ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A518H8G8 | MKPDDPNLKRLEPPKLTVLEQTYLPQILGGLAVTGRHILGAAFGGTAVTVQYPEEQHVPTANYRGVHRLNKDEQGRVKCVACMLCATACPAHCIDIVGATAPEGWDDREKYPESFVIDELRCIFCGMCEEACPVDAIELTGLYDLTGLSREELIYDKSKLLSVFDMTKDAEPMKTGNPSPSLPQPTTPLDPEGPGPRSTATAAQLPSRS | 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: 209
Sequence Mass (Da): 22697
Location Topology: Peripheral membrane protein
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A0A1J4XHU5 | MIARPNEPMALHTTWHLGGAADWFLQPETVGQWFDWCRDHPVEGPLLVIGRGSNILVRDGGVAGTVLSTKQWKGLTVQADGRVRAEAGVAVASLSRAALDKGLTGIEFLVGIPGSVGGAIRMNAGAHGGEIGPLVTEVVTCDRHGKRKVWRGDEIQWRYRHSSIPEDQIVVEVALELRPGEGGAIRSKMAAIIERRNATQPLHRLNAGSVFRNPDGDYAARLIEAAGLKGAKVGGAQVDPMHANFITHEGDASAADVERLIAMVQEQVHARFGVTLVREVQIVGRPA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 287
Sequence Mass (Da): 30805
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A0A1E3HJF0 | MGGAVFLGCWLMGGSWLVGVLGVVSHLSHWWFLEFVESPHMQKLYGNRLRKDGGLTKTLKSNLPNSTAVRQAVSKHPRVSRVVSEVNRGIEKVEERVRGGVEDFLDHARPMLDGVVDDARGLLQQSRERMIITRVAKPKDLTSFDPSSYSLQIPTSSSSPTPYPAFHVGQPIPISWNAPSNHSSKDWIGIYRLGSCKSEIVTKISSVGKWVGVYEEEWEGNEHVTPESEGKKADAGMVVLKGKQLPWQPGQYEIRYHHDGKHNVMSRLAPIELYVDKPRASRSSRVSSPRRSSASLSSSPSKSVKTAEIKEEVGVKEVRETMMKLVCLALEGEEELVPKAAKGKAVMRLASVPTAASQVSPGKALNKPTLSYTPELDEGDEGEDGVEADAEVEDQGSLLGSGVAGGEKRAGKAGKVDKKGKGKKGGVGIEDEVTRTKDTFSPSNLASADNPHALDHLASLADRSAVPQRSILGLADNDSTRDPGIDRTVDPDSDSEPEADDFTIMTETQAKRIASLAKHAFGVELDADVVVSEANVGALARRVVGAWSLAGV | Pathway: Phospholipid metabolism; phosphatidylcholine biosynthesis.
Subcellular Location: Membrane
Sequence Length: 552
Sequence Mass (Da): 59564
Location Topology: Multi-pass membrane protein
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A0A136JTZ5 | MNSSSENFIIESKEPEKNPEENNNKEHPFVEIVRFSIIALIIVIPIRMFVAQPFIVSGASMEETFQSGEYLIVDQVSYHLHEPVRGDVIVFRYPKDPSKFFIKRIIGLPGDTVKIEGSTVTIINEANPNGFVINEPYIKSMSPDNHLTEKLGAREYFVMGDNRDRSSDSRAWGVLTEDRIIGKAFLRLFPPSALDVMPGAVEMEVISDSK | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 210
Sequence Mass (Da): 23691
Location Topology: Single-pass type II membrane protein
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A0A7W0IPE1 | MKYYPVCLQVEGRRCLVVGGGKVAERKVLGLLGSGAVVIVISPELTPGLAQLGAEGSLTWMSRGYTPGDAEGFFLVMAATDDSIVQNQVRDDGLRFNILVNVADVPEKCNFILPAVVKRGALSIAISTSGKSPALAKKIRQELEVKLGPEYELVVEMMGLLRPHVLQWKLPQADNEILFNGLMEGGLLSLVVERDWPKIQVYLEEGLGRALPLGLVGELKKLVLR | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 225
Sequence Mass (Da): 24432
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A0A923XLI3 | MDDHGDHPWRWIYPPLQCHDQGWLDVGDGHEVYWEVCGNPCGAPALFVHGGPGAGCSRADRRWFDPAHYRIVLFDQRGAGRSRPLGCLQANTTQHAVGDIEALRSHLGVDRWLVMGGSWGATLALAYAQSHPQRVRALVLRGVFLGTGAERRWLYSRQGVAMARPSAWRRLTSALPPPRPLDAVEAFSRQLHCGEPATERDAARAWLQWEGDLMAPEPIGPPSTRPAMRSPQPDTSDHAAALATARIGVHFARHHYFLQDGELLAHAGRLRDCPGVIVQGDADLVTPPAAAASLQRAWSGSQLQLLRCAGHATSHPVLAKQLIAATDLLRDPRFQNKEIIHAGPDLER | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 348
Sequence Mass (Da): 38196
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U1GDI6 | MLSFFVAYAKSSTVGPRVGRLTRVGQKAIKTPHYVATTSRGVVPHISHDTLQKHTAVSSIYLALEDFIEKRITGAPIFKTPAKDGESPLRKYVAAQDDVLSILGPRRVPALPCPAHNNGSAISICTSVGFSQLNVNDYHDALRTLRPDIAITMADVVMHGTASVKRIEKSADRTHAWLRDACEQLSAHEKSSSKPAIFAAIPPIANVQQSLYLQDLAEEYRHMLSGLAIYSSTTAVDLPQALFDLPRMSLSEPGSPHSLLKDMALGVDLLCIPFIGFASDHGIALVFEFPGPDLAIDEPRPLGIDLWSIENEASLLPLSPHCECFTCTRHHKAYIHHLLQAKEMLAWTLLQIHNLSTMDRFFDACRKSIANGSFEEDVELFTRRYETDMPAKTGSGPRIRGYQIKSSGGGEARKNEKAWDRFDDMAQQIAEAESGLATAEGDSKQLEDQGIAERV | Cofactor: Binds 1 zinc ion per subunit.
Function: Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Subcellular Location: Cytoplasm
Sequence Length: 455
Sequence Mass (Da): 50028
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A0A969FEX7 | MERAKLSPAISISAAGVAITVISLWYGQNHGWLPEAASQNAPLVDGLFNLMMTISVWLFLAIQGAIVLAIIKFRKQPGDETDGPPIEGNLSLELVWTAIPVVIVMVLAVYSFDVYQQMGGLDPMASHDHTRIAKVSSGSAIAGSLDGDQGLPHGQNVALGIGANPASEGMDADVTIDVMGLQYAWLFTYPGNVMAGELHIPAGRDVELNIQAQDVLHAFWVPQFRLKQDAIPGRMSKLRFRPETPGTYPIVCAELCGAFHGAMRSTVIVDTPEDYDVWYQTQIASAIDGDANDSRVATAVGMTGLSDADRMALHPHAPAIDAAAIAAITPMAHHHHD | Cofactor: Binds a copper A center.
Function: Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
EC: 7.1.1.9
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
Subcellular Location: Cell membrane
Sequence Length: 337
Sequence Mass (Da): 36034
Location Topology: Multi-pass membrane protein
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A0A942LG87 | MNNLPNILSILRLIIAPLFYVCIISDNRQTAVLGVLLFIIGAVSDYLDGLLARKYHAISSFGKFLDPLADKVLTGFALIAFSSMNIFPLWMVLIVLFRDLVTTVIRTIDTSGRLNFKTSEIARIKTFIQMAFIAAILFIMFLYHTSLLEITQTDFDSFLKSDWIDYVMFVLVLLTVYTLVDYLLNIFASFKKKK | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 194
Sequence Mass (Da): 22144
Location Topology: Multi-pass membrane protein
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G4SUU0 | MSAVFELDKTKLRESFGSASLSYDRVAGLQRTVGINLLQRVAPAQLTGTVVDLGCGTGFLTKSLLDAENVERIVALDIALPMLHAARQKLGDTGRLHYVCGDAESPPLNTNSVDTVVSNLALQWCRDLTAVFCGLHRILKADGELVFSTFGPHTLCELKQAWAAVDDYHHVNEFYRETEIRRCLADAGFKEIAVQSEIYRPVYGSVLALMKELKSMGAHNVSSGRNKRLTTKQEMTSMIEAYPLNDANIEATFEVFIVSARVENND | Pathway: Cofactor biosynthesis; biotin biosynthesis.
Function: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway.
EC: 2.1.1.197
Catalytic Activity: malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 266
Sequence Mass (Da): 29340
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A0A808UQL9 | MIKNYSEFEKGKLLLIDKPWGWTSFEVVKRIKKKIISFSKKIKIGHAGTLDPLATGLLIILTGKYTKKVDSIQNYKKTYTGIIKMGCVTPSFDSETKEYNFSSTSHITSELIQKISKKFIGEINQYPPSFSALKIEGKRFYEYARKGKKIKNMKPRRVRIYQFNILKIGIPYIKFLIECGKGTYIRSIAQDFGIKINSGAYLLSLRRERIGPFSIKNSSKELE | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 223
Sequence Mass (Da): 25658
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A0A429XT39 | MIKKDKPLSPHLTIYKPQITSVLSIMHRITGFILFFGFLIILWTTNIYTFKSTTLEDFGKVLTYLVTNKFFISILILFSYCIFYHMCTGIRYLFWDSGKLMDIKMINLTGWLAVIFSVIFTCIFWYLIIYK | Cofactor: The heme is bound between the two transmembrane subunits.
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Cell inner membrane
Sequence Length: 131
Sequence Mass (Da): 15558
Location Topology: Multi-pass membrane protein
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A0A484GB52 | MNKAHQFGVLLVNLGTPENLSYSAVTQFLTEFLLDRHVVDLPALFWKPLLTKIILPRRIPNTINNYKKIWLSEGSPLWVYSQQLTQTVAAQLPDISCKLAMTYGQPNLMEQIECLKYCDRIRIIPLFPQYSTTTTLPILNKIKQITANWVNPPYIEYIPDYANESLYITALTDTIVAHVKQHGIPDTLLLSYHGIPIKYIRKRQDSYLTRCELTTHILKQQLQQYGYHLEIMHSYQSQFGKGEWSKPDTTTMLTELAAKGNHHVAVVCPGFAVDCVETLEEIATFNREKFIQSGGTDFYYISALNNSAAHVTLLLHLIHHASALPLSPP | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1.
