ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
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stringlengths 117
4.4k
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A0A2R6WQX4 | MAHLLSWAQGIVPNPRSPGVHHDNVHFQGSFKSVPTWAGRATVLYQPKSGDSCSNSLLRNSRAIRFSATSRPDSQGRTDATSVEPVETTEGRIAKLLAANERLLARIADLEKVVNEVRAENAGYIEDKASATPVASSSQAPNAFKSPEPGISLESDSGTGAVTVENSSLSQQPLPAAQEATLILSQLANIRWPSPNDEVPFWMRKSNVHDHVTSFIDNSGAGRKIEPDKNPLYIVHVTAELAPVAKVGGLGDVVTGLGRTCMERGHKVLVMLPFYESIDTTQVEGLAEAETFSSFHKGSWLPVKSFHGKVAGVPVLLIRTDNNLFKGSQIYGGDYDEMEAYLFFSRACLERMQVTGDQPDVIHIHEWHTGVLAMLYWDMYNHLSLKKPRIVLTIHNMEHYGECRVEQLNMCGLDGSAYGTIDRAIDERTIGHNPERLSLLKGGIVYSNAVTTVSPTYANETLCSGWLANTLLRNRSKYFGILNGIDTTVWDPASDPCLPMQYNARKIFGKLVCKQYVQRGLGLEADDLVGDGIQLVRRKQTPLVICITRLVAQKGIHLIRHAINQIGERGGQFVLLGTAPDPRVQAEFEQMSQKLQTSKNIRLLTFYSEDLAHKLYAAGDIVLVPSMFEPCGLTQMIGMRYGAIPVVRRTGGLADTVFDIDDPKNKNRGNGFVFDGISEDSLDSALNRALTYHQERREWWQDLTARVMELDHSWNKSAAEYLNLYNNVRVG | Pathway: Glycan biosynthesis; starch biosynthesis.
EC: 2.4.1.-
Subcellular Location: Plastid
Sequence Length: 731
Sequence Mass (Da): 80886
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A0A2A5QFX6 | MLGRKRVNEALALMGEMFPNAHGELEWETPFQLLVAVILSAQTTDKAVNKITPGLWARYPGIEDLASANLDDVEMCLRTIGLYKNKAKNIIKTARAVLMNFDGQVPKTHKELESLPGVGRKTANVVLAEVYGIPSIAVDTHVSRVSKRLNIVPEDASVEEIEAELMKKIPKRDWIISHHRMIFFGRYHCLAKNPKCQTCPLQSYCKYYKETTKK | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
EC: 4.2.99.18
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 214
Sequence Mass (Da): 24167
|
A0A286R600 | DKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTAYIKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Catalytic Activity: 2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5-bisphosphate + H2O
EC: 4.1.1.39
Subcellular Location: Plastid
Sequence Length: 178
Sequence Mass (Da): 19632
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A0A1S4EB26 | MLNQAVLEAMYSVPYVETYLDVVENLPDEIQRYLTKIRELDVCYHSYMKEIETIASQQASSEVFRKRNLSRVQVALIAAQEIGDEKLAILQQVQDIIENKTRQLDGIFCDLPFAKAETAKKEDNGDVNAKHDEKKSSGENQTEVEAPKKRTRRKRAEIEAAELIEHTTSTPLPRSSATIEVPKKSAATEAPVKKRKRKSKQAEKDVSIDPNEPTYCLCNQVSFGQMVMCDNDHCPIEWFHFSCVGITNTPKGKWYCPDCRKARSSTVRPKK | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 271
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 30840
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A0A950JYZ6 | MKIIIGTRGSRLALAQADLAREALSRTGAVDEIEVRIIKTAGDQRLDVRLSDSGPQLEKGLFTKDLEQALLNREIDVAVHSLKDLPTETALPIVAVLPRENPADVLISKAAGGLDALPKGALVATGSPRRVQQITYRRPDLKVCDIRGNVPTRIEKLIRSENWSGIVLARAGLRRLGLEEDQGRLRFGQSVVFVAELAEMLPAAGQGAVALQSRKEGGIQSLLDQINHRDTWSCVTAEREFLRLVGGGCNVPIGVRADLTGGSIAMTAIIFESTGKVRSASVTVPFRSPHDAARILFENIYAERR | Function: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
EC: 2.5.1.61
Catalytic Activity: H2O + 4 porphobilinogen = hydroxymethylbilane + 4 NH4(+)
Sequence Length: 305
Sequence Mass (Da): 33050
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A0A1S4ENH7 | MYSYYFLAALGPHMQKHLWWKKYITRLQLIQFAIILSYAVALLVNDCPLPKALNWIMAFQSTVFSLLFANFYYKAYVRSPTKKLKQQDDEAREKQRQFEKHQQMLNNNNNNNNITPPEELAKKVVNFTQS | Catalytic Activity: a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
EC: 2.3.1.199
Subcellular Location: Membrane
Sequence Length: 130
Sequence Mass (Da): 15452
Location Topology: Multi-pass membrane protein
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A0A1S3D4S1 | MDLILHERQEGCLCAQHCLNALLQGSYFTPVDLASLGQRMDDEERMRMAECGEESDEYQKFIKQPSGNMDDSGFFSVQVISSALEVWGLELVPYSSSDPKAIQAREGPE | 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: Nucleus
Sequence Length: 109
Sequence Mass (Da): 12206
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M4DD87 | MGRLYLRRDELALIILYLNKAEARDKICRAIQFGSKFLSGGHPGTAQTVDKNTSLARKVFRLFKFLNDFHLLIGPVPKGTPLPLVLLGKSKNALLCTYYFLDQFVWLGRSGIYKNKLLTDLIRSFAIFCWLGSSLCNIAIQIGELIMHSSSMKKMEKELKDDEEQDKEMDRAAKLQKSKDRILALIKSSMDTVVAIGLLHLVPFIVTTRVTGAFGFVTSLISCYQLLPGRPKLKTP | Function: Involved in peroxisomal proliferation. Promotes peroxisomal duplication, aggregation or elongation without fission.
Subcellular Location: Peroxisome membrane
Sequence Length: 236
Sequence Mass (Da): 26570
Location Topology: Multi-pass membrane protein
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A0A069PZ33 | MSTRLSSRGFTLIEVLVALAIVAIALAAAIRAVGLMTDGNGLLRDKSLALLAAESRLAELRLGVGAAPGNSDFECSQGRLRLYCEQRVEATDDPALLWVEIRVRTQREQAVPLARLNTLLSRSR | PTM: Cleaved by prepilin peptidase.
Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm.
Subcellular Location: Cell inner membrane
Sequence Length: 124
Sequence Mass (Da): 13430
Location Topology: Single-pass membrane protein
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T0BM73 | MKILYIMGFGFVGGVLRFSCGDSLTSILILNAAGAIALAMISSFAVHRTVWLETGIGVGFIGSLTTFSSLMFVTVDAYSQHSIEVLASMGITVGSIALCGLAMALTRRTKGRAELNDEPRDNQQNTRNQSRMPAHPSAPMGDDMQRV | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 147
Sequence Mass (Da): 15729
Location Topology: Multi-pass membrane protein
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A0A2R6WD91 | MEDCCAVCAEPLEWVGYGPCGHREVCFTCIARLRFVLNDKRCCICKQDCPQVYVTKALGDYTRVVTDWKVLPSRLGSSTAEGGDLWYDNVVEAYFDDEEPYKTIKAMCRLFCSVCENASPEDSGGKGMMKKGYIFKNIETLRRHQYTAHRVYMCELCLEGRKVFMIEQKLYSKSQLDRHNYKGDSEVDGTEEERGGFAGHPECAFCKKRFYGDNELYQHMSQEHYTCHICQRARPGHYEYYRNYDDLEAHFRQEHVLCEHPECLAKKFVVFPSEAELKRHNATTHGGHMSRSQRNAALQIPVSFHYRRTGQDSADDNNGGYSNRRSGRGRGGHPYSGGGGGGRSDHLDAAVRASVESAHLEEAVRESSAMSASSSDRPGSNNPQAGSERGISGESEAGFSGQGDGENEPSRYLAAVWGAGPSALGDAAFPPLPGTSKSSRRRAKSKNQGPASMAALLGGNGIGGGGRGGIRVLNTADHRHTSSSTQMRSVVEVDRTYTGQNSTSRREGLGTFVDTRIESSQAPSVSAVGGPGPPSVALRPATGGESSSSGNGVHTRGEWAVTRGPAGGASSVAGNGLPSRESAPVERSTMIKPLTAQVSELSLDLRAANKALVERIRTGLRGNEQQYADFKDVSARFRKGEMGSKEYYVHIARLGLSFIVPELARLCPDPQKGKELMEAHTTTITNNVVDPKSLPPGLAGAFPSLTSAREVERPAPKLAAMKSVVSDSAGSSGSSNGHTSKYIPEEAVEQLSSDGYRRAKGKNKIDMSSSTASTLSPYASTLPPFPALGTEGTLLNELAAARDRKPQVLVKAFPPLIQDPPQPQTSSATSDKPTASTPENGTWACVRCTLLNKASDLQCDACKTPQLVQIGKDAADAASASEKRKKKTSKFQRVRLGDGSAAALLDSTALNPWGQSSQSEIDSRNSGSSSGRGVWNNGGGQRLVSLVQREAIIDDAWSHGSK | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 962
Sequence Mass (Da): 103648
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V4SNA3 | MIDDQDLGFFANMLGIFLFVLVIAYHYVVADAKYEGN | 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 motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 37
Sequence Mass (Da): 4214
Location Topology: Single-pass type III membrane protein
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A0A2N8PTG5 | MNREKIEAAIEQLKKGQLVIVADDDDREAEGDLVGIANLATTETVNFMTKHARGLICAPISEKVAQRLQLSEMVERNTDSFGTAFTVSVDHQSTTTGISAGERAQTIKALADPQAKGTDFNKPGHIFPLIGKAGGVLVRRGHTEAALDLAKMTNQSEAAYICEILNDDGSMARRPQLEKLAEEWQLPMITVEELANYLTAQSRTTVQLPTEYGSFELTLFEDEQQREHLLLTKGDISNPKQPLLVRLHSECLTGDVFGSHRCDCGEQLHEAMRMIEAEGIGAILYLRQEGRGIGLKNKLRAYQLQEQGLDTYEANVELGFEPDEREYQFAAEILASYGIKEIRLLANNPEKVKELEERGIHVHQRVPLETAPLKENSAYLKTKKQKFHHLLSI | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Length: 393
Sequence Mass (Da): 43874
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A0A347ZZQ9 | MRTTLKPAQILSISLLLFAVFFGAGNMIFPPLLGLSSGENMWISITGFIITDVGLSLLAIVAVALAGGSFNTLASRVHPKFAAIFAIIIYLSIGPLFVIPRTGSVSYEIGIAPLFPDQWYSMLIFSAIFFTVVYFLSLNPSKLVDHIGKILTPILLGIIAIMATKAILSPGTFAEPVGDYKEIPFFKGFLEGFLTLDAIGALVLSTIVVNAIRQNGIPEKKSIAKYTIICGSIAALFLTIVYFLLGYIGASNGNLGQFENGGQLLATVMYHFFGTSGNVLLSIAIIFACLTTAIGVVSAFANYFATVLTNVSYKKLVLYVCIFSFIISNLGLSLLIKITLPVLIILYPITIILIFVSFIDKYTKRKPSVYIGAMIAAFLISCIHALDNVGMIPNFIANIVHTIPFYNLGIGWIIPAIIGGIIGYFIPQTEAEGEVSTK | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell membrane
Sequence Length: 438
Sequence Mass (Da): 47219
Location Topology: Multi-pass membrane protein
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A0A2V6DYA2 | MRITSKVLATVASSSVVALVLAAEHPAASVSADAALAKLKEGNLRFATSEVSQSKPTAARRAETAQEQHPFAIILGCADSRTAPELIFDQNLGDLFVIRTAGNLVDDHALGSIEYAVAHLGARLVVVLGHQRCGAVKAALESDHAPGHIESLVRDIQPAVKAAKGKPGDPLSATVAENARQVAAQIKAKAALGDLAKEVRIVSAVYDLDTGKIDWAND | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 218
Sequence Mass (Da): 22723
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A0A450ZFW1 | MSSSRLYLSATRRSSGKTTITVGLCAALRARGLTVQPFKKGPDYIDPIWLGMAAGYDCHNLDFHTMSHDEIREIFIRQSAHADINLMEGNQGLYDSVDVRGRNSNAALAQLLRTPVVLIIDTRGITRSVVPLLLGYQAFEPKVEIAGVLLNHVGDSRHEGKLRAAIDYYTDLPVLGTIPHDTDIEVPERHLGLIPGNEFGNSADFIARAAQSIEVNVELERLLEIADTAPPLVPEEQEPNNFLRNPGTDTTSAGKPSVKIGIPRDPAFGFYYPGDLMALRRAGAELIFFNTLSDTALPPVDALFIGGGFPEIHMQALQANIALRGSIHAAIRNGMPAYAECGGLMYFTRGISWRGKRCEMVGAIPAETIMHERPQGRGYVVLRETGKSPWKPLSDDGQSTEIKAHEFHHSSIAVISEPGEEIKYAYEVLRGHGIDGKHDGIVYRNLLAGFSHLRDVEGSRWAKRFVAYVRKISPSSGKR | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic route): step 10/10.
