325
Sequence Mass (Da): 36013
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R9KZH4 | MKRNLLSIIILALLVVNIVLSAIMMVTVSSASRKTAALVADISAIIGLEIDGLPASDVGAAPVTMADTAVYNITAEMTIPLKNDEDGTGHYAVGNVSLSLNKTHDDYKTYNEETLATSEGIIKDIIYGVLGEHTLEEARNNTEQIKAEILGKIQEKFGSEVIYDVSFNFLYS | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 172
Sequence Mass (Da): 18553
Location Topology: Single-pass membrane protein
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A0A7C4JPD3 | MQLRCPRGTRDLWGDELATARFVVSKMRSVFERFGFQEVQTPIFEHLELFLVKSGSEIIKQIYDFEDKSGRKLALRPELTAPAIRFFIQHLKRNPPPVRLFYFGECFRYEEPQAWRWREFTQAGCEIIGSPNPQADAEVISLTCEIMREVGMNDWKLRIGDVGILRNVLASVGVKEEKQDPILRAVDSGNRNRILEELRKAGVPEEEYERLLKIFSLRGDFRVFQKLSEFDIDESMLERSKELLRILREAGEKFEIDLGIARGLDYYTGTVFEVYVGDVQVAGGGRYDTLVERLGGPKTPATGVGFGVDRISSLLLKDSKAEKPIKPLVYVVPLERDLLPKALEISNMLRRKGIVTEMEVMERSLQKALSHADSMGMRFAVIVGRREVSAGQVALRDLKTKKQETVKIEELVSALKSVA | Catalytic Activity: ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His)
EC: 6.1.1.21
Subcellular Location: Cytoplasm
Sequence Length: 419
Sequence Mass (Da): 47731
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A0A133Q8B0 | MQKVSQYIIAFIAAIIFVFILNVFIIQGAVVKQQNMAPVLQKNDRVIVNKVKVTFNILQHGDVVMFRQHGDLKFSRIVGMAGESVEVKQGQLYRDDRQIKAPYAKNIKTDFQLRNLPHSEGDIIPPDKYLVLSDDSRLNKQSQSYQLIDKKDIIGDVNLTYYPFHHFRYNYER | 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: 173
Sequence Mass (Da): 20132
Location Topology: Single-pass type II membrane protein
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