Function: Catalyzes the ferrous insertion into protoporphyrin IX.
Catalytic Activity: 2 H(+) + heme b = Fe(2+) + protoporphyrin IX
EC: 4.98.1.1
Subcellular Location: Cytoplasm
Sequence Length: 329
Sequence Mass (Da): 37481
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A0A7W8B3M7 | MNSRPVLALILPPGPRLYRALQEALSGTGPALCPFSPQMPAFHRKELLTALAPAAVETISGQQPWVPAGSRVDPEVAVVLATSGSSGTPKFAELSASALRYSARAALDRLAAEPGERWLCCLPTSHISGLQILTRSILTHTKPDIVPRFDVAVVAASDAAFLSVAPTQLRRLVDAQVDMSRFRAVLVGGAALSQDLRTAAQAHGARIVTTYGATETCGGCVYDGTPLTGVRVQLSDSGRVLLAGPVLFRGYRNNPGLTAAAWDGNWFQTQDLGVLRDGQLHVLGRADNVINTGGEKIAADRVARVLALHPHVRDVVVVGRPDPEWGERIVAVVVPGNAPPSLTELRAWAQTYLPPAAAPRELELVSAIPLLASGKPDRAQLATPTASPGAAPSARHAVGPRGEDRSTETLTRWCTAERTTMVSELFDPREWKPVDGFEFTDVTYHRAIDQGTVRIAFNRPTVRNAFRPHTVDELCRALDHARQWREIGCVLLTGNGPSSKDGGWAFCSGGDQRVRGKHGYQYTDDGTSVAIAPDQAGRLHILEAQRLIRFMGKVVICLVPGWAAGGGHSLHVVCDLTIASREHAQFKQTDADVGSFDGGFGSAYLARQVGQKFAREIFFLGDTYTADDAHRMGMVNSVVPHAELETTALHWAAQINRKSPTAQRMLKFAFNLIDDGLVGQQVFAGEATRLAYGTDEAAEGCDAFLRKRSPDWSRFPWHY | Pathway: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 6/7.
Function: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
EC: 4.1.3.36
Catalytic Activity: 2-succinylbenzoyl-CoA + H(+) = 1,4-dihydroxy-2-naphthoyl-CoA + H2O
Sequence Length: 719
Sequence Mass (Da): 77569
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A0A939DNN6 | MLRLTSCILILLFSLPLNAAQQAAVAMPDSYSAEAAAKVLKDGGNAVDAAVTAGFVLAVTLPEAGNIGGGGFMLVYKDGKADFLDYREKAPLKAHRDMYLDKQGKVMTEKPLYGILASGVPGSVMGMWQAHQKYGSRPWKALLAPAIQLAEEGFVPHEKLVRYVERYIERVKQDRHGRNFDQYFSGMVTDQPFKQPELAATLKRIAETGPDDFYKGETARLLAGFMQKHGGLISLQDLAQYTAEWRQPLSEGWQGYQVLSAPPPSSGGLVLLQMLKMQSVLQDHFAGLEHNSARYVHLLAELAKRGFADRAEYMGDPDFYQVPTDKLLADDYIGRRAMEVNVEQISETAKIQPGLKESEDTTHYSIIDKWGNAVSTTTTINLSFGSGVVVEGAGFLLNDEMDDFSAKAGVPNYFGAVGSEANEIVPQKRMLSSMTPTILLKNGIVTMVTGSPGGTTIINSVFQSILNRHLYQMTAQQTVDAPRVHHQLLPKDTLRHHPDLNEQTRKALEKMGYTLDGRRFGDLQVISRDEHGQLQAASESSGRGRSLVF | 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: 549
Sequence Mass (Da): 60398
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A0A0K1P6T3 | MNIVVATKNKFKLKEYKSILTDYNVISLNDCDITEEIPEDNDTFKDNALQKALFISEKLNKPVIADDSGLSITNLNNFPGIYSARWANPITDYNIINNKIISMLDEKNLHSKNERKAFFTCAIAFVDKSNSIKEVFESTLEGYISNYEVGENGFAYDKIFKLFDSNLTLAELDSSQKNLISHRRKAIDKLIIYLNNKYKR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
EC: 3.6.1.66
Catalytic Activity: H2O + ITP = diphosphate + H(+) + IMP
Sequence Length: 200
Sequence Mass (Da): 22971
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A0A9D9H2M4 | MQIASFTLSSIVEATHGRCFHAGGRIMAGNPAMDMRIDQIITDSRSFETVRSALFVALRSRKNDGHRYVRKMYVEGVRYFLISCFLPEFETMPDAFFIEVEDTMIALQEWAAWHRSRFSVPVVGITGSNGKTIVKEWLSFLLGFDKHIVRSPKSFNSQIGVPLSVLQMDTADDMGIFEAGISEPGEMASLRAVMQPTIGILTNIGTAHDAGFENRRQKTCEKLKLFGLSQKLIFCADYQDIIGALADGGLPKSVRLLSWSAVTSDKQSVSAGPADMQILENRVCSGGRMLKALFRAREHSLRIPFSDQASFENAVHCWLFMLDAGFPDAVIEDRFRQLPSLKMRMEMKEGVGHSWVLNDAYSSDFTSFCLAVDFLCNHAQGKPCCVIMSDILQSGRPEAELYGEVADVLRQKGIRELVAVGSAVMRQQSCFAEFEARFYPDTDRLLQDFRCEDYAGKAILLKGARVFAFEKIDALLQRRVHETVMEVNLSALVHNLNYFRGLLKPETKLMVMGKAFSYGSGSHEIADVLEFNHVDYVTVAYVDEAVALRNNGIRLPIMCMNAEVEGLETAVRYQVEPAIYNFRMLETLENYLSGENRPSGLASDSGQDVVKVHIGLDTGMHRMGFEEKDLDSLLPRLASNPRIKVQSVYTHLATADMPEMDAYTRKQLALYTQMSHRFKTLFPDILRHCLNTAGIFYYPDYQFEMVRLGIGLYGVGTDAVMQKHLETVSTLKTVISQIRIIPAGDAVGYGRRFVARRETRVGVIGIGYADGLNRHLGNGRYHVLVNGCKVPIIGSICMDMCMIDLTDVPAQEGDEVEIFGKQHPIDVMASCLDTIPYEILTSVSLRVKRVYIND | Pathway: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1.
Function: Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids.
EC: 5.1.1.1
Catalytic Activity: L-alanine = D-alanine
Sequence Length: 854
Sequence Mass (Da): 95609
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J9G9A3 | MKIPNAQQVKALDEYTIQHEPIRSIDLMERAAEAVVQVIMSRWGAEVPVVVFAGPGNNGGDALAVARLLAARDYRVTAYLFNINDYLSEDCACNKERLQYVSGVEFKEIKNAFEAPALNRSTLVIDGLFGIGQNRTLTGGFAMLVKFINASDAEVVSIDMPSGMMCEDNTYNVRGHIIRATLTLTFQLPKLALLLPDNQPFVGELQVLDIGLSPQAIADLDTVASISTKEEMAQLLKPRDPFGHKGTFGHGLLVAGKYGMAGAAILAA | Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This 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: (6R)-NADHX = (6S)-NADHX
Sequence Length: 268
Sequence Mass (Da): 28997
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A0A4Y7LEA2 | MANLIQKLCGKLNQFFMNGGKEEGISKNEFMPVGADGRDLLAPVAEALAPIANITVESQVLYHTPKSSFSYWDAKLSSYVFRTKDLPFFMWGGVIVWNPPRCFRSSKSMQPQKHTLTSEDLEELLEVSLGQLRQLFGLKSNNLYVGESGMSSVLSSERGFTEWELDALSRQHTCFNLHSCATTLGSLSRLVQSLPRMIIKDEIGKQVKFSLEAANLAQTNASSGIYEASAVSSRQARALAEDAFFHPSIMSISYYSFEHCFAVYTPFFLPVALHVLLASAKEWRRYKQEHMKYFTWISKTKAE | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 303
Sequence Mass (Da): 34143
Location Topology: Multi-pass membrane protein
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E4TFZ4 | MIFEKELNLPFKKEISGEITPHKCNEFGIVSDDYVSLKPKFEKNPGDLIKPGDLLFYDSKNRGIRFYSFVNGEVCEITRGEKRRFISYTLKGEPSVYNYPENLSKISLKKENRDKIIDIIINSGFWISIRQRPFDRVANPDVVPDKIFVLLIDTRPYSPEIKTILNGNEEYLKTGLQIFSILTKTDLYLIKDKRITFDVELENLKIIDVSGHHPAGLVGTHINNLYPLNRKRSIWYIDYQDIIAIGKLFKDNIIDNQKVISVGGEGVKNSLYRVYNYASLDMLVPFNDDIRIIYGSPLYGRKATNKTNYTNRYINIVSSLKEANKREFMGWLKPGLNRFSVKNVFLSKLLKKEITFDTSLNGSFRPMIPVGSYEKVCLLNLPITYFLRSLLVEDIEMAEKLGVLDFGEEDMSVFTFVCVGKYDYAVYLRKILDEIEGEM | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
EC: 7.2.1.1
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Sequence Length: 439
Sequence Mass (Da): 50725
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A0KMB0 | MHILLFGKNGQVGWELQRALAPLGRITAVDFDSTDYCGDFSKPAGVAETVRQVKPDVIVNAAAHTAVDKAESEREFAELLNITSVAAIAREAEALGAWLVHYSTDYVFDGSGERPWLETDVTAPLNVYGETKLAGEQAAALCSRHLIFRTSWVYAARGANFAKTMLRFGKERSEMSVINDQFGAPTGAELLADCTAHVLRVAQSRPEVAGLYHLIASGTTTWFDYAQLVFAKAREAGVELAVTQLNAVPTSAFPTPAKRPHNSRLDTSKFQRTFDLVLPDWTVGVERMLTEILGK | Cofactor: Binds 1 Mg(2+) ion per monomer.
Pathway: Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Function: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose.