Function: Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source.
EC: 6.3.5.11
Catalytic Activity: 2 ATP + cob(II)yrinate + 2 H2O + 2 L-glutamine = 2 ADP + cob(II)yrinate a,c diamide + 2 H(+) + 2 L-glutamate + 2 phosphate
Sequence Length: 479
Domain: Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and cobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate.
Sequence Mass (Da): 52656
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A0A481ZJF3 | MSSNSFYLLLIPIINILLLYLNILLGPNKNYGEKGSSFECGFHSFLGQNRQQFNISFFLFGLLFLIFDLEIILIYPAKWLGKSFVWVIFSNSVDSLKILILNYNKKLWMDELIIHVW | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity of complex I.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.2
Subcellular Location: Mitochondrion membrane
Sequence Length: 117
Sequence Mass (Da): 13728
Location Topology: Multi-pass membrane protein
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A0A3L7AK94 | MTSGTNQSEARFDFVVVANRLPVDRYTTAEGEPGWRTSPGGLVTALTPVMERLGGAWVGWAGADTEGISPFTHNGTRIVPVPLSAEEVESYYEGFSNDTLWPLYHDVIAPPTYHREWWDSYVKVNRRFAEAAAETANERATVWVHDYQLQLVPGMLRELRPDLTIGFFNHIPFPAYGLFSQLPWRTQIIEGLLGADVIGFQRVADASNFTRAVRRLVGYETKGTSVYVPLESDSAPGQTGGYRRGGPTRHVLAKHFPISIDSASFEALARTPEVQARAAEIRSDLGGSGKILFGVDRLDYTKGIRHRLKAYGELLADGRIDPADVTLIQVASPSRERVETYRQLRDEIELTVGRINGDFGQIGHSAVHYLHHGYPREEMVALYLASDVMLVTALRDGMNLVAKEYVATRFDQDGVLVLSEFAGASDDLTQALLINPHDIEGLKDTIMTAINMPQPERAKRMKSMRKKVRENDVERWSTAFLAELERSAAARLDEARGHRVGAEQQ | Pathway: Glycan biosynthesis; trehalose biosynthesis.
Function: Probably involved in the osmoprotection via the biosynthesis of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor.
EC: 2.4.1.15
Catalytic Activity: D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-trehalose 6-phosphate + H(+) + UDP
Sequence Length: 505
Sequence Mass (Da): 56238
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A0A098GEA2 | MTLCYLGLGSNLNSPARQLRRAINALRRLPDSCITQEASFYWSEAWGRKAQPKFCNTVVALQTRLSPQRLLDCCHQIEQQQQRIRKIKWGARTLDIDILLYGSQKIDTLTLKVPHPRIIERDFVLLPLLEIAPSLTIDGLNLSSLVLNKPCSTHKVRV | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 158
Sequence Mass (Da): 18031
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A0A2W6EBR3 | MGELSPWHLLIVAAVFMLLFGANKLPHMARSVGQSMRIFKAETRALSGEKEPEQLPRTPSSSAAETSLQGQSSFQGHSQQPQPHQSAQPHQAPQPHQTPAAPAQSVPPPTA | 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: 111
Sequence Mass (Da): 11905
Location Topology: Single-pass membrane protein
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T0C0X1 | MNETLRGMWTRVVDRWKSVSPNMRRNVIIIAVAVLAALSALLWIVSRPHYVMVMSGLDDKSLGQVQTQLQTLKIPNEIEGSSVLVPAKDANEARVQLAEAGLPQSGYIGYSGVSNSMGMTQDEFNIQVLDALQQSLNETISSIDGVESAQVHIVMPQQQLFVSQTTQDAKASVFVTLGNGVQLSATQVAGIQQLVAHSVQGLSVNNVSVVDQNGNTLSNPDGAADASTVGGASSELALRQSVENDMTEKLTSGLQQIVGAGNAVVVVHANVTFNQTKSQSHVLQNAPNSTSGFVTSQNQEKSQSTNTNGQAGGPAGQAGSNPNSTTSYGASSSTAGNSTSSESNTTTNYDYSYENQTTTDDPMQIQGYKVGVLLNSNDKAMTPAEVQKIKSFVTNLVGQSPTTQGANTVSVSTVPFAQSAVAPSQSKSNWILYVVLGLLAALVGGFVLWWRRKRAGGNGPTDVPARIQDAYDEQLEELPPTEDEMLMSQLVNMARQRPDDFASLLRSWLSE | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 511
Sequence Mass (Da): 54358
Location Topology: Multi-pass membrane protein
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T0CJM3 | MKFTKMQALGNNYIYVSLFETKLPDVSLPELSTIVSDVRRGIGSDGLILIQDSRVADVGMRIFNADGSEAESCGNGLRCVAKYVYEHRLVNTSVFSIETKAGVVEAQVHVRPDGTVKQVTVDMGDAKFGVDSIRYTGSHAVGGDDVVIHVDDTKLRGTVVNVGNTHFVTLVDRVDDKYVEQIGPRIESHPDFPDRINAEFVSVINRSEIDFRVYERGSGVTFACGTGACASVAALARKGLVDNRVTVHLLGGDLDIELREDGHILMTGEAVTVAEGTFMWPTAEPAFLPL | Pathway: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step 1/1.
Function: Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Catalytic Activity: (2S,6S)-2,6-diaminoheptanedioate = meso-2,6-diaminoheptanedioate
EC: 5.1.1.7
Subcellular Location: Cytoplasm
Sequence Length: 290
Sequence Mass (Da): 31476
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A0A965CM17 | MQLIAGLGNPGEKYQDNPHNIGFRTLDQLMKALDLEGFQRRFNSEFQRTLENGQVTLMLKPETYMNRSGEAIAECARYFKIPSEKILVISDDLDLPAGKARLRVSGGHGGHNGLRSVIQCLGTDQFLRARIGIGRPDSSSSGKETSVSQYVLGKMEETKAELCLQAMEKVVEMLVRFVRQSRFQSTSISIPTPALPATGQG | Function: The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Catalytic Activity: an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-amino acid + H(+)
EC: 3.1.1.29
Subcellular Location: Cytoplasm
Sequence Length: 201
Sequence Mass (Da): 22189
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T0DN12 | MRRRDNQRTDERRRQRLRQDRQANELQANQATTHSVRNTWRIVLRVLLIWVVVFVVFSLAYWITNWFYHWLGKEPGSYWTHMTTVGVAIALILLTGFIMARFAAPRQQAFWQSLIDAIRQMAKGNFNVRIDVGQMGGPGEFHQLVNSLNNMAQELAQVEQMRQEFISNVSHEIQSPLTAILGFVEALKSEEITPENRQHYLNVIETESKRMSRLSENLLKLTSLESGAHPFHSESFRLDRQIRDVVLTLEPLWLKKGIEIELSLETTNVFADKDLLNQVWMNLLTNAIKFTERGGAIFISLGPEEGWTTVRVRDTGMGIREEDQQRVFERFYKADKARQRTESGSGLGLTIVKKIIDLHQGEIRVESQYGSGTTFIVRLPHPV | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 383
Sequence Mass (Da): 44274
Location Topology: Multi-pass membrane protein
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A0A945HY91 | MPTTTSIQKGMAISYKNQPWLIVSTKFTNPGKGQAFTKAKLKNLKTDQVIENTFKSGEAVELIDTIRKRSQFLYNDGADYHFMDNETYEQFQLDEAILGEATKYMKDGSECHALYIEGIPVSIQLQAKMEFEVTEAAPGAKGDTASGNASKEVTIETGTKLKVPLFINQGEKIIINTEDGTYVSKA | Pathway: Protein biosynthesis; polypeptide chain elongation.