EC: 1.1.1.133
Catalytic Activity: dTDP-beta-L-rhamnose + NADP(+) = dTDP-4-dehydro-beta-L-rhamnose + H(+) + NADPH
Sequence Length: 295
Sequence Mass (Da): 32246
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L0P9N7 | MLEARLQQASVLKKILDAVKELISDVNIECNESGIALQAMDNSHVALVVMLLRMDGFEPYRCDRNISLGVNLNSFSKVLKCAQNEDIITLKAEDTPDTLNMVFESPTNDRISEYDIKLMDIDQEHLGIPDTEYSVVVKMQSIEFQRICRDLLALSESVHVEANKEGIKFSCSGDIGNGSITLIQNQDTNIELNEPVSLTFSLKYLVNFTKATPLAEIVILSMSNELPLMVEYKMETGHLRFYLAPKISEEYKLASLYTRTILNNKPWITSCKYVRWQSMVPFKRSHRHSSTVSSQRSSLYEQTINKDKTYHAAQAVSLGIENPPLSEKETFTSNAKDISTETSPPLTKQEGKKDKKKTLWQKIKGEAQHYWDGTKLLGAETKISYKLALKMAAGHELTRREHRQLQRTVKDLVRLVPFSAFILIPFAELLLPLALKLFPNMLPSTYEADKDKEKRQTKLSDTRKSVSQFLRATLQESGLPFSTTTKQRQEFTEFFRKIRSGKELPSQTDVINVSKLFRDDITLDNLSRPQLVAMCRYMNLNTFGTDPMLRYQIRHKMRKIKSDDKAIWYEGVDTLSVPELQVACANRGIRTHGLSPAKLRDELEQWLDLRLKHGVPSTLLLLSNAFMYDQDDQSDRHYNALIATLSSLPDELYHETELNVQDKEATNKQRLEVIMEQEV | Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
Subcellular Location: Membrane
Sequence Length: 679
Sequence Mass (Da): 77689
Location Topology: Single-pass membrane protein
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A0A0P1FA25 | MHVVTILSNPNEPHLEASLLDSLRNAWGGDDVVWLAPSQAAEFEIPQLPDNRWDVWGDVQRMGLDMVVQPVEGRQKKMLLADMDSTMIQQECIDELADEAGVGERVASITARAMNGELDFEGALLERVGLLKGLQESVIDKVLADRITLMPGGRELIATMKAAGGYAALVSGGFTAFTRQVAKDLGFDENHANILLVEDGVLTGDVARPILGREAKVAALERISKHLQIEESDVIAVGDGANDLGMLGRAGTGVALHAKPTVAAQCDVRINFGDLTSLLYIQGYAKHEFATS | Pathway: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
EC: 3.1.3.3
Catalytic Activity: H2O + O-phospho-D-serine = D-serine + phosphate
Sequence Length: 292
Sequence Mass (Da): 31398
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A0A7Y5HAF5 | MKWSIRIARVRGIGIYVHLTFFLVLVWVGWMEWQRSGSMAQVGGGVLFTLLTFFIIVLHELGHAISAGWFGIRTKDITLLPIGGLARLERMPEKPWQEIVVALAGPAVNVILALAIGGAILLAGRRPDLFGSDPMTGSLPARLFWLNVILTAFNLIPAFPMDGGRVLRASLAAVTDHATGTRWAALVGRGIAALFVVAGLTWNPGLALIGIFVWFGAGAEARAAELKSSLAGLLAGHALQTDIRILDGRETVGQAALRTLASPQFEYPVMVEGRLVGIATATALTEALAQSGPATPVLNATRTDAVVAGLDTPLEQMVGLIQGSGLRSGLVTDQAGKLLGAVTLDSISSAIQLRAAWADAGSAGRS | Cofactor: Binds 1 zinc ion per subunit.
Subcellular Location: Cell membrane
Sequence Length: 366
Sequence Mass (Da): 38434
Location Topology: Multi-pass membrane protein
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G4SVA1 | MHQEFWLERWQQNQIGFHSESINPHLEQYWPALHIEAGSRVFVPLCGKSNDILWLLAQNYRVIGVELSPLAVNAFFTENKVPATAGRKDKFEVWENDDLCIYCGDFFHLREEDLTGVDAVYDRASLVALPPEMRANYAAHMKRLLKTGTKILLVAFDYSQQEMDGPPFSVQCQEVEMLYRDWCRIDLLLTEDILSKEPRFRERGLSRLQEQVYVLTVL | Catalytic Activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether.
EC: 2.1.1.67
Subcellular Location: Cytoplasm
Sequence Length: 218
Sequence Mass (Da): 25441
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A0A1G9QXP4 | MTDFNRSEMLTIGAEEELFVVDHKTKAPVSNGLAGFSTLLNGRSTGEIGGYDTEFQAAIVETRTGICGSLGDLHSELVALRRALADAADAEGRSVVCAGTLPIGDWRAVDVVPKPRYHQIADHYHDVVRRRFTCGYHVHVGVDDRDRAVHVLNRVAPWLPTLLAVSASSPFFASRSTGYASYRHTLWGGFPVAGPAPRFESYSQYQQYADMLIATGTILDAGHIYWDARLGTRFETVEFRIMDACPSVDDAVLVAALCRALVLTVLREIEQGKPEVRMDQPFLRAATWHAARWGLDKDLIDVGAKEAVPASTMVERFLQYIRGALEDLKDFDAVSDLMRQVSRSGNSAVRQRAILLRGGSLRDVTEQLVSLTDSGNVAVP | Function: ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
EC: 6.3.2.2
Catalytic Activity: ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-cysteine + H(+) + phosphate
Sequence Length: 380
Sequence Mass (Da): 41734
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A0A011Q4K7 | MSDGDKTSTHPEQPEHSHSALATPTEHLAYVALGANLADPQAQVRAAARALAGVAECRLQRLSSLYRTAPVGGRVIRRQADFINAVAALHTRLTPAQLLDALLAIERVFGRRREYHHAPRTLDLDLLLYDDLVVDSQRLSLPHPRMHLRAFVIAPLLEIAPQAPIPGRGSAAAWWPAVSRQAVERLAD | 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: 188
Sequence Mass (Da): 20598
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A0A849WI51 | MSFIGKTALITGASRGIGRAIALELAKQGADIGINYVSNQEQAQSLSQEIQALGRKSILLPASVAQEEEVKRMFNSFVEAFGKLDILVCNAGIVRDNLILRMKAEDFMEVIRVNLIGTFLCMKEAGSLMLRNRYGRVVAVSSITGTLGNIGQANYAASKSGMIGLVKTFAQEFAKRDITANVVVPGLIETDMTNKLTAETKEKFLSCIPKKRMGTPEEVAKMVAFLCSEEAAYITGDTFSIAGGM | Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
EC: 1.1.1.100
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+) + NADPH
Sequence Length: 245
Sequence Mass (Da): 26418
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A0A151EBS9 | MTPFQRKVYALLKKVPKGKVTTYGALAKKLKSSPRAVGQALRVNPYAPKVPCHRVVSSDGSIGGFRGKTQGKAVREKIGLLRKEGIKIINGRVEKSSFSF | 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.
EC: 2.1.1.63
Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
Sequence Length: 100
Sequence Mass (Da): 10913
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R7LUZ2 | MQKGLFITFEGADGCGKTTQLNLLKAYLENKGFEVVLTREPGGKGLGEHIRKILLNYDGEVSNRCESFLFLADRAQNIDIIVNPAIERGKIVLCDRHTDSTVAYQGYGRGLDIAQINKLNDLATNGKKPDLTFVFDVDIETSMQRVGAEKDRMESAGKEFFNRVRQGYLKLAKLEPQRIKVVDSTKSIDEVQIQVQKIIEKYI | 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: 203
Sequence Mass (Da): 22858
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A0A834G7N2 | MGNPEVGRDEPLSPLGRLFLTPEMHQIVHCIMGCENPIDVAAITSEIANSVMVRLPRFSSLLARDSHGREHWRKTQVDVHRHVIVVEEPVSSAVDDGEAVNDYVADLSVSYPLSYDKPLWEVHLLKAHNCIIFRIHHALGDGISLMSMLQEWCQRADHELDRRLSVGSMGTNSNSSSNREKRWTQLWKVVVGMLMGLGFIMEFALRALWVKDKRTAVSGGAGVELWPRKLATAKFRLDDMKAVKKVVTNATINDVLFGVVSSGLSRYLDLRTPKALQDGVQITGLAMVNLRKQSGLQELSDMLRCNSGNPWGNKFGMLLVPFYYRRGGANPLQYVRIAKQMMDQKKQSLEAQFSYNMEKLLMSYFGPQNYPIVKLLKHNSDFPSDHSNVIGPKEEITIAGNPVKYLRLNNTSLPHVKLLKLTLIFHPIILEARNPPFAMLKVEKTFSGSTPLPQQHHFRAATKPENPFSWKQSYATASAITMHMLSYAGRVDMQILVAKDIIPDPQVLAKCFEDALLQMKEAATKE | Pathway: Glycerolipid metabolism; triacylglycerol biosynthesis.