Function: Involved in peptide bond synthesis. Stimulates efficient translation and peptide-bond synthesis on native or reconstituted 70S ribosomes in vitro. Probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
Subcellular Location: Cytoplasm
Sequence Length: 186
Sequence Mass (Da): 20588
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A0A8H6PRT8 | MYRNLFLAVLALLTAFAHAHTTFTTLYVDGENQGDGVCVRMNRNPSKATFPIEPLSSKDVACGYDGEKAVARVCPAKASSTLTFEFREYADGSQPGSIDESHKGPCAVYMKKVDDATADNNAAGDGWFKIWEADYDATAGKWCTEKMIENNGHISVQIPADIEGGYYLVRPELLALHAAQDSPPDPQFYVGCAQVFVQSTGTAKPPTVSIGEGTYDLSLPGMTYNIYKTPLSLPYPMYGPPVYKAGAASVNTAPANTAPATAASANPAPANTASANAGSANSASADTAPVNPAPADTALVNTASDDTGSEKPAPVPANVCKSKNKKKRTTKKKRAMLVQTKGLKPEGCILVRDNWCGFEVPSYTDEDSCWASAKNCWDQADVCWNTALPTGSAHCQIWSDKCTALGESCSNKVFPGPPNAGQDLTPRPASLVGSIKLFERGVRASCLGGAGNIVRESTKAMENEMRALGISEDDIATILVTIYWGINANTRKAAFWLLTYILHYGPQHYVDMIREETLPAFSPDKSIPDLDYLHDNCPHLDAMWNETIRLSAILCKGNRLMIPYQQLHFDESIFGVDYPVEEFRHELFMQKGRNLTRSDNWRPFRGGTKQCPGRYVAKRFVLLFVAMLLRRFDVELVTRRIPAAEEGKPMLGIMSIKDGEDVLVRVRPR | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 669
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 73000
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A0A6J2XB44 | MEAQVVSRENRSFFNSRLTSPTGSNDVQDANISDVEGKVKNRFLSMWNNMKYELNSVGMKLKPNFSKESPVWLLGMCYRKLEPPNPDSTELGTDVAAFQSQSEIVNNEEEGLDGFRKDFLSKVWLTYRREFPILNGSTYSSDCGWGCMIRSGQMLIAQALIVHFLGRDWRWNPDRREANYHQKIIKWFGDKPSINSPLSLHSLVKIGESLGKKPGDWYGPGLVAHLFKQAFKNAAKENSDFDYLTVCVAQNCTVYIRDVFAECVGKSPKAWKSLILLIPVRLGAEKFNTIYSPCLTTLLSIKECIGIIGGRPKHSLYFVGYQDDKLIHLDPHYCQEVVDVWAEDFPLSTFHCRSPRKLPITKIDPSCCIGFYCATKKDFLTLIETVQPIVVPPNGANDYPMFTFCDGFSCDEESITKDILPSDYQYSSTSDFEDIETEAFELI | Function: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Catalytic Activity: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine
EC: 3.4.22.-
Subcellular Location: Cytoplasm
Sequence Length: 443
Sequence Mass (Da): 50313
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A0A2R6WXI3 | MMRRVFRSGNLELLVVCVTGIILQLHNAEAYLSTESSVVSRTTFGDATATFYGGSDASGTQGGSCGYQNPFALGYGIKTAALSNSLLANNMNCGACFEVKCKYDASAYTKKWCYPNSPTIIVTATNQSPPGLNGEHHFDLTEPMFMKIANRIGGRIPIQYRRVRCYKPGGIKFTLTGNPFFNLVLVYNVGGAGNVYGMAIKGSRTDFYPMSRNWGQYWQAFVKLTGQSLTFRVTLGNGKSTTFWNVAPANWQFGQTVAATYNFY | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 264
Sequence Mass (Da): 28989
Location Topology: Peripheral membrane protein
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A0A947X4M1 | MTSDPSIVEEFIVEAQEHLENIEDDFLELGQQKESPDPALIDKIFRAAHSIKGGAGFLQFKNIGSLAHIMETLLSSLRSGTISVTDEIIEALLAGVDKLGAMLANADSSNDMDISAEHGTLDAILKGVGGKDTADVPVTTGEGLQTGFEITEFSLNNIPKNHDFLYILKYDLVELAKVRGKSPIGLIRELLSTGEIVDARIESAADDLSDGVPKGPLHYEVLYSSLIGPETIELAVGLPSDKVVVIDKSKLAPKPREVAAPVVEEMEDEFQLPITPEMIEQFVAESDEIVETVEQSLMEVFENPDKVQEGIAESFRLIHSFKGNCGLLGYKGLERVSHTMETVLDFFKTGVVPRREADRNILMKGVDTLREGVSELSKSGKLEPHDYSELIEELGSLLPSHKAAATARPARREDTDKSDTPKKTVERRDLRVDLEKLDVLINLVGELVIAESMTTRHPELEGMHLEGFDRSVHNLRRIIADLQDVAMAVRMIPLSRTFRKMIRLVHDLANKAGKQIKLELVGEDTEVDKTVIEQINDPLVHIIRNSVDHGVEPPEERIAAGKAGQGNVTIEAKHEGGEVLIIVRDDGRGLSREKILKKAVENGLIQGDGANLPDDEVFKMIFEPGFSTAETITDVSGRGVGMDVVRRNLEKLKGRVDVQSNFGQGSNVVLRIPLTLAIIEGMLIRVGDSRYTLPLLSIRESFRPEPEQVTITMDGLEVVRVRDEMIPVVRLHELYKIRPDAVDLQEGILVIVDSGRKQVCIFADEILGQHQTVIKALPTYLGSARGLSGCTILGNGEVSLIMDVSSLIAMAENSNLQGGQYVDGE | Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY.
EC: 2.7.13.3
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Length: 825
Sequence Mass (Da): 90515
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A0A0K0JD92 | MKAELTETRDIFNLLNVLNELKHLKRTGWVKFNIPEPETVACHMYRMAVLAMLLDNNDCDRAKCIRMTLVHDLGEAIIGDITPRCGISVTEKHRLEDEAMKKITEMVPSTVGEDWYSLWQEYEANETKEAKIVKHLDKFDMVVQASHYEQKYGIDLEEFFTTTKDSFTLEPFMSWNEELRMKRYIRKNATQENN | Function: Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
EC: 3.1.3.89
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate
Sequence Length: 194
Sequence Mass (Da): 22829
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A0A288Q8Q5 | MDNKALVAQAIAVAVPELDLATITAKLETPKSADLGDAAFPTFTLAKVLRKAPQQIATDILAKIDQSAFEKVVAVGPYLNFFFDKNATTNTVLRDVLAQGAAYGQNNDGAGANITIDMSSPNIAKPMSFGHLRSTVIGNAFANLVKKNGYNPIKINHLGDWGTQFGLMIAAYKKWGNKPIEEYSVDELVKLYVEINKAAKTDEAVADAGRNWFKKLEDGDAEAVSLWQTIRDASLSEFQEVYERLHITFDSMNGEAFFNDKMIPVVAEIKDKNLLTDSQGAEIVDLPTLLPDENLPISMILKSNGSTAYITRDLAAAEFRQREYDFVKSLYVVGAEQTEHFRQLKAILKLMGHDWSDDIEHISYGLITINGEKMSTRKGNVVTLVEVLNMAHEAALKQISEKNPDLPNKDLVAEQVGAGAVVFNDLMNERKNFIDFTPADAVKFEGDTGPYVQYTIARANSILRKAGVEVNVNDLQLDDAATWDTITLLKNFPTVVRDAWSKRDTSMTAKFALRLARAFNKYYANSKILVDDEQRNSRLALVSAVIIVLTEALNMLGVEAPSEM | Catalytic Activity: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
EC: 6.1.1.19
Subcellular Location: Cytoplasm
Sequence Length: 564
Sequence Mass (Da): 62271
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A0A956W774 | MDEWMRAALLGAVQAATEFLPVSSSGHLVIGHRLLGEPANPLAFDVGLHVGTLAAVLVEFRRDWLRMGRGTLALLVGGWGAARAIPGESRLVGLIAVATVPAVVAGLLLADLVERELRSPAVVALMLILGGVLLWLVDRRAARTRTEADLSFRGALTVGGWQVFALIPGFSRSGSTLIGGRSLGLERPAATRFSFLLSVPVIAGAAVLEIPSALADGAGLPIGPLLVGMLVAFAVGLVVIRFLLLYVAAHGFGLFAFYRVGLGILLLAALGAGWI | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Cell membrane
Sequence Length: 275
Sequence Mass (Da): 28605
Location Topology: Multi-pass membrane protein
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A0A2E9UPA7 | MIARALNRAITLQLSAYFDPFSPYLPVSFLTQNGYVFILDHYRMCSARLPETGWPPLNFRSSRRNPRLSNYIRQFEENPRLDSSHSPHGMIGEAYRPPKVGSKGAVVANHTMAAQAGMRILHLGGNAVDAAIAVAFALGPAEPQGSSIAGDGFVMVHMVENRKIDVVNGTGAAPLAATAERYSGGIPVTGILGTSVPGILDALLAAHGKYGTLPLAQCLEPAIELCEDGVPVSEFQSSQAAGNPVLRSSPTSSRVFAPNGQWLKPGELRRNPDLARTYWLIAEQGRDAFYEGDIARDIARYSEENDGLLTYEDLKRHRVEWQDAISIDYRGRTVYEAPPNSSGHVLLQELAMFGQFDPQEHGYMTPESVHLMIEAKKLAFADREAFLADPNYVDVPIEGLLDPEYLAKRAKLIDLDRAAENPVEGDPWSFMDRSPDPSKKHRIGGRLHSPGPDTTHFCVVDRWGNSVGELQSIQASYGSCVIAGSTGILLNNRMTYWHLDPDHIDYLNPGQRVRHTMNPVMVFSAPVERGGKLELVCGTPGGDTQVQTNSQIVTSIFDYGLNVAEAIDGPRWTHNQRGTNSYVLLRDANSLWIEDRAGDAVIDGLAKRGHPVESTGMWGGAGSVGAIQVNLENGTLFAAADPRREGDALVW | PTM: Cleaved by autocatalysis into a large and a small subunit.
Pathway: Sulfur metabolism; glutathione metabolism.
EC: 2.3.2.2
Catalytic Activity: an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate
Sequence Length: 651
Sequence Mass (Da): 71103
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G9IB30 | MFSMVTEFMNYGQQTVRAARYIGQGFMITLSHANRLPVTIQYPYEKLITSERFRGRIHFEFDKCIACEVCVRVCPIDLPVVDWKLEMDIRKKRLLNYSIDFGICIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALGRLPMSVIDDYTTRTILNLPEIKNA | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. 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 in a proton gradient.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Subcellular Location: Cell membrane
Sequence Length: 167
Sequence Mass (Da): 19553
Location Topology: Peripheral membrane protein
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T0BK05 | MKLFGLLGYPVGHSASPAMMNAAFAADGETAVYVPFAVSPERIEEALAGLSALGAVGVNVTVPHKVVAFHWVKTHTEEARRIGAVNTIRFTEDGAIGHNTDVSGWWRSIGHHVPSASPSFAVIGAGGAAMAILAAIATHRPKADVTVIARRESQVAALARRFDTELSIQYAPWEKRNAVLAAANVIVQTTPIGMWPKVDQSPVTDAGVFQPGQIVQDIVYRPRETMFARLAKSRGAVVVDGADMLIYQGVDAYEWWLGHEAPVDVMFAAVDRHLAHEQLAHE | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Function: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 282
Sequence Mass (Da): 30330
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A0A1S2M424 | MLVFITGGVRSGKSAFAERLASSFLTSDRNKLIYVATSKIYDSEMKMRIEKHQEDRGRSGLEWETWEQSTQLEHILPNFREHHVVLVDCLTTLVANELFFEIDMWNDPEYRQKIFKRISSFLTEVKKNNVTILLVSNELLNGGTSYDAATLSYMKLIGLLHQKIVEIANAVYLVEAGIPLRLKGRDENERNYASRYKL | 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 = adenosylcob(III)inamide phosphate + ADP + H(+)
Sequence Length: 198
Sequence Mass (Da): 22879
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A0A6B1CR67 | MENITAIIPAAGRGQRMGADRPKQYLPLGGRPVLWHVLARLEASSLVTGIVLVVRREDMDYCRSQLSESGSFAKVAALVPGGAERSASVYRGLQETRADMVLVHDAVRPFISEGLLERVVAATREHGAALPALPVVETIKEVADGRVVGTPHRERLWQAQTPQGFDRELLLRAYHAAGTDAVATDDAALVERLGHPVCVVPGEADNRKLTTPEDLAWAEWRVRAREEVPAMGLRIGQGYDVHRLEEGRPLILGGVTVPFDRGLAGHSDADVLTHAIIDALLGALAAGDIGQLFPDSDAQYKDISSLVLLEQVGTLIAERGARIQHIDAVVAAQRPKLAPHIAAMRQTLAATLGLDVGQVSLKATTTERLGFVGREEGMEAQAVVLLAL | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6.
Function: Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF).