Catalytic Activity: a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA
Subcellular Location: Cell membrane
Sequence Length: 526
Sequence Mass (Da): 59197
Location Topology: Single-pass membrane protein
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B0D3Z9 | MSPRKRKRSQAFEEYDENEDFLPQNQDSQEIDSGERDQLQLDKERDIWDAFREEHFEVVEQLPLTLHRQFSLMRQLDEQAQGYTSHLIPTLMRYIKTRRSIGARLPSDETGHTHQNGTINGESSSITPAKVAAPLRQDIFDSCTSSEPPAPMGLPPERRKIPQTTREMLSHIAWLSEELLRGSQEKVNLAQAAHDSIDRQLRLIEQAIAEQEANLSQEDVAAVNIHLPDLIIPKWSRNTTSSKGNDQDNVGAMEGSTVGRSLLPGEWSGPLNNSQDGRGAKREGHFTGPVPRKALQENAMQDAPPLKITLPAPHSRNHLPSNGGDSTEELYCYCNRVSFGEMIACDNKACTREWFHLGCVGLTEPPEGEWFCEDCSVTEI | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 380
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 42732
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A0A1I5X8H0 | MELHVCKDYDDLCEHLANWMVDCICKTLATKERFSIAFTGGNTAKRLYALLAGDAYKNKIDWSRANIFIGDERFVPYSDERSNARMIRETLLNHVAVNEAHIHFMQTENMSAETSAAEYEEVLQHYFNKGTNEPTFDVVLLGMGDDAHTLSLFPGHTDAINEKNKWCTYLWLEQQDMYRITITAPITNAAKYLAFIVSGSGKAVALNNVMHKPYDPEKYPSQIIKPVHGELNWFVDEAAMNG | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Length: 242
Sequence Mass (Da): 27536
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U5LCH6 | MCINHEKPDISNLDNPSYYNNRELSWLDFNNRVLEEAEDNQNALLERYKFLSIFSSNLDEFFMVRVAGLLDQVKAGFNKPENKAGLTPKEQLSAISEKTHTLVKKQDEIYCNELTPLLTKEQIEISRIKDVPSKDLAFLENFFEAYVYPVLTPMAIDAYRPFPMLLNKSLNLAVIIEEKSPDKKKHLSLDGNLVIVQVPSVIDRLVELPQKGQARKFVLLEEVIIYCIHKLFTGYKVRSATPFRITRNADLAIHEDEAEDLLQEIEEELKKRKRGAAVRLEYQQAENSSQVIEFLRKELEIHGKDIYPVEAPLDLTFLFSFCKKIQASHEHLAAQSFIPQPPQDLEGEGGIFEKIRKRDALLHHPYESFEPVVDFMREAADDKDVLAIKQTLYRVSGDSPIIESLKRAAENGKQVTVLVELKARFDEENNVQWAKELEQAGCHVIYGMTLLKTHSKITLVIRREKGNIQRYVHLGTGNYNDATARIYTDMGLLTCNHQLGEDAINFFNYLSGYMERPCFPLRVL | PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
EC: 2.7.4.1
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Length: 524
Sequence Mass (Da): 60251
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A0A1H1TWV6 | MGPTAWRHWAEAARPKTLPAAVIPVLVGTALAAAHRTADCGKAAICLLFALLVQIGTNFANDYFDFVKGADTPARVGPRRAVAAGLIAPRTMLRATGLVLGVAFLVGLLLVREGGWILLPIGIISIVCAIAYTGGPFPLGYNGLGDLFVFIFFGLVAVDTTFYVQAGGLAPDATSCAAAVGLLAANILVANNYRDAETDARAGKRTLVVRFGRKFAVWQYALSHIVALLCPAALIIHGYRWPVLLPLVLAPWAFGLTRRLAASREPAEQIALLAATAKYLAAFGVLLSAGLILGR | Pathway: Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 1/2.
Function: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK).
Catalytic Activity: 1,4-dihydroxy-2-naphthoate + an all-trans-polyprenyl diphosphate + H(+) = a 2-demethylmenaquinol + CO2 + diphosphate
EC: 2.5.1.74
Subcellular Location: Cell membrane
Sequence Length: 295
Sequence Mass (Da): 31029
Location Topology: Multi-pass membrane protein
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A0A7V5FRN2 | MITLDITLFIHIINMIVMMVVLNAILYKPVLGILEKRREKLDSLAQDVEQFEENARHRQAEVDRKMHEASMQAKKALDGARSEAQAAGAEKLAAIRKEAEGEKEKQLADLRTQIEKARKELADNVSGFAQEMAGKILGRSLEA | 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: 143
Sequence Mass (Da): 16027
Location Topology: Single-pass membrane protein
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U1FWT0 | MSVVSKKTQFLDSISFVGGFYTDSAYLQMAPNSNHGRILFIDAYDSFSENIAALFCQILPVEVTMIHIDTQIEELLDKPADCTQNALALYLQNFDAVVLGPGPGNPEATSDVGLFSEIWRLPSLDVVPVLGICLGFQSLCLAYGASIRRMLEPCHGHAKGIKHCDEDIFTNVGEVIATNYNSLEVELGDKHSLAEDSGPTSSSPSVESGSSSPSTLCTEFYPSQPEFEPSLTCPKLRPLAWDGFGTSMSVKHVELPFWGLQFHPESCKSNAACQSIIKNWWNTSMHWSTRTRRATNLSRSKLLSGHVWSRPLTPIHIIAEPCDIAENHRLTSTLQEELQALTASSAATVEFHTMMLPKSAGQVLELCRSLSQNDQAILESTRKGRFSIYAVPGPSEFRMEYNLETSTCTLNLTDQDKMQWKMKLLHVLDEIQGLVVRRRVKAGHDSVPFFGGFIGYFSYEVGLERLGVKQELRSASEVLPDINLLWVERSIVIDHVSNEAHIQSIRKDDSTWIAEMVDKLNRLGCPESPIALRSARLQALLTAAKIRLPDEEIYKREIQACQDYLHSGDSYELCLTTGAQISLPTHPENSWLLYHNLRHHNPVPFSAFLRLGRTTILSSSPEQFLSWDRSSGSINMIPMKGTVAKSPSMNLALAKEILASPKESAENLMIADLIRHDLYSTVGWNASVEVIKLCEVVEHETVYQLVSHIRAMPSIPPTLSADERQQEIMRYGHKALRQTLPPGSMTGAPKKRSCEILRRLEQRRRGVYSGVLGYLDVGGGGAFSVCIRTAVSNADEDRDGRQTWRVGAGGAITVLSDVDAEWEEMKTKLESVLRAFRPDG | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-aminobenzoate from chorismate: step 1/2.
EC: 2.6.1.85
Catalytic Activity: chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
Sequence Length: 840
Sequence Mass (Da): 93354
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A0A2T2VXR2 | MHTLDAQTKRLLEVTASFPHLRVLVIGDAMLDSYLQGSSTRLCREAPVPIVDVGETSHVPGGAANTAANVATLGAEAYLLTVIGDDGAGQQLEAALAESGVNLAGVVRSRDRTTLVKQRLLAENQLLLRFDQGSTAGLSTADEDQLIARLECYFPLCDAVIISDYAYGILTSRITLTLQRLQSLHPRILVADSKRLEVYKRLDVTAVKPNYDEAIALLGLPRLSGAARVEQMTRHGQRVLSETGAWMATITLDRDGVLIFLEDGEGTVGEPTRTLATPAPNTHATGAGDTYVATLALALAAEADPYGAASLAATATGVVVTEPGTTRCHPLALRRALMEGNKRITDQTELVSIVAQQRHRGQRIVFTNGCFDILHSGHVTCLERAKALGDVLIVGVNTDDSIRQLKGPTRPVNALADRLTVLAALGCVDYVVPFADLAPRELIRLICPDVYAKGGDYTRQSLPETPLIEELGGEVVIVPYVGDRSTTGLIEQIRTAGGS | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
Catalytic Activity: ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-D-glycero-beta-D-manno-heptose + diphosphate
Sequence Length: 499
Sequence Mass (Da): 53282
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A0A2T2WB78 | MAEPLSPFVARHLGPAERDVEAMLEALGYTSLEALIEATVPAGIRLKQTLDLPQGLSESAALEQLKGIAAQNQVWRSYLGLGYANTLTPAVIQRNVLENPGWYTQYTPYQPEIAQGRLEALLNFQTLVTDLTGMDIANASLLDEGTAAAEAMTLAFNARKQKEAKTFWVSATCHPQTVDVVKTRALPLGIEVMVGDHHRFDFDVPVFGVLLQYPATDGAIYDYADFTAQAHAHQALVTVAADLLSLTLLRAPGEFGADIVVGNTQRFGVPLGYGGPHAAFFATCNAFARKLPGRLVGVSKDTYGNPALRLTLQTREQHIRRDAATSNICTAQVLLAIMASMYAVYHGPEGLRAIASRLHQQTQTLAQALTEAGFELGQEPVFDTLRVTVGDAQAAILARAAARRINLRVLDAETLVVALDETVTEQDIQDLITVFIGDSVQNSKFKISPSETLRVGEASPEDLQNSEPSGDSSSPHPLTFPTALRRTTPYLTHPTFNRYHSETEMLRYLYRLQGKDLSLATAMIPLGSCTMKLNATAEMLPITWPEFGQIHPFAPAEQAQGYRQLFTELETWLAEITGFDGVSLQPNAGAQGEYAGLLVIREYHQQRGDTHRHICLIPQSAHGTNPASAVMAGMKVVAVACDDDGNIDVGDLAAKAEKHGDNLAALMVTYPSTHGVFEAEIAEICAIVHAQGGQVYMDGANMNAQVGLCRPADFGADVCHLNLHKTFCIPHGGGGPGVGPIGVKAHLVPYLPGHSLASGIGGSQGIGAVTSAPWGSASILPISWMYIAMMGGAGLKRATEVAILNANYIAQRLTGRRVIGLRRRAKYILGDLDDATSWLIHLGMSGRMLLSNGGDPVLERHDHVVLRTDKGWWLRFNDARRFGMMDLWPTADVENHRLLSGIGPEPLGNAFSGPALEAALE | Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
EC: 1.4.4.2
Catalytic Activity: (R)-N(6)-lipoyl-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[glycine-cleavage complex H protein] + CO2
Sequence Length: 921
Sequence Mass (Da): 99327
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A0A3L6QHJ2 | MPKALLLLAVVLLAARLGRTQQPNDSLTTGQSLLVGQTLVSAQGIFVLGFFSNGDSTYLGIWYNNMKTRTVVWVANRDTPIKGGNGSLTLSTSSLDLLDRRGNNVWSSSSRFSTNSPQAFLLDSGNLVINDSMSGTPNPLWQSFADPCDTLLSGMAIGYDTSPTIQYMQLTSWKSVSDPSTGSYSIKLDPRRRPPELLLFNDTTLLYRTGPWNGQGFSGQPYLKTTNKLAFNMTVHDDSAYYSFTSLDSSVQWRFVMSSDGLAIAGIAIRAKMIGLNTGTCPRISVIPMRSVEFVPRSPNDWTQRNFTGGCVRNAALSCSSANGFNRLQHVKVPDTLNATMVGGKSLDDCKELCLKNCSCSAYALLGESNCVVWSGDLVDVVLFVDGINDLYTRVSHNNPSRPGPNVAIVVSISVVGVLLAVSAMLGFCYHRSRQKHLPLALEQDHAPGPKLAAKNLDLDAIRVATNNFANQNCIVSTRSRTIFKGTLPNFGDLAVKRLNTEAGLEDLKNEVKMLAKLDHPNIIRMLGSCTGNNENVICYEYMPGGSLDAVLFAEDEKSAVLDWPSRLHIMQGICEGLLYLHEHFRIIHRDIDPSNILLTEGLVPKISDFGLATMLDQGQSEGKDQNFRGTRRYSAPELFYGKSYSMKSDVYSFGIVLLEIVTGCKAASFCREDTDDLPTYVRQRWTHGTAYQLKDPRMGDAAPRGEIERCIHIGVRCVQDYPTMRPLMSYIRNTLAAIHP | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.7.11.1
Subcellular Location: Membrane
Sequence Length: 741
Sequence Mass (Da): 81533
Location Topology: Single-pass type I membrane protein
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G8QHT9 | MSDESRLQAPQRFPFPKRYRLTKTDEFSSVFGFRRAIKGPYFLLHWRLCSPEEARQGARLGLVVGKKLCRASVGRNRVKRLAREAFRLQRQDFPAVDLILRLGVSLDKAKPRPSKAEMAAEIAGLLRRLSRRLAEPRDAGNPPPAANPAAPEPR | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 154
Sequence Mass (Da): 17428
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A0A3R9XSC0 | MTKILISISNFYQDVSTILLDSSKKVLKKNNLDYEQVIVPGAFELPSSINMGLETFEYSGVVALGCVIKGETSHYDIVTHECARAIQDISIYYSIPLGFGVLTVDNKQQALDRAAKYAANAANACIQMIKVKEQFMIYNDKRNSRFN | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
Function: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
EC: 2.5.1.78
Catalytic Activity: (2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2 H2O + phosphate
Sequence Length: 147
Sequence Mass (Da): 16440
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A0A136JSK7 | MIYFDNVSKLYDDGRSAALQRVTFQVAPKEFVSIVGHSGAGKTTLLKMIIAEDKPTEGQVFFESIDIHSIPRTKLPHYRRKIGTVFQDFKLLPNKTAYENIAFAMEANGRSDEEIAENVPQALALVDLDDKAWNFPNELSGGEKQRVAIARAIVNQPDIIVADEPTGNLDPIATYEVVQILRKINDLGTTVIMTTHNKGVIDELGRRVITMNEGQIVRDDSTGKYVL | Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular Location: Cell membrane
Sequence Length: 227
Sequence Mass (Da): 25274
Location Topology: Peripheral membrane protein
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A0A8J3ELB7 | MKKLLTSSKGLTLVELLSSFTILSIITIIIMNYLLGGMNSYEKTSKDVSLHNDANYVMSAFVRHIYEGTEVEIEESTSDSILIKVTNLSGEETILGFKNHQAYIKSGPNESKSLSHYQFPCCGNDASNITVKNDTVIIKMMIEDQKSETSLELKNEVSFRKPAEEMD | Function: Required for transformation and DNA binding.