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate
Sequence Length: 388
Sequence Mass (Da): 41637
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A0A3P6C5T3 | MDLSPSEVGYLALCSAMERLLFSILKWERQFLDVILDSVMEFVDDDLSGGNITRRKTRAVTRMLLMPSKLETSLLKGKRGTRPTCHSLESLVVSHQDRLLSNIKLLHSTYTFIPKARAPPVSVHCSDRNFAYRTTEEMHQPWFKRLLIGFARTSEANGPRKPNNLPHPLIQEIDSELPAVQPALQLTHRVFGSCPPMQSFDPAKLLTDSGKLQTLDILLKRLRAGNHRVLLFAQMTKMLNILEDYMNYRKYKYLRLDGSSTIMDRRDMVRDFQQRSDIFVFLLSTRAGGLGINLTAADTVIFYESDWNPTLDLQAMDRAHRLGQTKDVTVYRLICKETVEEKILHRASQKNTVQQLVMTGGHVQGDDVFGTADVVSLLMDDADAAQLEQKFRELPLQVRDRQKKKQPVKCIRIDAEGDAALEELEDAAERRDKEQEPSQEPEKTKPSNKKRKAAASTPKPRVPPKANEEGDAPLQPQRTKRVKRQTKSVNESLEPVFSASVTAANGEVNPSSSNPDAN | Function: ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.-
Subcellular Location: Nucleus
Sequence Length: 518
Domain: The DBINO region is involved in binding to DNA.
Sequence Mass (Da): 58572
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A0A6I4Z166 | MLELLESRCRHGQTLLLGMQNAALWRIRRGDGCRCCFEAHRGSFRSMLDDSNGSVTAMQKAYPEQAARVNEQRPEFALAAPFCEADRSMNDLAPGLYVVATPIGNLGDLSERAATVLQAASLIAAEDTRVLRTLTERVGSPATALSLTEHNVEARIPRLLEAAREGVVALTSDAGTPVVADPGGRAVEAAHEAGIPVFAVPGPSALAAAVSVAGFDGSDTHFLGFLPRAQGERRRRLTGAASTANTLVFFESPRRLAASLGDVAGALGDPPAVVCRELTKVHEEAVRGRASELVERFRETRGECTVVVDVRGWAAGSDERDLRAYLEEMREAGAQRSSAASAAARRFGVSRAEAYEVWPDDKE | Function: Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(1402) in 16S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.198
Subcellular Location: Cytoplasm
Sequence Length: 363
Sequence Mass (Da): 38824
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A0A6G2JND7 | MTSRPMASGAADSRLIPVLVGPTGVGKTAVAIELARRFDAEIISADSRQIYRYMDIGTAKPSAEEQAAAPHHLIDVIDPDVRFSAGEYGRLARESIRELAAREVQALVVGGAGLYIRALDGGLFDAPEIPRALRKRLAEGYLARSTDALHDRLGEIDPVSARRIHPNDRQRIERALEVHDATGATLSSWFERPVQSRSRGMRLVGLRRDRAALYARIDCRVEKMIESGLEAEVHGLSDRGYGPGTHAMSTFGYAEMLRYAEGELDLEDAVSAIQQRSRQYAKRQLTWFRQTRGIEWITVDEGEDPAKTCEKIIRSFPDLLF | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 321
Sequence Mass (Da): 35715
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A0A6G1MBE5 | MAEKRSHSQASKARKRRKIGSAPAQAVLKPWKTVTPDSLKWRKVDMPDRLDDVEGFFGLEEIDDVKIINNNGLLQFKAAGAADSEAETEGKGSDVGDDEWNGFSDVDTSDKGATTEMNDESKTNQAQESPKGKAQAKELQKKKKEKGNRKGKEKEKREKQKKKQKENEEKSKPKPDDTVVINSFAGLEGLSDDDLEVDLPAWESLSLSPYTLQALQKLTFTEPTPIQKLSIPSIMAGHDLIGKAATGSGKTLAFGIPIFEHWLSSSKDRAVPAKLLSEEDKEADASKLTNPLSALILSPTRELAHQITEHIQALITASGVTSPPHVVSLTGGLSIQKQLRKLGQSGGADVVVATPGRLWEILSEKSGYTRWFRKTRFLVVDEADRVLQEGHFKEVEQILDVLTRDAEKEDVAQNPEVYGTIKTIKNSKPKDRQILVFSATFSKDLQQKLSSKKSWKNANSGLLNDKDSLDYLLKKLPFREEHPQWVDVNPVDQMAENLREGIVECGNMEKDLYLYYLLLRYPLRTLVFTNSISTVRRLTNLFQNLELSVNGLNSNMIQKARLRSLERFSAPTKPVGKDGKPQHQILISTDVAARGLDIKGVELVIHYHVPRAADTYVHRSGRTARSKNSGASIILCAPDEASGIKRLISKVHEDRGSKNHAGIKSIFVDRSLVTTLRTRIELAQKIAGSTLAKESQRKEDDWLKAAAEDLGVDYESDEFAELSEKGRRGAKKRQEARSVGKDEMAALRARLREELSKKVGKGSRLYLTSGVDNLAQRLVDGKEHDVFFGEEGGWGLNNL | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 799
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): 88842
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A0A1B8P695 | MSWAILSAGLLVFLGSGAVLGAALGLTGFILLHFQAGGASALAINSAWNLLTEFTLSAVPLFIFLGDILLASGVSTRVYNGLTPLFRRVPGQLLHTNIAVCTLFGAVSGSSTSTAAAIGSVGYPELSQRGYSPRMIVGTLAAGGTLGLLIPPSLALLIYGATQNVSIGKLFLAGMLPGLMIAMAFFGWIMVRSSLGSSVAPPREEKMDWGAVGRGLLEVWPLPILIFFVLGTIYMGIATPTEAAALGVTASIVLGLTWGDLDMPKLWGAFKHASMMFGAIAMILIGTVILSQAVSLLGLPRAAVDAIAGLGLDRYGILLMIVLVYLLLGCFFDGISLLLMTLPITFPMVTSLGFDPVWFGVIVTLLMEIGMITPPVGLNLFVLCSITRNEVTLPDAAWASLPYWLILLGAVGTFTAFPELILWLPNLM | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 428
Sequence Mass (Da): 44979
Location Topology: Multi-pass membrane protein
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A0A0M8JQE1 | MRNGIQIATIWKVPVRLDLSWFIIFGLVTWSLAGGVLAEGLPGAAPALRWALGAAAGLLFAASVLLHELGHVFFALRNQVPVRGVTLFLFGGVAEITRDPQTPGAELRIAAAGPAVSLALAGIFGAAAFFTQGWLAEASVPAAWLARINLMLALFNLIPGFPLDGGRILRALVWMRTGSFARATRAASTGGQGVGYAFMGVGLFSLLTGGAFNGLWLIFIGWFLRNAAASSQAQTSLQEALRGLTVAEVMDRRVDSAAAHHTLEQVVREHVLSGSQRVLLVTDSLGNGIRGWVTLEDIVRVPRGAWPVVTVGQLMSPRENLLVLSPQAELLSALQKMDESSLSQAPVIAENQILGWLSRERIQNYLRLRTELGI | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 374
Sequence Mass (Da): 40042
Location Topology: Multi-pass membrane protein
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A0A947VUR4 | MPKIIGIDYGEKRVGLALSSEDMKYSFDYKTIIYENKHQLFHDLKIICQDEGVGRLVIGLPLDQDGQLGKKAQEVKEFSQGVSEFLKLPFEFEDERFSTALVKQLNREAGKSEKRGKKEIDQQSAKIILQTYLDRKHG | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 138
Sequence Mass (Da): 15851
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A0A845S3I4 | MILLSLGSNLTSKFGDSKKTLLKCYEFFNNEHIIILKKSSFYESVAIPNKSDPKFINSVISIETKFSPEELIKYILKVEESFDRKREQVNAPRTCDIDILDFNGEVINIFNKNISLEIPHPRLEQRSFVLYPIREIDKNWKSPLSGKNIDQLIENLDSETKKNITII | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4.
Function: Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
EC: 2.7.6.3
Sequence Length: 167
Sequence Mass (Da): 19381
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I7JWI5 | MAISSGCCGSSLAAAMAMTSATNLSSRASTTLIDSSADVVCAFGARNARFGFASKGLRSNSARRSGVCSVRRANGGRFRTGGRDCVGVRAEGAGSGNGMEPERVTRNEQLAYDGPGKGGQWLSATTRHVRIYIGVADPVSLALDQSQLDKVTLMLDPDNEFVWPDDKVQKVYDYFTELVENYAGADCTEYTLRLIGSDIEHFIRKMLLANEIKYNLECGVLNFSMGQPRYDPATLEGVEVDAE | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Subcellular Location: Plastid
Sequence Length: 243
Sequence Mass (Da): 26191
Location Topology: Peripheral membrane protein
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A0A6L7W005 | MSGFFISFEGIDKSGTSTLARLLVDHLRSSDREVVFTYEPGSTQLGGEIRHLVLDWKPQGEIDATAEMFLFAADRAQHVNEVIRPSLDAGKVVISDRYVDSTLAYQGYGRGLDLNDLRMIQNVATGGLMPAITIWLDVDLQTARKRGWGIGADRIEKEDEAFFQRVRQGFAAGYKSEPDRIFKVDGSQPISDVFDDVKKVVVDRMSGTK | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
EC: 2.7.4.9
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Length: 209
Sequence Mass (Da): 23278
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A0A947QPA2 | MKPVSDFQSILKPRPKKIHKRQLGHILVVAGSYHMSGAASLTALAALRSGVGLITMSYPERLERIFRKTILEAMHLPLPENRQGSISSSAYKNIKKEFKKYDLMIIGPGLSRSKSTEVFCKSVISRVDLPMVIDADALNALADLKLTDKILKNRTAATVLTPHHGEMERLINKKIPDDLNERQRIVKKYSGEWNAHIVLKGYRTIIGSPQGVVKIDQHGGPVLATAGSGDVLSGILGTLVVQNIKETFKACCVAVHLHSLTGSLAAKDLGEKSVIASDLINYIPSGFDILSKIR | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. 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: 4.2.1.136
Catalytic Activity: (6S)-NADHX + ADP = AMP + H(+) + NADH + phosphate
Sequence Length: 294
Sequence Mass (Da): 32149
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A0A1N6M8C5 | MQAQHFSADDERFMRRAIQLAHQAELEGEVPVGAVLVKDDQIIAEGWNRSITTHDATAHAEIQVLRKAGQVVENYRLVDSTLYVTLEPCPMCAGALLHSRVKRIVFGAPDLKAGAAGTVMNLFESEAAYHYAQIEPGLLEAECREQLQCFFRRRRQEIKAIKRQQQESDQFDQPSARAVQSANGVDTD | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 188
Sequence Mass (Da): 21051
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A0A947JDW7 | MISYVSGIIKVITKRSVVLETNGVGYEIYVLPLVLEKAKSGEELSLFTHMHVREDAMELYGFADMEQRIFFQDLISVSGVGPKSAVTIMSLAPLPDLKKAIVQEDASLLTKVSGIGKKTAERLILELRNKLTVSEEDKIDSSSAGTSDSQSIDGLISLGYSAGEAREALRQVDKDITEVKDRIKAALKMLGKK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Subcellular Location: Cytoplasm
Sequence Length: 193
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Sequence Mass (Da): 21076
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A0A250XW51 | MEAKAACTEAAGRSCVVSAEETEKWMEEAMRMAKEALENTEVPVGCLMVYKSEVVGKGRNEVNQTKNATRHAEMVAIDQVLDWCRRSGQSPSAVLEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFGGCGSVLNIASADLPNTGRPFQCIPGYRAEEAVELLKTFYKQENPNAPKSKVRKKECQKS | Function: Probably participates in deamination of adenosine-34 to inosine in many tRNAs.
EC: 3.5.4.33
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Length: 191
Sequence Mass (Da): 21078
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A0A6J2Y4D7 | MDKGNVQSYMDFVLPLVLASGKELLTVEDINVEIKDGNVWDIVTEYDRKIEKLLIQKLKKKYPDHKFIGEEESAEKNCISTLTASPTWIIDPIDGTANFVKRMPLTCISVGLTIDKEQVLGVVYNAYANELFTAVKDQGAYLNGKRLKTSGLTEIDKSIFNYEISLAIKNTKLRKLYMSRLNHLIDKVSGIRSYGCAALGLCYVACGRVDAYQCDGLYPWDAAAGTLIVREAGGYVTDSSGKEFDLMQPNFLAASSKELSDQFMAIERQADEEATNKIKNHFLPEQPKLPTEKIK | Pathway: Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.
EC: 3.1.3.25
Catalytic Activity: a myo-inositol phosphate + H2O = myo-inositol + phosphate
Sequence Length: 295
Sequence Mass (Da): 32984
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A0A098GAH3 | MSLQIVILAAGQGKRMYSKTPKVLHCLAGKPMLQWVIETAQQLNPDAIHVVYGHGGEEIKSALNHSPVNWILQAEQLGTGHAVKQALTHIPTQSQVLILSGDVPLIRAETLRGLIKGSLPNEKKPAPLSLLVAILDNPTGLGRIIRNESGEIQAIIEEKDATAEQKQIKEIYSGICCAPAADLARWLPKLNAHNAQGEYYLTDIIAMAVAENLPITSIQAKDIMEIQGVNNRLQLQQLERVWQKQVAEQLMLSGVSISDANRLDIRGELQCGQDVFIDVNVILSGKVSLGKGCRIGPNCVLTNVVLGENCEIFANSVLEDCVLDNNCHIGPFARIRPGTKLAAGCKIGNFVETKNAVFAEGTKASHLSYLGDVTIGKEVNIGAGTITCNYDGANKHQTIIEDGVFIGSDTQLVAPVRIGANATIGAGSTIRKDVPEGELTLTVSKQKTILGWKRPVKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
Function: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Catalytic Activity: H(+) + N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Subcellular Location: Cytoplasm
Sequence Length: 458
Sequence Mass (Da): 49335
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A0A965EYJ5 | MTVPWAEMVREADALGIPVTEEHLGQFDAFASLLAEGRQLLNLTSIVDPEEVAFKLFLDSLTALLGLVEALPEAARLIDIGTGAGFPGVPLAIVLPDAGVTLLDATGKKMTWLSGAVDTIGLRNAYPVAGRAETAAHDPGWRGQFDVAVVRAVAPIAVLAEICLPFLCPGGQLIALKSATRTETELPEARYALQMLGGRVASVMPVRSDRLPNRVVVTIVQDGRAPRGYPRRPGVPATDPLIG | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.170
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 25674
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A0A2V5RA48 | MSIVTKTGDKGETSLMYGRRLSKADPGVEAYGCIDELAAALGLARASSTDKFLSEEIFAAQRDLIVVMGELATAPRDRERYVKDGFHLTTAEMVDRITALIFDLEKDKTLYPKDWVIPGATAVSAALDFARATCRRAERHIAVLSIREKDFNPEILRYVNRLSDLCWVWARYAERKLQSSN | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
EC: 2.5.1.17
Catalytic Activity: 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate
Sequence Length: 181
Sequence Mass (Da): 20335
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A0A455VG71 | ALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMLGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPA | 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: 178
Sequence Mass (Da): 19084
Location Topology: Multi-pass membrane protein
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C6F772 | CLTLRLADEYSSNAQARRQLPSPELVPRLTDNSYHHFVLATDNVLAASVVVASAVRASSKPEKIVFHVITDKKTYAAMHSWFALHPLPPSIIEVKGVHQFDWLTKDNVPVLEAMETHIEIR | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 121
Sequence Mass (Da): 13598
Location Topology: Single-pass type II membrane protein
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A0A6G2JM80 | MQDFSAVRQRDEELYGLLVAERERQRDGIELIPSENYVSPAILEAMGSVLTNKYSEGYPGKRYYGGQQYIDKIENLARRRAKELFGAEHVNVQCYSGSPANTAVMFGLLDYGDTIMGMKLDQGGHLTHGLHVNYSGKSYNVVSYGVQRETGRIDMDEVRDLALEHRPKLIISGATAYPRQFDFEAFKAISDEVGAVPMADISHISGLIVGGVHPSPLPFTDVVTTTTHKTLRGPRSAIIMCHKKYAKDIDRAVFPGLQGGPHDHITAAKALTFKEAMRPEFKDYARQIVDNAKALAETLLGHGFDLVSGGTDNHLVLVDLTNKGIIGKDAETALDKAGLTVNKNTVPFDTRSPFSPSGIRIGTPAATTRGMKEPEMKQIAGWIDTAIENHGNDEKLSSIHDEVRELCAGFPVPGISTAGAALMQEIGAG | Pathway: Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1.
Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine
EC: 2.1.2.1
Subcellular Location: Cytoplasm
Sequence Length: 429
Sequence Mass (Da): 46698
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A0A5P8HL33 | TLYFIFGAWAGMVGTSLSIMIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMMGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLXPSLTLLLASSMVENGAGTGWTVYPPLSSGIAHSGASVDLAIFSLHLAGVSSILGAVNFITTIINMRSVGITFDRMPLFVWSVGITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLF | 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): 23538
Location Topology: Multi-pass membrane protein
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Q3MND7 | RKTHPLLKIANDALVDLPAPSNISVWWNFGSLLGLCLGAQLVTGIFLAMHYTADIATAFSSVAHICRDVNFGWLIRNMHANGASFFFICLYSHIGRGLYYGSYLYKETWTIGVVLLLLVMMTAFVGYVLPWGQMSFWGG | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 139
Sequence Mass (Da): 15484
Location Topology: Multi-pass membrane protein
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A0A8J1TSW8 | MEFPSGVLTMTSEPPSTIPKGTSSLASHNPNIGHNTNKPHLQPKVSPGNPGHQHTAEMQSLVSTLENAIKKGDTLLAQKIVSLLAGYRLNLQMEVKDKQGVDDLDKEIWMKVYIEDQKTTVGPKSIKVQPSMTIKDLKNKIFLDFDFPPAIQQWIIDKKITKDHMTLAECGARIDDCTVFLYLLSAKSVGLKWEAARKQYERLSATGSIDEEDQDPGKTLQGPMISPPPIAAPRKVAGTPGAEGGLPVKPQVLAGQQHKLDNMLHEIVQGAGALVGAVGGAEGGAVGGIDPPSLEVDPNQEGWVCEVCTYFNRPLRPGCEMCSTDRPTDYKVPTNYRPTSEEKQILESMLRSDEQTKMAEITRQEKKLREQQENLTQLLSTDERDLITNTEDFECLICYNIVEEGEGVVLRECLHTFCRECLEGMIEVSEDAVITCPFQDNDYACNGVLQEREIKQLVPPGVYERHLQRSLATAEGQETHSFHCKTADCKGWCIYEDDVNFFNCPVCGNQNCLTCKAIHKGINCRQYQEDIRIRAANDIAAQQTQKMLQDMITSGEAMYCPSCKIVVLKKDGCDWIKCSMCKTEICWVTKGPRWGPGGSGDISGGCRCRVAGQQCHPNCNNCH | Pathway: Protein modification; protein ubiquitination.
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: 623
Sequence Mass (Da): 68995
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A0A0N4VZG5 | MMKKKILADPRLTVFITHGGLGSTTELAHLGKPAILMPVFADQTRNAHMLAKHGGGIVLTKFALEDPQIIRDSLKKIFNDASYSRNAKRLSEMLLNQPISAEQLLIKHCEFAAK | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 114
Sequence Mass (Da): 12623
Location Topology: Single-pass membrane protein
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A0A8J1TIL7 | FKAGHSSWINTFKDLNANTSGFKVDLWKQNINKSLTTVRFINVRDPWERLLSAYMDRMTYHENRPHKSWQRNSIGRRIMFKYYPGSNAMVVPYEKISFTFTDFLRYIIDEPKQLAGRLDDHWLQYYERCRPCDPYLDYNAIVKLETVTEDSNYVLEKIGVKTKIKDGPRKTAKYLQEQYKEVPRWIIDDLTKIFYWDFKLFDYDMNSPLVRKSIS | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 215
Sequence Mass (Da): 25903
Location Topology: Single-pass type II membrane protein
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A0A2Z6S2B4 | MTKATETARLFVQEEILPVLPWWALVSFGAYSLGNIGYHVYRFRDCEDAYHELMAEIQIAKDDLKAKGVTID | Pathway: Protein modification; protein glycosylation.
Function: Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 72
Sequence Mass (Da): 8249
Location Topology: Multi-pass membrane protein
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V4UH20 | MQLHISPSLRHVTVLPGKGVREFIKVKVGSRRLSYRMLFYSLLFLTFLLRFVFVLSAVDTIDGESKCSTIGCLGKRLGPRILGRRPQSTVPEVIYQILEEPMSKDELKGRSDIPQTLEEFMADMKESKSDAKTFAIKLRDMVTLMEQRTRTAKIQEYLYRHVASSSIPKQLHCLALRLANEHSTNAAARLQLPSAELVPALVDNSYFHYVLASDNVLATSVVATSLVKNSLHPAKIVLHIITDRKTYYPMQAWFSLHPLSPAIIEVKALQHFDWFSKGKVPVLEAMEKDQRVRAQFRGGSSAIVANNTEKPYVIAAKLQALSPKYNSLMNHIRIHLPEVSIMFML | Pathway: Glycan metabolism; pectin biosynthesis.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 345
Sequence Mass (Da): 39032
Location Topology: Single-pass type II membrane protein
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A0A0N4X5F0 | MMIETFLSMARYLSPRHDDDWCDRLHYLITPNILFAFSVLISFKQFGGRPIECMFPNKFPGSWEQYAENYCWSQDTYFVEPQQHVELLKQDQRYTPERQLSYYQWVPFFLLVQAVFFRAPSFLWKTFSNHSGIRMHEVVEKAKDSANVEEEVRQKNIGILARHLQNALRFKRRMQKKKVIVHKTVTCLNYQYSSGFVSAVYLFTKALYLVNVVVQLWLMNKYLMLFAAAAFTFISWFILLLFPCFSRWFIEQHLELSTLDGFETDSLQTAXRDGVFVLRMVSSHAGIIFGTDLILELWSTFYGIEKKVVYLATL | Function: Structural component of the gap junctions.