Subcellular Location: Cell membrane
Sequence Length: 167
Sequence Mass (Da): 18682
Location Topology: Single-pass membrane protein
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R7LXJ1 | MKEIKNVLVCGIGAVGSIYANKINEYNSEYLRVLVDEARLEKYKKNPKIFNGKPLNFNYILPSDETFKADLIIIATKFDGLKDTIKNIENFVKDDTIILSLLNGVTSEDMIAQKYGWKHILLSYFIGHSAMRDGNIITHDGIGDVVFGVKHGVGTDLYDVKLLKQYFDNVGLTYKTPDDMERALWLKYMLNVSSNQSSAILGMTFGQMQTNKKFMEFLINVMKEVQTIAKAEGVKNTETMIDEALVSFNKMIPDGKTSMLQDVEAKRKTEVEMFGSTMVKFGKKHNIPTPYNLVMRDMLEIIHENYQG | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantoate from 3-methyl-2-oxobutanoate: step 2/2.
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
EC: 1.1.1.169
Catalytic Activity: (R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH
Sequence Length: 308
Sequence Mass (Da): 35003
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A0A518HAY2 | MRDRLTRPSPLAAVALLVAAALGAAQAGGESKPDDPFATARDRMVRRHLAERGIEDPAVLEAFRTVPRHKFVPESYQRLSYEDESIPIGEGQTITTPYEVAFMTEVLEPKPTDRVYEVGTGSGFQAAILGQIVDEVYSIEIHEPLAKRAAEVIKELGYENIHSRPGDGYLGWPEAAPFDKIIVTCAPEAIPPPLVEQLKEGGRLVIPIGSRFDQKVYVFDKKGGKLEGGAVRPTLFVPMTGKAQREAAERRARGEDEPEPRDP | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-methionine = [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-homocysteine
EC: 2.1.1.77
Subcellular Location: Cytoplasm
Sequence Length: 263
Sequence Mass (Da): 28866
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A0A517P9P6 | MPLFGSHLSVAGGFHNAADRAGELKLAAVQIFTKSNHQWAAKPLTEELTTRWTAAHAAAGLRFACSHASYLINFATPDPELREKSVAAMAIELERADALGLAGVVVHPGSHVKSGEDVGLAAAAAAIADVLERAAGGTCGLWLENTAGQGTNLGWNLSHLGAIVDAVPERLRGRLGVCFDTCHAFAAGYDLRDDAGYERAFEELDAAVGLDRLACLHVNDSKGGLGSRLDRHEHIGEGEIGDAGFRRLMTDPRWDDTAFILETPKKDRDGVPWDTLNVKRLQSLTR | Cofactor: Binds 3 Zn(2+) ions.
Function: Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
EC: 3.1.21.2
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
Sequence Length: 286
Sequence Mass (Da): 30595
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A0A3N5EKH7 | NLMVTQQSLVEAGIPLVHIERGGDVTYHGRGQLVLYPIIHLRQARLSVTEYVFRLEELMLQVALDWGVDAGRDCRNHGIWVHGRKLGSVGIAIRHGVAFHGLALNVNISLTPFSWINPCGLTGIQMTSLSRECGTEISLAQVTPLLLCHLAEIFLRDFSAIDIQDLSPAGVA | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
EC: 2.3.1.181
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Length: 172
Sequence Mass (Da): 18858
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U1HMU9 | MASGFTGPLISTVESSQHVHSHSRSQSHQCSSQRSARPFTLPRIPSERFDPGSINYDGRPPGHESRQKHGENGIINHVSFAANGSISAPSHQTNGRLTRLSKQEKAAAQDHQPEVTSLPHSYKLPRVEGKAQISAGGMDPNSRPRSYLRRVFFSSIVPLPYILLSYFNPRHTERFSTTTNSNLRESSISQISNDILISLMLTSCILLLLGTFEKCRGYNSPSYNAKPGLSVAGDTKKASTIGLDLWTVLRILRRAVGIAIPYIAALQLGGLAVSVLVLVSISSGLVPRNKEHFNLSHVHGWKNLLAQKTWTLAFSIFLCVTAIHYGSSSGLSATAGVLAVIVFTFFCSPPYLVEAPHESSLTSPPNSANFTPAVPFTPWNVAEPSYHLSVKIKTSPLIATAEETSLTLLSGALTAGAAGILYLFSEFSALTVESFAILLVVAMLTMWSLVTMETSMFQEALVPLATGLAAAILGNAMTLSKFDTLWQDAILGAMAYMAVQLDATRPQASLHTHPMSSEKHMQRRDRNISAPTKVLLQSTKRYSLLHGILADKDSRRIFYFMLLNLSFMLVQSTYGVLTGSLGLISDSIHMFFDCFALLVGLCAAVMSKWPPSVKYPYGYGKMDTLAGFGNGIFLMLISIEIIWEAIERLVEGSDVSRTMELLIVSSLGLGVNLVGIMAFEHGHAHGHGGHDHSHGGHSHSHASHAHDHSAPLALPAPSAAKSEQAHHHGGDNMYGIYLHIMADALGSVAVVISTLCVRYFGWSGFDPLASCAIAILIFASAVPLVFSSGKKLLLSLPSDVEYTLRDVLAGVSKIRGVVGYSAPKFWLDDIGKRDSEPGHEHHHHHPHENSHNHHHHHHHHHHLNEHQHAFEHSHSHHHDENNDHSHRSEHENQNQTVLGVIHIIASQHADLDDVRARVSDYLQSKHMDIVVQVERDGDIKCWCGGGQKAG | Function: Functions as a zinc transporter.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 950
Sequence Mass (Da): 103788
Location Topology: Multi-pass membrane protein
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C7RK55 | MNIARRQVWRPSLPRTADSTPLLGWLRDRGSLTARIRSRGRFAVRVLRQGLGIPTADEARLLGLDPGVHAWVREVALSCNEQIVVFAHTVLPRRPRGPLTVWLSRLGERSLGALLFAHAGFTRGPMAFHRLDRRHALFTAAWAALQLAEQSPATLWARRSRFGLGGQSVLVSEVFSPRLAQLPEPGKESWTNGKPVL | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
EC: 4.1.3.40
Subcellular Location: Cytoplasm
Sequence Length: 197
Sequence Mass (Da): 21916
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A0A366FJC2 | MTRMLATVTDVAEADEAVRLGADIIGLSAAGAMAAVDPALARAVVARVAGRRETRASLGEPPDEGGALAERAHALGAAGVDALELALDGRSLERLAGVLAPLAKQRRLVGVLIADAAPDFDLLAKLAALGFPGAMLDTRAGSAGRLLDHLDIARLDAFCARCRALGLASGLAGALEAPDTPRLLLVEPDVLGFRGALRRGPDRTGRLDPQRFALIRDLIPSERPDGDGSPALDRRPPAGETSGHARDSDVDHIYVRDFVVSASVGGYDFERSAPQRVVFDVEAAVRRSSGPADDLRSIFSYDVILDSIRLAVGRGHVQFVETLAEEVAEAVLRRERVQSVRVSVRKIDVIDGSVGIAIRRARSSAAAASRAPGAARPPHGKD | Function: Catalyzes the formation of 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) from two molecules of glyceraldehyde-3-P (GA-3-P).