Subcellular Location: Cell membrane
Sequence Length: 314
Sequence Mass (Da): 37121
Location Topology: Multi-pass membrane protein
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A0A8J1XZU3 | MLNTTRAFCSIRILILCSIGVLIFQVFILHQIFFSKMNNPNGEKQRTGIDGRAGHFERVNIEPNKNNRQNKQVVVQPHGEILEERKRQVEKICDTLTKNALLNSSLDPKEYYGHIYVDPMKKILYCYTPKVASTHWREILTANFYNMPIEELTVNITGGDWKRWYKGHILTPLGKIAPNKRQYIIDTYYKFMFTRHPLDRFYSTWKNKFMETNDSYYREHFGSVILKKYRENATIKDLYEGEGVRFEEFIKFITFEGIRFRDEHWQSFFELCKPCQIHYDIIGNFETLSEDTNYVIEKTNLSKYQFPQVISKSTYNRQTLYENIYKPDLIQLYKRFRLDFDMFKYTMQLS | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 350
Sequence Mass (Da): 42027
Location Topology: Single-pass type II membrane protein
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A0A8J1XRA9 | MTSNVTKLLEFMSKIGQLKRVKRTGWVLRRVQEPESVSDHMYRMAIMSMLLTPEKYPNIDKERCIKLALVHDMAECIVGDIAPADGISKEEKHKREQNAMSELGDLIADEETQKEIHGLWEEYEHQSSEEAKVVKDLDRFEMVLQAHEYEVQENRPGELQDFFDSTKGKFQHPGVQEWVDQLYSNRDKHLQTKSSHNPKKQKLDRTSNTQATDSESS | Function: Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
EC: 3.1.3.89
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate
Sequence Length: 217
Sequence Mass (Da): 25204
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A0A8H6PME7 | MRGLLLAGALALPASVFAHPAQSQGLYRRTVDLNAFRLKSLAKYVNATETVIDAPDSFAPFAQQSYVEAATQHVKMTVADATFRLVDDHYVGDNGVAHVHFRQTANGLDIDNADFNVNVGKDGKVFSYGNSFYTGKVPSSGPLTKRDFSDPVTALKGTTNTLQLPISVDGASSESTEEKESYVFKGVSGTVSDPKAKLVYFVKGDGKLALAWRVETDIDSNWLLTYIDAKSGEEIHGVVDYVAEADYQVYAWGINDPTEGSRTIVSDPWDSAASEFTWISDGSTKYTTSRGNNGIAQSNPSGGTSYLNNYRPSSSSLSFRYPYSTSMSPPSSYVDASIIQLFYTANTYHDLLHTLGFNEKAGNFEYNTNGQGGRGNDYVILNAQDGSGTNNANFATPPDGQPGRMRMYVWDASTPYRDGSFEAGIVIHEYTHGLSNRLTGGPANSNCLNALESGGMGEGWSDFMATAIRLKPGDTRSKDYTMGEWASNRAGGIRAYPYSTSLSTNPLTYTSVNSLDKVHAIGTVWASMLYEVMWNLIDKYGKNDAPKPTIRDGVPTDGKYLSMKLVMDGMALQPCNPNFVQARDAILDADTALTGGANQCEIWKGFAKRGLGDGARYSRNNRILKPASANQIKEYEINMMRSVIPLIVSLGSLAAALNITTPAANETYAAGSTLNVKWTSVDTDPTNISLYLWNFVSWPPSYVPLAYDVPTADLSHEVQIPCDNNPEWGYQISAINGTNVYIIYSQSAKFTISESDSVCEPEPEPTPSTCPTAVSTVYVTVSPTGSSSRLFHPSSSSHVSPTPSPSTTTTPTSKYVKPGTVPKTIGWCSDYSHPVTLDKVPTPTPSPMVTPAPEGPGASGPRVKTITTTVTVEACPVEDDMW | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 882
Sequence Mass (Da): 95270
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A0A0R3X9L5 | MAKEMRWYDHSVFYRFRAQVFVFMFGCSVTILPILCLVYYTRQFIYPLFRMTFGNAIDDAQSRYCFLSILLYTIYWIWDIETPYRGGRRIMWIKELALWKWMAQYFPARLVASRELQKWASEQGQTVNEKDTVVRLPTSVNYLLGYHPHGPLAAGMLMTCGFDALNFSKFFPDIKPHMATLNVHYKVPFFREFALLAGGVSVNQESLTYLLDRELTGKTGNLVAVSVGGAIEALESRPGQYVLMFSRRRGFFRMALRTGAYLVPSIGFGETSMYNQVANSTGSALRKLQDWFTRTFTLAPPLFYSTCIIPYRKPLTVVVGRPIVCKRTPHPTEGEIDNLREEYKEELRAMFNKYRPIYDPTAEDIRFF | EC: 2.3.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 368
Sequence Mass (Da): 42767
Location Topology: Multi-pass membrane protein
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A0A0R3TPY8 | MDSDYINIPCDVLPLDCKSFDLLSSIEKRYLCFLDEVAWIGGLIDLIQLSPEAAGIFLLGQRIFEKQTVSELSDSAKSAHVSDTDISAFISYFSCILGNLGNYLNFGDTKFVPDLSKDAFTKIVKSSASYSSSEEVRDIFDKVIDAIYSLHPRRLRLAFAPDGLTTYYSGNCTREDADIVQEYLKAMKIEGYNTRIMKSLNPNSDGKHEYHIAFASAEKKEEIITHPSLPTNAIFKACYGDYQEIMTLLVEAIDRVKASVLNDTQLRMWEQYQVSFRTGSIEAHKLGSEFWVSDKQPTIETYCGFIESYRDPYGVRGEFETFVAIVDKDVSAKFSKLVSGAMDFLKLLPWPSTYEKDKFLKPDFSSMDIIAFGVSGPPLGINIPNYDDIRQSIGFKNFSLANILKANFQDPTVQFVRSEDRDIYVSTVGHSFDIQVGLHELLGHGSGKLFMRDENGCFNFPKSVRDLLTGGDITHWYEPGETWDSKFSSVASAFEECRAECVGVYLCDTPAILQLFDSDSKFNSDDVVFVNWLSMVRSGLRSLQYFTPATDGGFGGAWGQAHCQARFAIFKVILDCDSSALRIEMIEGEDGKPDLRIHLNRAAIQSTIKPAIGEFLKKLQISRLTVTISAPILFVLLFQYYKSTGNSDEGVPFFVGASTPTREQLEWRKIVIQRKKPRPNYVQPVTFHDTASGSVTLKNYPGTDEGMIQSFVDRYSDRRCFGRRALSALKAVWERDQQYFTTVPL | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.14.4
Catalytic Activity: Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Sequence Length: 745
Sequence Mass (Da): 83890
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A0A0R3X6Q2 | MSSASSRSVRSRLGDDASQQPLVEPMSTDLFTNDTPNLDVEGSETHGTAPSSSQRRRSAHEQSDTDARSGLRTSEVDPGSPLSYSDMSSFGSGRAADALSSFRPGVNEGGTPRSHFAASGPIGPAIDTEIGSSAELGAQASCFAHSSWMEDMAVSGATTLDIDCQHLRDANPELYNQLITFPKEVIPACDASLHTLFLDRFRDARPERPLQTRPFNSGKSRSLRELNPEDLDQLVSITGLAIRLSNLIPEMMRAEFKCAVCGALSSVVCERGRVAEPSACARCHALHTTQLQHNRCLFVDKQLIKLQFPMSSEFVSSQLQEAPEDMPASQTPHTVALYAHEDLVDKVKPGDRVCVTGIYRAVPLKLSNRMRTLKAIYKTYIDVLHFKKELSGRLLIDDGEGENEVGGLEESVGSNVMRHLSEERIAQIIALSKKPDLYERLSAAIAPSIYENEDVKKGILLQLFGGTRKDFASKGRGNFRSEINILLCGDPGTSKSQLLQYVYSISPRGQYTSGKGSSAVGLTAYVTKDPETGQLSLQTGALALADNGTCCIDEFDKMTDSTRSVLHEVMEQQTLSIAKAGILCQLNARTAILAAANPVGSKWDPSKTIIDNIQ | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.6.4.12
Subcellular Location: Nucleus
Sequence Length: 614
Sequence Mass (Da): 66631
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A0A0N4WCL6 | MTSSKYPLLLAVQIGMLATDLAFNAASVLLFGNSIVLLMMYILQDTLILLSVIVLIITFSSTFVFQAGLIFLLFRRFASTLIAAFVYLAASISLHYVTLVSPFFELF | Function: Required for ciliogenesis.
Subcellular Location: Membrane
Sequence Length: 107
Sequence Mass (Da): 11837
Location Topology: Multi-pass membrane protein
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E4XGP9 | MSSVSRPEKKEATVLAATSSIATRTIMAPVERVKLILQLQNELIKQGRLIEPYRGFRNCFRRIVSVEGAQSLWRGNMAQVVRCVHTQEINLMFKDRILSLFTINSDTSASRLMLFNIAAGGMAGVLTDCFLYSFDFARTALAADVKDPFTQKRVYENGFKDVLSTVYKSDGIRGLYRGFLVSSVGLFIYRGLYYGLYDSIKPLVLDETSSFGRRFTLAYCVTIFAMQMSYPFDTLRRRMMLTSGTGRHYPSSFHCLKEIIKYEGKSALLVGSTANVLRGTGGALILAGFDHLKTVYLKWKFMIDPGKSQTLSMIHIICWLQSCFL | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Catalytic Activity: H(+)(in) = H(+)(out)
Subcellular Location: Membrane
Sequence Length: 325
Sequence Mass (Da): 36670
Location Topology: Multi-pass membrane protein
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A0A0N4WDK8 | MKYLQLVVLPVLIVLSNCQSECDSKAKRSTFLWSVRSPDRTSRGFLFGTIHVPYTEVWDKVSDRVREAFSYSDTVLLEIDLRNDDTVKRLIKCKNLKRKQTAASYLHPKLHQRIKDFMENFRRTLLRCVQKQDQHRPDSYKMAEDLYENIAGNWDRKRPEWLLFALYQLCENFLDRPTTPMLDVFLANKAYEEDKQIHAIETAHEQCNPVASLTQEEIIFAINYTVHYLEYLHHTKKLFQTDNQRSLSTLVKDYRCGNLDDRYFERNEYAVNGFHMSEVEKLRAEKIQRHLREDIIAKRNERMAHRLHRLLSANPHITIFSAIGTGHFFGNGSILHHLHNMGYIIQSVKEDDIM | Cofactor: Divalent metal cations. Mn(2+) or Co(2+).
Function: Metalloprotease that acts as a negative regulator of the Wnt signaling pathway.