EC: 4.2.3.153
Catalytic Activity: 2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + 2 H2O + phosphate
Sequence Length: 382
Sequence Mass (Da): 40098
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A0A4Y7I8W5 | MADVVRKFFTASMLMWIVPILILYGFNNNLFPGASQLSSHSLTILSGLIAVISVNIVIAFYIYMAMKEPSNKHEPDPTFLAEAKASIKQQHSSSETEDPSQAREKHD | Function: Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 107
Sequence Mass (Da): 11927
Location Topology: Multi-pass membrane protein
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A0A192B2E3 | MGARASVLSGGKFVAWEKIRLRPGGKKKYRLKHLVWASRELERFALNPGLLETAEGCQQIMEQLQSTLRTGSEELKSLFNTIVTLWCVHQRIDIKDTKEALDKLEEMQNKSKQKTQQAAAATGSSSQNYPIVQNAQGQMTHQPMSPRTLNAWVKAIEEKAFSPEVIPMFTALSEGATPQDLNMMLNIVGGHQAAMQMLKDTINDEAADWDRAHPVHAGPIPPGQMREPRGSDIAGTTSTLQEQIGWMTSNPPIPVGEIYKRWIVLGLNKIVRMYSPVSILDIRQGPKEPFRDYVDRFFKTLRAEQATQEVKNWMTETLLVQNANPDCKSILRALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVQQSKVMMQRGNFRGQRTIKCFNCGKEGHLARNCKAP | PTM: Specific enzymatic cleavages by the viral protease yield mature proteins.
Subcellular Location: Virion membrane
Sequence Length: 403
Sequence Mass (Da): 44921
Location Topology: Lipid-anchor
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A0A433V6S3 | MKILIVEDDGFVSEALAAILRNQNYVVEVANNGLSGWELIENFDYDLLLLDVMLPKLDGISLCRQIRAHGLLVPILLITGRDSSHEKAIGLDAGADDYLVKPFDAEELVARVRALLRRGGVTSQPILEWGKLRLDPTSCEVSYDDQLVPLTPKEYALLELFLRNSRRVFSCGMILEHLWSYEDTPGEEAVRTHIKGLRQKLKEKGASSSLIETVYGIGYRLKSQSESSGSKQKEAYELQVNPVSHSKSESKSQQTALAINKVWQKFKGRVAEQVNILEEASQALVQNALNQELHCQAKKEAHTLAGSLGTFGFPEGSKIARKIERLLKEETISLNNAVQLGALIKALRQEIELEPQHSQYTTDAIPFQEHSLILAVDDDPKILELLQTLLTPWGLRVKTLAEPRAFWETLEAVKPDLLILDVEMPGVSGIELCSSVRNHSDWSELPILFLTVHNDADIVNQVFSVGADDFVSKPFVGPELVTRIINRLERIKLVRRMAQQENQRLALFLEAAEIGIWDWNVLINQISWSETHERLFGMTPGSFDGTFDTFINCVLKSDRESLHSKINQVRSEHTKYHHEFRIVWQDGSIHWIEARGQFYYNDAGEAMRMLGTVTDISTRKKIEADLRKSKDELERKVAERARELIRVNEHLLELNERYSRAASFTS | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Cell inner membrane
Sequence Length: 666
Sequence Mass (Da): 75466
Location Topology: Multi-pass membrane protein
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A0A6B9SHB1 | MQSLVILAIVALVVALIIAIVVWTIVFIECRKLRRQRKIDWLIERIRERAEDSGNESEGDTEELMEMGHDAPGVIDDX | PTM: Phosphorylated by host CK2. This phosphorylation is necessary for interaction with human BTRC and degradation of CD4.
Function: Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Ion channel activity has also been suggested, however, formation of cation-selective channel has been reconstituted ex-vivo in lipid bilayers. It is thus unsure that this activity plays a role in vivo.
Subcellular Location: Host membrane
Sequence Length: 78
Domain: The N-terminal and transmembrane domains are required for proper virion budding, whereas the cytoplasmic domain is required for CD4 degradation. The cytoplasmic domain is composed of 2 amphipathic alpha helix.
Sequence Mass (Da): 8901
Location Topology: Single-pass type I membrane protein
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A0A9D9DUJ5 | MEHKIVKIKDKEFKPYIEAKDIDRIICQLAERLNRDYAGKKPLLVAILNGAFIFAADLVKKLDFPCRISLIKVSSYSGVESTHNVCELIGLQESIKDEDVIIVEDIVDTGVTMEHLLARMKKEQPKSLAICSLLFKPDKFTKDYKIDYIGKSIPNQFVVGYGFDYDGFGRNLPDIYQLNE | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 180
Sequence Mass (Da): 20537
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A0A3N5EY98 | GSRKKEISTLLPLFLDAAENIQKESSEKLIFLLPLASTLEEKDLWQNGLKKGGTGLDIRIIRDDRYDVMAACEVVIAASGTVTLELALLDVPMVVSYKFSPLTYQLGRMLVKLKYFSLVNLIAGEEVVPELLQDEVRPENIARNILEILHNPERSERMRKGLLDVREQLGKKGASDRAAQLALNMLC | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
EC: 2.4.1.182
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Length: 187
Sequence Mass (Da): 20920
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A0A3L6TT32 | MALPLRRALLAVLLLRVASEERRPPPATATAQGASTPPASPTSRGTPAPKAKERRLEKSMVVDRESGKSVESEARTSSGVFLTKTQDEVVARIEERIAAWTFVPPENGEPIQVLRYKNGEKYEPHFDFFNDKQNQLIGGQRIATVLMYLSHVKMAGETIFPDSEDQLTQEKDGTWSECATLGYAVKPVKGDALLFFSLHPNATTDTKILHGSCPVVEGEKWSATKWIHVRSLSSGFPKARTGGCQDEDDMCPRWAAAGECAKNPEYMVDWWVPEPRLVPAGRALMCVECSCKLLNSMAVVMIKIKKSRCSSTQIICPFHHIYLGL | Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 325
Sequence Mass (Da): 35973
Location Topology: Single-pass type II membrane protein
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A0A2N6C7K4 | MRMLICGGGTGGHLFPGIAVAEEVLDSVPRSEVLYVATERETDAKVLRDKPFPFVVLKSEGIKGKTVRQKLGALLRMPASLWDAWRIISRFRPDVVLGVGGYVTGPPLLAAWLRRIPTCIHEQNSVPGLANRLLGRLVKRIFVSFPGSEQRFPARKCFFTGNPVRKEVRALSGGEKIGDNFTLVVMGGSLGAHSINTMMMEAAQIMRTTVPAGFVVIHQTGRQDSKSVRQAYKEAGIPARVASFFSQMPFVLAKADLVVGRAGATSLAELTVMGKPMILIPYPHAADNHQEINADWLVEAGAAIKCREDETSGAELAALIVELADNDRKRREMADRAHRLGEPAAAKKIVRHCLDLCGDNAIM | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Catalytic Activity: di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans-octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + H(+) + UDP
EC: 2.4.1.227
Subcellular Location: Cell membrane
Sequence Length: 363
Sequence Mass (Da): 39529
Location Topology: Peripheral membrane protein
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A0A932P4X2 | MTEMSNPDSSIAFQGEPGAYSHLACRNAYPGMQPLPCPTFEDTFAAVREGRARYAMIPIDNSVAGRVADVHHLMPYAGLHIIAEHFERISHHLLAVPGASLQTIKTVKSHVHALGQCRNLIRELGLRVIVGTDTAGAAAELAQRQDKTMAAIASELAAEAYGLVSLKAGIEDAEHNTTRFVVLAREALEPNRGEFSATQFYADVEGHPTQRGLRQALEELDFFSHEVRILGVYPRHPFRMKQQAGGE | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
EC: 4.2.1.51
Catalytic Activity: H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O
Sequence Length: 247
Sequence Mass (Da): 27050
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A0A525CTR7 | MRNYEVFIVKTVKLTITTDLVLIDAISDYLVGVWDAAVEFEVESKEQHRVLSAIVEVADEMQYTALRDKLETVVIELAQIFTVTPPTIGSQELTEKDWSTQWRSRFKPLHLLDNLVIVPSWEDYQPKTGEHVIEMDPGMAFGTGQHETTQMCMALIRLVQQRSTTHSMLDVGTGTGILAMGAACLGMKSVVGIDHDPEAVSAAQQNVINNSLVDLVSISPAVIDQVRGQFDLVVANIVHDVLLDLAEQLSEKTGTDGHLILSGLIEGSQVRSITATIESKGFQMVEKSTKGEWASLLFVKP | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
EC: 2.1.1.-
Subcellular Location: Cytoplasm
Sequence Length: 301
Sequence Mass (Da): 33133
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A0A849WF38 | MEQRKYGFTVTQEYAGYSLCDYLVHQMIHFSQQTLKKMIHSKLVLVNGENVGAFTRLLAGDEVKIEIPLDQKETYEPCPPLEILFENAQFLVVNKPAGLAVVQERWKHDNFFKEAILQHYQKTKQEDCLPLAVHRIDKETSGAVLVAKNKQMESYLCGLFEEHKIQKEYLALVAGIPENKGRIELKIVQASDKSSKMIVSESGKEAITNYELLETFGDFSLLKVTPETGRTHQIRVHLASQGYPLAIDSLYGYRNAIKLSEIKPSYKPKDTNLERPILSRLTLHAHRISFQLPDEQPFSIEAPIPEDLELLIKMLRKYRPQQSSIFSEGKKRAR | Function: Responsible for synthesis of pseudouridine from uracil.