EC: 3.4.-.-
Subcellular Location: Cell membrane
Sequence Length: 354
Sequence Mass (Da): 41862
Location Topology: Single-pass type I membrane protein
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B7FZT2 | LGRQGSVTRKTKETSISATLRMDGSELGVHVNCGIKTLDTFLTLLATTACMSLDLTCHGDLWIDEHHTAEDVAIALGQVLTDALGTKAGLNRMWCASAEQNQTKIEVTMDLSNRPCFTHNLGLDNGEEMVGDLSLEMFEHILDSIVVNARMTVHILEVYATNNLEDTVQAVAIAFGQALKYCAMVDSRRAGATASSKGTLSV | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
EC: 4.2.1.19
Catalytic Activity: D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
Sequence Length: 202
Sequence Mass (Da): 21773
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A0A2D0WT78 | FFGHPEVYILILPGFGLISHNISQESGKKEAFGVLGMIYAMTAIGLLGFVVWAHHMFTVGMDVHTRAYFTSATMIIAVPTGIKIFSWLATFHSAQISFNPSSLWSLGFIFFFIMGGLTGVILANSSIDIILHDTYYVVAHFHYVLS | 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: 146
Sequence Mass (Da): 16153
Location Topology: Multi-pass membrane protein
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A0A8D1D673 | MAVARKIKTLLTVNILVFVGIILFSVYCRLQDRSEGLVQIVRSADRRVRSRHAKVGALAEREAILQRLDHLEEVVYNQLNGLAKPIGLVEGPGGLGQGGMAATLRDDSQETESKYEEYGYNAQLSDRISLDRTIPDYRPKKCRQMTYSDDLPQISVVFIFVNEALSVILRSVHSVVNHTPSQLLKEVILVDDNSDNVELKLNLDQYVSKRYPGLVKIVRNGRREGLIRARLQGWKAATAPVVGFFDAHVEFSTGWAEPALSRIREDHRRIVLPAIDNIKYDTFEVQQYASAAHGYNWGLWCMYIIPPQDWLDRGDEAAPIRTPAMIGCSFVVDREYFGDIGLLDPGMEVYGGENIELGMRLVRYSAEGLLQLGPLGSTAFLPDSKCLVDDGRGRTPALKKCEDVARPAQRLWDFTQGGPIVSRDTGRCLEVEMSKDANFGLRLVVQRCSGQKWTIRNWIKPGRH | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 464
Sequence Mass (Da): 52157
Location Topology: Single-pass type II membrane protein
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A0A352VQB0 | MRGREGRTDRPSAGLLGFVVVGAEIVRLMMAISNPTRADVILPESAPVKRILLVDCDAFFVQVARLEDPEGAGKAPLLIVGGSPTGRGVVTSASYEARAYGVRSAMPTAHALRLCPDATVVGVPRSAVSARSQSVKEALMDLSPVVQAASVDEFYLDLTGTERLFQNESFAETAWRIRETVLERTKVSVSLGGGTRRVIAKLATNFAKPAGVHIVPAGEEEAFLRGLDLADLPGIGPSLAAALEKRGLVRVEDAYAVQIEWLQRWFGERRGAWLYRRIRGVDSSEVDPRERRKSISSERTFFADIDDDEELERRLMRQAGSVARTMRQQSFRAKTVTVKLRDHDFKTRQHSRTVPEPIESDHAIYGVAKTLLAELRRKRRVPARLLGVGLTGLVASSATSQLGLFAEPVAGETERERTVSRTVDELRNRFGREAVMPGRLVEDDHAPRVPKGDAK | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Subcellular Location: Cytoplasm
Sequence Length: 455
Sequence Mass (Da): 49995
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A0A6G1M307 | MAEEIKAAEPPVAASTEVEPTKTEKVESPTPDQPIETAAAPAPAPKAEETAATDSTAIASKAEETPVEEAAPALPELTNAKWGSISPNLAAFYRRLPEILEKSKHSEVYSVQLTYVEGSTEPTFGTLLILQKFLRANSDNIEKAVEQLSASLAWRAEKKPLDSLATEHDRSAYEGLGYVQVLPETDEVLTWNIYGAVTDYKKTFANLDSFLSWRVALMEAAIAKLDLPNATKPIPDFGKGADPYQIIQVHDYLNVSFLRMDPDAKAASKATIAVFRDFYPEMLSRKFFVNVPLLMGWLYKATTLVLPEATVKKFRVLSYGKELAAELGDAVPEVYGGKGVKDVKELGDPVKLSAVPVVEPETEAPAPTATTQETTSPATTTTPAAPAPATDA | Function: Non-classical phosphatidylinositol (PtdIns) transfer protein (PITP), which exhibits PtdIns-binding/transfer activity in the absence of detectable PtdCho-binding/transfer activity. Regulates PtdIns(4,5)P2 homeostasis at the plasma membrane. Heme-binding protein that may play a role in organic oxidant-induced stress responses.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out)
Subcellular Location: Cytoplasm
Sequence Length: 392
Sequence Mass (Da): 42354
Location Topology: Peripheral membrane protein
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A0A8B8Q8A5 | MADGGEVKLLGFWGSPYALRVIWALKLKQVPYDYLEEDLLSKKSSLLLQYNPVHKKVPILVHRGKPIAESLVILEYIDEMWKQSPLLLQDPSERARARFWSKFTDEKCAPAIKAVSCSQGEEQQKAVLEAQESLKTLESGLEGKLFFGGETINFADVATGWIGCWARIVEEITGTSLIDAENMPSLDAWSKRFLELPIIKQCVPPWDKLIELNSGFVKMYLASSK | Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
EC: 2.5.1.18
Subcellular Location: Cytoplasm
Sequence Length: 225
Sequence Mass (Da): 25376
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A0A158REE0 | MAPTLAYWNIRGLAEQSRLLLKYLGVEYNDKQYKVGPPPNLDRVEWLSEKFSLGLDFPNLPYYIDGDYKLTQSGAILEYIADRHGMVPDCKKRRAVLHMLQCEIMDLRMAFVKPCYSPDFEKLKPSIFEAMDQKLPNFEKFLGDKEWLTGDKINYPDFALCELLNQMKKFEPTCLKKYPKLQAYLERFELAEQSRLLLKYLGVEYNDKQYKVGPAPGFDRSEWLSDKFSLGLDFPNLPYYIDGDYKLTQSGAILEYIADRHGMVPDCKKRRAVLHMLQCEIVDLRMAFVKPCYSPDFINYPDFALCELLNQMKKFEPTCLKKYPKLQAYLERFEDLPALREYMASKEFKTRPSVALAVCLRVCGVMAPTLGYWDIRGLAEQSRLLLKYLGVEYNDKRYKVGPAPTYDRSEWLSEKFSLGLDFPNLPYYIDGDFKLTQSGAILEYIADRHGMIPDCKKRRAVLHMIQCEVMDLRIHFAHTCYSPDFAKLSPKFLETLSEKLPNFEKFLGDKEWLTGDKINYPDFNLCELLNQLTKFDSTCLKNFPKLRAYLTRFENLPALKDYMASKEFNTISCHGPSAHWRGDMKTLTDDFECPSFQNLPTLKGYIASKEFKTLPCMSAGAHWLYDG | Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
EC: 2.5.1.18
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Sequence Length: 627
Sequence Mass (Da): 72909
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A0A0R3WN21 | MSLLWTITATFLYTEAAVITLLLMPFISSKMQVREQNRSVYLMKLFRAQRNLYISGFCLFLWFGSDLLLVFHKHLINFLMDFCLCKSLWHKGP | Function: May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 93
Sequence Mass (Da): 11012
Location Topology: Multi-pass membrane protein
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A0A8J1T566 | MLPRKSTITKWLMFVLILGGMLYTVINNNASPVNKEIEIRKLLEYAKDPIINKPPKGEKDLENHSGKVYSSINSSAGHENQPNPLTLTPPVNPHNFKYMIKPKYQCDDSVFLVVYVHSHPDYYKRRILIRQTWGNPKNYKEKIRVIFIMGKGLKQKVQDSLMFESETYGDIVQEDFIDSYKNLTYKGIAGLKWVSENCAHTKYTLKTDDDIFVNMFNLLRHLKSISMHDLGRTKLVLCLTWHAMKVLRDKNSKWYIAKEEFEPDHFPPYCSGSAFIFSTDVVKDMFEISLTIKFFWVDDYYITGALVNKLGLNHTQFISVYSLQKPKFEENFSGPKGDLYIFAHTHEADKIRKVWKRIISKEGKSMKSDYLLSS | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 374
Sequence Mass (Da): 43539
Location Topology: Single-pass type II membrane protein
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A0A8J1Y4Z6 | MKMDKEIALKYNASLRTSYNATFLNQFDSNGAPINYTRTETLIIGIILCCLILLTILGNLLVIVSVVTFRKLRTLTNYFVISLAIADTLVAVLVMPFGVYQQVTNLQWGLGAVACKLSTCFDIYFSTSSIFHLSCLALDRYFAICKPFFYTEHISKTPILIIIGLCWIIPSFISFLPILNGWNLFGIESIYEELNSDEGICVFIVNIPFSLVCSSIAFYVPVVFMIVVNSKIYSAARRQARQIQSLQIMDSPNKSNLDRRHKHMKAETKAAKTLSIIMGVFSLCWFPFFIFNVLDVFIGYQIPYVPWTIVLWLGWVNSTINPFLYYWFNQNFRNAYRMIISCGHCKGYRQRDTLSISATGVSNLSE | Function: This is one of the several different receptors for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone, and a mitogen. The activity of this receptor is mediated by G proteins that stimulate adenylate cyclase.
Subcellular Location: Cell membrane
Sequence Length: 366
Sequence Mass (Da): 41718
Location Topology: Multi-pass membrane protein
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A0A8J1Y5B7 | MCQLFLGVFFALIAILMYYVILQYEDHKEVPHYHIIVGVMSARNHYKQRQAIRDTWLAHSQTQANISNKVVVKFVLGKKACHIPPEDRLDPYSCERWDVQVSDWENDITVAKVDNTSPSIKQVTAIEQLTFKVHHPIVITKIGLLAGDTMHLNYKVKLVDSLNGETIASAVFSDSQPGLPQEGFRYRAVENYLLPKHFEGTIIGEILDSEITNSTNTTTGFNIDNFNIKLYNGSGIISLYASDIFQTNQTSPVVSFMFKVYEPGALKLHIAGKKLRAFEWGESMELENIKVTEEFIEKNDMVLVNVIDTYRNLPLKLLKFYTWMTQRYMFNYTLKTDDDCYLNLENIVERSRLILDEGGSKQWWGQFRRNWYVERHGKWSERLYTSSSYPTFGCGAGNVLSSDLVYWLADNEENLQVYQGEDVSLGIWLAALGPQFIADAHWQCDNRTCEPDMYNMPELSPQQLTNMWQNKMKCGNPCGC | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 480
Sequence Mass (Da): 55228
Location Topology: Single-pass type II membrane protein
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A0A6B9SL44 | LMLNSPDMAFPRMNNMSFWLLPPSLTLLLSSSMVEGGVGTGWTVYPPLSSYLFHSGPSVDLAIFSLHLAGASSILGAVNFISTVLNMRSNEMKLDRMPLFVWAVFITAILLLLSLPVLAGGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF | 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: 154
Sequence Mass (Da): 16888
Location Topology: Multi-pass membrane protein
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A0A8J1UAE6 | MKLPIFYGIIFTNGVLTLILWLYLKKHFRAEKSEATTEAFTCRSIHQYRDMKQSTNSTRNEKRTSTPKQFFAAKLVNAHFDDYTFVQNPVIKDTGKQTESENVILVLVMSDSNVVSKSFRTVLRDAIGNVSIVKKWRLKILFLIGTNPTESSNMMRVKEESRQFGDIILGDFPDDYLSFTIKTAMAYRWVLQYYAKVKYILRITQDVIINPYNLVNLVESIKTKNPEKDSIIMGLVITGAKPTFNHPRWAYKSTIPWPPGVPYPPYPAGPAVLSSIAATMAINTAICDTPVIFPDDCYLGIIAEKTEINPIGLEHFLWSQGELFLTINEKIRRRKVAIHCRGSPDIMAKAWKYIQKINRTNKN | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 363
Sequence Mass (Da): 41543
Location Topology: Single-pass type II membrane protein
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A0A8J1TU13 | MASSAKRPRRHVRPSSNMAKFREHFAKAKHIVLLTGAGVSAESGVPTFRGAGGLWRKYQATDLATPEAFAANPSLLWEFYHYRRNSMLDKRPNDAHKAIAECEARLEKQERRVVIITQNIDELHAKAGSKNIIELHGNLFKVRCTKCGRIDYTRSRVLCPALEGKGEPDPKAKDARIPVEDLPKCSDPDCRGLIRPHVVWFGEDLDEDIFKRAEEELEQCDLCLLVGTSSVVYPAAMFAPNVAARGVPVAEFNMEDTKVSGHFGFHFSGPAGVTIPIALAEHKNEIIAQVESEPLSNAQLPDSEESVSNHSNDTSVSGSTIDSTGFDFPRGKEESESTRTKMESDSTQVKTESGSPHVKLESDTSHVKTESDDRIKESEITQVKMESDSHIKTESPYDKTQSDISDGKTNSNSPNLAESDSTNDQSEKNTPNEPYKIGTGENDLTATEIVDHPSGQTYEPENEVSNPKGIDTHGEIVNDSTEPPVSDTNQQ | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo.