EC: 5.4.99.-
Catalytic Activity: a uridine in RNA = a pseudouridine in RNA
Sequence Length: 334
Sequence Mass (Da): 38302
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A0A2S6TDJ1 | MNEFEIIKTYFYPLAKKFPGALSLLDDAALLDIDPDHQMVITNDILTAGVHFFENDPADLVARKSIRVNLSDLAAMGAEPLVYLLALSLPNTVDDAWLELFSNGLKRDQINYGISLIGGDTSSTPGPTSISITMLGRIRVNKALKKSNAKLGDDIWVSGNIGDAGVALKIIKGEVNVIDDKSKNYLFKRLHLPEPRLELGNNLIEIANSATDISDGLANDLNNICQASGFGAVVQGDSIPISELVSTLIKQTKHLKMSHIISGGDDYELVFTAPPEYTKNINTLSKKMGLKISKIGSIVEGKTIRIIDKIGHDLPLETEGYQHF | 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: 324
Sequence Mass (Da): 35285
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A0A357ZHE1 | MRRFFVDQFAIDGDEVLLNAAESHHLTRVLRLVKGDGVELFDGDGAVYDGVIVETGAVGQGRARVRILSRRHEETATKPLVIAQAMLRGGKIDELLQRYTELGVDTFVPLWTSRCQGKFDLIKEEKRQARQLRIIEAACKQSGRARPLRLARPQNFADFLANSAEERSGWRRLMFWEEEETTSLRDISFAGAGAIVAVIGPTGGLTPEEAVMARAHGFYTVRLAGHILRAETAGXA | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 236
Sequence Mass (Da): 26172
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A0A524HLQ3 | MIKETIENPGLTIHCCGLADYRSILQLQTELHEKRLLDSICNTVLVLEHPDVITFGARQSINLLKVERDALTQKNIDLVETRRGGGVTAHNPGQMVFYPILRLTDFGIGPAEYVRKLEMIGQELLMLFGVKTEIRGGLPGLWAGDRKIASIGVRVSKGVTYHGMAININNDLGIFDLIVPCGLKEVQVTSVLKETAENIPMQLVKEKLIKLLIKCFSHHAEPHRKENRKLPSWLVRPLPSGSIYNKTEEILNRLGLDTICNSANCPNRGQCWSRGTETVLILGRICTRNCGFCSVTSGKPLPPDPNEPANIAEMVKELGLK | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
EC: 2.3.1.181
Subcellular Location: Cytoplasm
Sequence Length: 321
Sequence Mass (Da): 35620
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A0A6G8PWC8 | MKAELATDVGPLRLKNPVMPASGTYDWFGRDPEQVSADSFGAVVTKSVTLRPQAGNPPIRVAETPSGMLNAIGIPSVGIEEFLEEVLPQYHALDPPVIVSVQAYSPRECESMLARLSEQPRVDAVELNLSCPNLAHGTITAQSARLSAEMVAAARGATRLPIVAKLSPNVTDIAEIARAVEEVGADALCLINTVKGMAVDVETRQALLGNRSGGLSGPAIKPIALSMVWECYQEVDIPIVGVGGIATAEDALQFLLAGARAVQVGTATFREPRSLARIIAGIEEHLAQDGLHSVGELVGWCHKGRLTVGS | Cofactor: Binds 1 FMN per subunit.
Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
Function: Catalyzes the conversion of dihydroorotate to orotate.
EC: 1.3.-.-
Subcellular Location: Cytoplasm
Catalytic Activity: (S)-dihydroorotate + A = AH2 + orotate
Sequence Length: 310
Sequence Mass (Da): 32652
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A0A1R1LAG4 | MAVTESQPQPGATPTGDYDFIVVSNRLSVDRVVVDGESDWRRSPGGLVTALAPVMAQADGAWVGWNGAVDEPLDEFDHSGMHLVPVDLSQQEVELYYEGFANATLWPLYHDVIAPPEFHRTWWDAYRRVNRRFAEASAKAAAEGATVWVQDYQLQLVPAMLRQLRPDLRIGFFNHIPFPPLEIYAQLPWRQQVLEGLVGADLIGFQRPGDAQNFTRCVRRFLGTASRQGIFTVTDEDGSERRVEARSFPIAIDAQHIAELAADPDVIERARQIRHELGDPTTVLLGVDRLDYTKGIPHRLKAFGELLEDQRVSVEDCTLVQVASPSRERVEHYKTLREEVESTVGRINGTFDTLEKTAIRYLHQSYPVEEMVALYLAADVLLVTALRDGMNLVAKEYVAARTRNSGVLVLSEFTGAAEQLRQALLVNTHDIDGVKNAIVRAIHMEPREAARRMRAMRKQVLDHDVQRWSTDFLSALQEQR | 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: 480
Sequence Mass (Da): 54113
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A0A0E4C8W7 | MRFWLTTITVLLLDRASKLWIMSHMNPGSSWDLINGILSITYIFNPGAAFGIMQGKAGLFVAAAALVITFALYFMYKYNPAQRIQYALALIVGGALGNVIDRILYNAVVDFISVGWFPIFNVADIAIVCGGALLLIYILLNGDEPSR | 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: 147
Sequence Mass (Da): 16137
Location Topology: Multi-pass membrane protein
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A0A653TL81 | MSTEDTTVDRSDQDTDGPSGSRQGLGRWLLGLLVTTVLLALLVKTFLLQAFYIPSTSMEPGLEVGDRILVQKVSTWVGSPDRGDVVVFEDPGGWLGAQGEPEGNALTSTLGAVGLYPEGGHLVKRVVGVEGDVIECCDDGRLTINGSDPLEETAYVDVEGLTCLGPMTGNCDWTAGPVPEGEIFVMGDNRDASGDSTTHLCTEMETDCTDDPFVEEDLVVGTVLATVWPFDRFGLQGGSASSFDDVPDPVTAP | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 253
Sequence Mass (Da): 26732
Location Topology: Single-pass type II membrane protein
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A0A429XKU8 | MDFLKKLGIYKLVLFSLSTLAVLIALVYFVISLSKPIYSPLYNDLTQQDQNIVTLKLQSMGINYQVGAKNSQILVPADKVLSLRMYFAQKGLITSGNLVGYEIFDKENGLSSSQFLNNVNALRALEGELSRTINSLSQVENSRVHLVLPKKELFSKSSVTPSASIMLKLKVGESISKNEIKAITNLVEKAVPDLSSDNISIIDSIGSSLKAPGSEDNGLFNDNNSEFKSFEYQNLVEKKLKSKIENLLESRVGIGKVKVNVAAKINTNRQVMVSEVFDPDGQVIRSKKVSEEKEDDENDGDGISVANNIPNSNQQLNNSNSILKKKSKLDDITNYEISKTVTNKIIDEGGVEKLSVGILIDGYYVYDEKSKSNVYEKRSDEELEKLGALVKSAIGYDQNRGDTIEIVNLKFIDNNFEKDIQKANWLDDNLKNLIQMGMIGVIVILVILLIFRPILAKILEANKSGFGEINKFFDFKKFGTNNKYSGEDNMDNKDFSSSALNDYSESGGKKYL | Function: The M ring may be actively involved in energy transduction.
Subcellular Location: Bacterial flagellum basal body
Sequence Length: 512
Sequence Mass (Da): 56953
Location Topology: Multi-pass membrane protein
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A0A5C8PAD5 | MADLRSPVARVRGLGSARDGTHHWWLQRVTAVALVPLVIWFAVSLLRFAPEGQAAVRAWIASPVTMVMLILAIAVGLWHAALGVQVVVEDYVHAKGWRIGLDMAMKFIAVIGSLAAIVAIFRIAFGG | Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 127
Sequence Mass (Da): 13709
Location Topology: Multi-pass membrane protein
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A0A849WE51 | MAILGIDYGRKRIGLAICGALKIATPLETLERENTEKDFKKLKEIIEEHEIEKIVVGCPKNMDNSMGEMAKEAQSFSDILKNRFSLPTVLWDERLTSAQAERSMIEAGLSRNKRKKSSDSVAAALMLQSYSDRNG | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 135
Sequence Mass (Da): 15120
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E4TGD4 | MYFPLEAQTLILQYADKVGYEIVPSTEALGRIAYEKVYSNRKLPPRDNSAMDGYVIRWEDYENGIREFRVNGVIKAGDDVSGYHVGKGECYKIMTGGFIPSGGDSVAEIEITDEGAYKVQIDGKMKYGNHVRKAGEDVDLGDEIDIEGKEITPFILSRLLSAGITYIKVSRRLRVGIFSTGGELTFPTDAAYPEKIIDSNGFFARGFLKNFGVDVEYLGIFKDDNEDLKNFLEGIDKKYDILVSSAGISSGDYDVVGNVADELGIKWLIRGIKQKPGKPFSFGFINELPFFALPGNPVSSTFCVFFYLVPFIKKMYGVKDVLPKSVDAYLKGRMKKRNDRVHFNRVLLRYEDGRFVAYPFDSQDSHMIGSIAESNGFCMIPSEMVGEIEEGVLLKVYPYDFKTII | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Function: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP.
EC: 2.10.1.1
Catalytic Activity: adenylyl-molybdopterin + H(+) + molybdate = AMP + H2O + Mo-molybdopterin
Sequence Length: 405
Sequence Mass (Da): 45427
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A0A366F983 | MSETLSVAAPDGSISEAVVYADFASLIAGAADTIAAAAAEAIAARGRFTIALSGGNTPRPVYQRLASATIDWPHVHVFFGDERCVSPRDARSNYHMAKVALLDRVPVPSEHVYRLRGEDPPEAAADAYAAELRRALGEDGRLDLVLLGLGHDAHTASLFPGLAAATETRRTVMASYVEFVGMWRLSLTPAAINAARRVLFVVTGEDKAEILRRVLKGPREPVVLPAQAIHPKERPATWLLDRQAAAKLK | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3.
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
EC: 3.1.1.31
Catalytic Activity: 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+)
Sequence Length: 249
Sequence Mass (Da): 26764
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A0A9E0QI39 | WFLKDPKCAVVQTPHHFFSPDPFRRNLGMKDGEPAEDMLFHGLLQDGNDFWNATFFCGSCAVIKRGPLLEVGGIAVETVTEDAHTALKLHRLGYNTAFINKPQAAGLATESIAGHVGQRIRWARGMIQIFRTDNPLRGPGLTWAQRLCYTSSMLHFLYGIPRLIFLLAPMAYLFFGLHLIATSAAAILAYILPQLIHANVANSRAQGQHRHSFWSEVYETVLAWYIAVPTTMALINPKLGKFNVTSKGSLVDSSFYDWGIAKPYLLLIVINVAGLFFGIARMLSPEHGEIGTVLLNVFWVLYNLVVLGVAIGASRESMQLRVSPRVNGEMSIVLYRIGDQAIRAKSLDYSMTGLGVILPDGIELNDGEHIRVLLPSDEDEMAFNAQVMWRAGRRVGLRFENLTLRDEANLVRCTFARPGAWYASPVVGDNAWQSLTRINKLCWHAYGQLFQLIPAFWRSRRVRHITSAVERP | Catalytic Activity: [(1->4)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->4)-beta-D-glucosyl](n+1) + H(+) + UDP
EC: 2.4.1.12
Subcellular Location: Cell inner membrane
Sequence Length: 472
Sequence Mass (Da): 52864
Location Topology: Multi-pass membrane protein
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A0A2N6BZ67 | MLPEQLVIVGTDTSVGKTMVAALLLDYLRSRRITAGYLKLVSCGGEQADDCLFCRAQSGVAAEAVYHFKLAASPHLAARSQGVNIDIGRLAAALAAKREDDVLVVEGAGGLCVPLTDETLLIDFLADQGLPALLVARSGLGTLNHTLLSVEALQARRIPVLGIIFSDEADYEADAPLVLDNMATVARFTGLAVLGRLRRCADFAQGRACFADIGQALLGK | Pathway: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2.