EC: 2.3.1.-
Catalytic Activity: H2O + N(6)-glutaryl-L-lysyl-[protein] + NAD(+) = 2''-O-glutaryl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Subcellular Location: Mitochondrion
Sequence Length: 491
Domain: In contrast to class I sirtuins, class III sirtuins have only weak deacetylase activity. Difference in substrate specificity is probably due to a larger hydrophobic pocket with 2 residues (Tyr-80 and Arg-83) that bind to malonylated and succinylated substrates and define the specificity.
Sequence Mass (Da): 54044
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A0A8J1YAS6 | MGSTWTIKLFLGLLTAWALLRESECDGLPAERQSPIDIETSETKCLKLSLIYIPKKTCEDVHLVNEGGHTAQLELDKCDYTILVGLLGAYSVLQAHFHWGEDSTRGSEHTIDGQRYPMEMHIVAKKKFGTSTCAEIAVLGFFFEISGTDNAAWNDIITGLSLIKMPDEKTTINNFNLQDLLPSHKSEFYRYFGSLTTPPYTQFVKWTVFKETIKISESQIAQFRTLLSEHGDNIVDNFREVQPLNGRTVNKNCYMPYEQ | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 259
Sequence Mass (Da): 29400
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A0A0R3WJB4 | MSRISDVRTIVETANQFSGCELLNKTFHTDSYVTIDCCCCSFVIKCFWPPELTPNYKERIFSILEKNMKEFYMKSSWGWNGRNKFHELFSAESRLLLLKSHCDSVDTRRPVLYCYEIQLLEEVRGMKLGHKLLNVLYTIAANNQMTRVMLTVFKFNSLAHTFFTKNGFKTDISDPSLHGQSVDYSILSRPP | Catalytic Activity: acetyl-CoA + N-terminal L-seryl-[histone H2A] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[histone H2A]
EC: 2.3.1.257
Subcellular Location: Cytoplasm
Sequence Length: 191
Sequence Mass (Da): 22206
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A0A158QK23 | MSANQYGIETDAMTLQRFVLHEQRKHPSASGDLTNLLTSLSTAFKAISSSVRKAGLAHLYGIAGNTNVQGEEVKKLDVLSNELMINMINSSYTCCAMVSEENDNLIEVEASKQGKYVVTFDPLDGSSNIDCLVSIGTIFGIWKKHKDGPVTREDLLQSGRNMVAAGYCLYGSATMVVLCTGRHVNGFMLDPSIGEFILTHPKMKIPEKGKIYSVNEGYERFWSKGLREYIHSRKHPEPGKKGMVARYVGSMVADVHRTLLYGGVFLYPPTGDAPQGKLRYLYESAPMAFLVEHAGGIAHTGKFSERIISRQIMPAPSAYGFETDSMTLQRFVLAEQRKHPQASGDLTNLLTSLLTAFKAISSAVRKAGLANLYGIAGDTNIQGEEVKKLDVLSNELMINMIRSSYNCGGMVSEENDNSIGEFILTHPHMRIPEKGKIYSINEGYAKHWSKGLTEYIHTRKFPKEGKKAMVQRYVGSMVADIHRTLLYGGIFLYPPTKDAPNGKLRLLYECAPISFLIEQAGGLATTGKTPVLDVVPEDIHQRCPLYMGSKKDIEELLSYIASD | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.11
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
Sequence Length: 563
Sequence Mass (Da): 62189
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A0A7C4SK64 | MIWGLLTVLIDKYGRPLLNVRFVITLRCNFRCIFCHRENSQVCDSELSPDELSILAEAFAKVGVRKYKITGGEPLLRDDVVEIVKCLKSYGEADDISITTNGFYLREHINKLVEGGLNRINVSLHSLRPSRFEFVTGVNALERVVLGIKESLNYSLSKIKLNFVALKGVNEDEVWDIIRFAEGLGIHVQLIELHPVGRGRDVFSNYYASLSEILTDLREKAVKTIIRGELHNRPIYVLPSGTTVEVVRPVLNPIFCAGCSRIRVSPNGALIPCLNSDEVFPTTHIIKEGSCRDKKVGEVVDLILRVNNIRRPHALWPIKSDIEYEYLSLMKLGNTVRKFTLTTR | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
EC: 4.1.99.22
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Length: 344
Sequence Mass (Da): 38903
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A0A0N4WJT4 | MPSVDIFGACGKRSLNKPEAHRMIREHYKFYLAFENSNCHQYITEKFWINALRNDAIPIVMGAPKNDYLSVAPPNSFIHVDDYTPEQLSR | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 90
Sequence Mass (Da): 10430
Location Topology: Single-pass type II membrane protein
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A0A445HHK9 | MTRCDAAARQPLREVQAYFKSMAVSYVHMLQRNRAFHKAFVANLDLKIVFLRSQTVTVSFYLQRRGKRVVSNLENNEGESRTASEMADVLYHSMALLAKKGVKIEDVLQVLRLRFSQSGIEEKKSRVFQKSMD | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
EC: 3.6.1.31
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)
Sequence Length: 133
Sequence Mass (Da): 15345
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A0A4X1SLA4 | MGIWLNQSSIDGFILLGIFSHRQTDLVLFSMVMVVFIVALCGNILLIFLIYKDPRLHTPMYFFLRQLSLMDLMLVSDIVPKMAVNFLLGRKSISFVGCGIQIGFFVSLVGSEGLLLGLMAYDRYIAITHPLHYSILMSQRVCLQIAGSSWTFGIIDGMIQMVAAMSLPYCGSRNVDHFFCEVPALLKLTCTDTSIFDTLLFACCVFMLLLPFSIILASYACILKAVLHMHSAQARKKALATCSSHLTTVSLFYGAAMFIYLRPRHYRAPSHDKVVSIFYTVLTPMLNPLIYSLRNREVMGALRKGLGLCKICSQH | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 315
Sequence Mass (Da): 35282
Location Topology: Multi-pass membrane protein
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K4FSS4 | MAVGAAAAPGARAAAPGHGAGRPVPPPWQLWTVTGTPLEQVQERLRRRGLSDPWARNEAWRFSGKFAQTSSFTNIMFRGFKWGFAAFVVALGVEYVLSPPKKDGGQH | 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: 107
Sequence Mass (Da): 11589
Location Topology: Single-pass membrane protein
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A0A0R3T859 | MCIGISYAFWSLLLYLDTFGRSDVQSTPTKSINQHRPPAWILVLFTCTVFIFLGGLSRAFHQSPLRSFYQLLPLTLALILLLTPRYREDLSHLLQNALFSPASPSRGMFTKIVLLLFLLMEFALWGFIHRILLSFGGVLLGLWPYLDPTFITLQNRATLQRLWLVALCSSICILSAVLAVHKVFLKSDLSAAWLTSPSGLLVSGSAISGLLVFLVRNLVDWSIPIPILLHVISWILLVTSPMIALFGKTSTVCERLIGISLAFFIPFNLLNTFYEGFFFLALATTVFMWIWLESGLQLQEVFSLKSRPESINGSSKQGNDSQMTSFSLRRPFFYVFFVIYAFFGTGNIASINTFDPVSVYCFITVLSPPVMGALLIFKIICPIVVVGTSYALLGYVKSNTSATSSRQEITVLMIIANFLAVHFFAMLRDEGSWLDIGESISHYVIAMSIGLASVLLSHVGGWMLTSPWTSRHTDTKLS | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
EC: 2.-.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 478
Sequence Mass (Da): 53314
Location Topology: Multi-pass membrane protein
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A0A8J1XYK3 | MAAPMKTIFVISLFAVILLGAIDVLLNFEKNGCEMTYMYEYPHYEPVPLKKSVEQKYPKYGLYVYGEGAYARTLGKMEFNGIPVLFIPGNAGSYKQVRSLGSVAYRRMRDKKIPFQFNYFSIDFSEELSGVYGGVLQEQTEFVHVCLKHILTLYKKASHPPSSVVIVGHSMGGIIARGLFALTDFNSKLINTIITQATPHQAPVMAMDIHVKQYYDKVNAYWHWHVNDTLKDVTIVSTGGGYRDNMVRSGLTSLRDIVPPERSLSTLSMSVPKAWVSTDHLCAVWCKQMVMATKRAMFDIIDRKTHQVITNTAEKMAIFRHHLYRNKGGAYVANKAETPIVLDKSIKQEVRTETSWRFLRNKVKNAHYFCVMIPQGDDWRIVATSTVDVDMWVLGCKADQSETCLTATDLSHKGGIIPPQYANKKMISIKPTDVTGFTHVILSIPKSKTQIEVTVETFTNTERYLSYTLLNISRGLFNFPNSLMTAETVIKATRENELFYDVELIGLSAPLQAYTASLTSLSCSNDTQKGNYDGSLMILNIPWSNENVYQFSKPNKNSSLAVKLQIPRPQNFEANARLQLFLQPGCTYRLAMKPAWTELLGQLVRFYGNLFPTFIVINILMVLSWQLHTLHKTGSAVGFTDAHTAWGQSYRVAPPAALLRIILGTFIFAPALQLLRVPRDDVEGLAAQGIWFPLLPLSLYVLATSLVLVHHALVSIALYIASAILGFICARCCRSNRSGDIATFFQYNIVVIATLVAGIFSGSVGLVMVFVLLLAKVLLLHIQKKSGTKDVSTYNVYKTVLLLWNWLVILNAPSLIVWFQNLSYSMSLSRDPARVTSIVSCLSLIILFYTLGPVTNRAVYKTASWAVYLQCIPMVLYSISSIYRISYFITIAILFVAVSAILQLVVPSSEEVDISEPTVDGKEKTE | Function: Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
EC: 3.1.-.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 926
Sequence Mass (Da): 103696
Location Topology: Multi-pass membrane protein
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A0A0N4W550 | LILIWKTQSQSVNRRLTGTVPIIAEAEEYASVVQLATQKADYCECSQVLLFICAWFLYSQTLASVEPSGMMECEVRNFSLRFILAVPNGIPDTECQWLLNNMFPALFKWLRFIDPKRVIRKTNALLDIESYSIRYRKLKENYGRQLVETWTEKTDPKKFVYEDCGIAAYLLVCLKRGRTPKKIADIGCGNGLLVYLLNKEGVGGVGVDIRRRKIWLELLRDTTLIEEVVDPSKVFLTLIEDVALPEGVDYLIGNHTDELTPWMPVMAARINCDFFVLPCCPFNFHGKYTARPGDRGSQYNAFLGFIREVR | Function: Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Catalytic Activity: S-adenosyl-L-methionine + uridine(44) in tRNA(Ser) = 2'-O-methyluridine(44) in tRNA(Ser) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.211
Subcellular Location: Cytoplasm
Sequence Length: 310
Sequence Mass (Da): 35498
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