Function: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Catalytic Activity: (7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate
EC: 6.3.3.3
Subcellular Location: Cytoplasm
Sequence Length: 220
Sequence Mass (Da): 23178
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A0A3R9ZRB8 | MYKFALNSNQMHAIEAPIIRNKDTSLDLMHKAGKEVFDEIFKRFKPCKVLVICGFGNNGGDGYVVANLLHQNSWDVKLLKLGEPKTNSAKYYAKKYKGKIIDINNLNLEETDLIIDAIYGIGLSKEIDVTLKELIHKINNSNLKCISIDIPTGISENTGEILGAALKATLTITFHTKKIGHLLMPGLKHSGEVIVKDIGLSNLENTENYIKINTPEIWKNKLRFPQYEDNKYTRGCLGIIAGEMLGASILSTQAARKSGSGIVKLFIKNNVQFDNKLDAGIVIIKYKDIQQLNDLIIKHKVSSILYGPGTIASSETHNIVKNILKHNKPIVLDAGAIINYKSLKKLTTSNQDVLITPHEGEFKKIFNLSSELKINKVKLAVQLSNCKVLLKGVDTVIGCNDNILLQENGCPYLSTAGTGDVLAGICAGLMSQGLNSYFAASIAVWTLNEAAWKIGYGLVAEEIPQTIPNLLLQFRNPSRKI | Cofactor: Binds 1 potassium ion per subunit.
Function: Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This 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.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Length: 481
Sequence Mass (Da): 53014
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A0A849WC47 | MPKSSRLFAMILCLFFLSTFTLIYAATGSKEAADPLSSTSLIWISVVSLASMGIVFGCGLAIASQIFEVKTDPTVAAINEVLPQINCGACGQPGCAGFAEAVVKGTAQPNGCKPGGAAVANKIGEILGIKVEAAQIPVATVLCTRKHGVKKLKEYHGVQDCRAAVTLGTNIYECAFACLGLGTCSKVCAFDAIQMDSTTNMPVVKEDLCTACGICVKECPVQIIRLTPRDHHVHILCASTEAPKIKAKVHKPGGCIACKKCVKTCPEGAIAVIDNVAVIDYKKCTNCEKCVAVCPTTAIFKIRTVALPSQEGSNQEKLEKTPTL | Cofactor: Binds 3 [4Fe-4S] clusters.
Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
EC: 7.-.-.-
Subcellular Location: Cell membrane
Sequence Length: 324
Sequence Mass (Da): 34041
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A0A0S7XLT5 | MAARIIDGEKIAAQIKEGLRKDVEELAGKGKCPHIAGVMVGENPGVRVYVRSQERACEELGIKYTLDQHPDTMTEEALAGRIQELNGDPEITGIILLMPVPAGINARRIQAQINPDKDVEGMNPQNLGRLIYGTPLLGPCTAVGAVELLKTTGVPIEGAEAVVVGHSEIVGKPIAVLLLGLNATTHICHIFTKDLAYHTKNADILFIAAGKSGAVWQRYWKEKRKYNENPEGEPPALPDLSPLIKADMLKPGVVIIDVAINRIPEALDESGDPVLSEKGRPQMKTTGDVDFEGAKEIASWITPVPGGVGPMTVAMLLKNAVEAAKMAVG | Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Length: 329
Sequence Mass (Da): 35173
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A0A9E0QK91 | MAAWILGVSGGIGSGKTAATDHFQTLGIDVIDADIVAREIVQIGESALADIAEHFGQNVLQADGTLNRAVLREIVFADPAQRKALEAITHPAIRQRLHEQCMAAQSPYAILASPLLWESGQAALTQRSLLIDASEATQLARASQRDGVSEAQIRAIMAAQWTREQRLAAADDVISNEGSVAELQQQINDIHQTYLAWQP | 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: 199
Sequence Mass (Da): 21471
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A0A8J2ZS71 | MIEIEKPRIETVEISDDATFARFVVEPLERGYGTTLGNSLRRMLLSSLPGAAVTSVQIDGALHEFSTIDGVVEDVTQIVLNLKKLALKIYSDETKTLELDVQGEGIVTAADLMYDSDVEVLNPDLHIATLNERGSLHMKITAERGRGYRPAEENKRDDQPIGVIPVDSIFTPVSRVTYQVENTRVGQSTDFDKLTLDITTNGSIRPEEAISLGAKIITEHFNIFVNLTDEAQNAEIMVEKEEDQKEKVMEMTIEELDLSVRSYNCLKRAGINTVQELLT | Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
EC: 2.7.7.6
Catalytic Activity: a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1)
Sequence Length: 279
Domain: The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements.
Sequence Mass (Da): 31085
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F2UTV0 | MILSDKDIREYIDKKSLLIEPLSNDTIRENGVDLKVGDELLRFIYNKEPVDINDKSALEKVYTKEKVEKDFVIFPQERVLIKIDEKIKMPSNLVGLCNVRSTFARLGLAIPPTIVDAGYEGNLTIMMIGGNVPVKISKGTRFLHLVFSTTLSEVQKPYSGNYHQSSGVTGAKI | Pathway: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 1/2.
Function: Catalyzes the deamination of dCTP to dUTP.
EC: 3.5.4.13
Catalytic Activity: dCTP + H(+) + H2O = dUTP + NH4(+)
Sequence Length: 173
Sequence Mass (Da): 19388
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G4T2C8 | MAANPEFMNQPQIGFKLDGEEVFALEGETILQAAKRHGKEIPHLCYSDNLRPDGNCRACVVEIEGERVLAPSCCRKPSEGMNIKAESERAVRSQKMVLELLKSDMPKQSQSPYTLKSELDFWAEKMDVGTPRFKGRSQPQADLSHPAISVNLDACIQCTRCLRACREEQMNDVIGYANRGSHSEIVFDISDPMGASSCVACGECVQACPTGALMPAGNVGLQEADKTVDSTCPYCGVGCLIKYHVKDNKILYTEGRDGYTNHFRLCVKGRYGFNYIHNPLRLTKPLIRREGVPKSTELLDPNDLDKEFREATWEEALDFAANGLKKIRDEKGKKALAGLGSAKGSNEEAYLFQKLVRIGFGSNNVDHCTRLCHASSVVALLECLGSGAVSNPVSDVAQAEVIIIIGSNPTVNHPVGATFMKNAAKRGTKIILMDPNRTAIAKYASHVLQFRPDTDVALLNGIMHTILAENLQNDAYIKQYTEGFDQMRTHLRNYSPEKVAPICGIDAETIKEVARLYATSKGSMILWGMGVSQHIHGTDNARCLIALALMTGQIGRPGTGLHPLRGQNNVQGASDVGLIPMVYPDYESVEDPKFRAKYEKLWNTELDPKRGLTTVEMIHAILDGEVFGMYIEGENPAMSDPNQNHARKALASLEHLVVQDIFLTETAGFADVILPASAFYEKTGTFSNTDRRVQMGRQAVNPPGEAKQDLWIIQEIAKRLGCDWNYQGPEDVFNEMRQAMTSIAGMTWERLENEDSLTYPLENVGDPGQPIIFTDGFPTATGRGRFVPADFIHADELPDNEYPLIFITGRQLEHWHTGSMTRHSPTLDSIEPDPVVSVHPLDLEKLGIEPGGFITVESRRGKLSAYARAELGIQQGTVFMAFCYNEASSNLVTNDALDPAAKIPEFKFCAVKAYAGGTPDQRIN | 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: 1.17.1.9
Catalytic Activity: formate + NAD(+) = CO2 + NADH
Sequence Length: 924
Sequence Mass (Da): 101842
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A0A7T9V2N0 | MRFDFNDFRLRKYSKITKKILALDKEYQQLTDEQLQAKTILFREKLAEGASLESILVEAYATIREADYRILGLKPFENQVLGGVILHYGMVAQMNTGEGKTLTATMPMYLNGLTGPGNFLVTVNGYLANRDAEEIGKVYHWMGLTSAAGVSPDEEELDMQAIYNNDIVYTTNSALGFDYLTDNLVENATDKKLNDLNFALVDEVDSVLLDAAQTPLVISGSPRVQSNLFNSTDRIVKSLQKDKDYEFSEDLTSVWFTKEGIKHLEDYLGITNLVSKRWSDLYRHLVLALQANYTIKRNQDYVVVDDEVLLLDSENGRALTGMKRESGIHQAMEAKEEVPLTEQTRAMASITLQNFFKMFKKLSGMTGTAVTSAREFMDVYNLPVLKVPTHKPNIRVDRPDIVYATMDEKIEATVKLVKKAYEVQRPVLLKTGSLSLSRLYSRVLLKNGIVHNVLNAQSESKEAMIVADAGQAGAITVATSMAGRGTDIKLGPGVKEKGGLLVIGTERMNSRRVDDQLRGRAGRQGDPGESIFLVSLEDKVVIENAPDWVDKYRMRLAQALKEGKRKYGEPLRGRRAKNIVERAQQAADTKAESARKSSVKMDDILRIQREMIYDFRDYVMANGDLGEITQRIWDDFFKLYSSGKGITRDKLSDFIINNLDYNYSDEQFDSKILEDPEQVEQYVLKVAKQKWEDQKLILDNEFKQNYLKRLSILKALDVAWIEQVDNLSQLKTVVSSRSTGQHNPIFEYEKEAMNSFRQMRKAFWQNTIKYMLLSDLIVGKNESIRVEFP | Function: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
Catalytic Activity: ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.
EC: 7.4.2.8
Subcellular Location: Cell membrane
Sequence Length: 789
Sequence Mass (Da): 89618
Location Topology: Peripheral membrane protein
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A0A6N9DZZ8 | MFLYLEEKVTMSPLPPLYVVTDRLRTGEDRCLHVLEDIIPEQGMMIQTREKDLGARELLRFVEAVHQLARPFRVPCLINDRVDLVLATKAAGVHLRADSMPAKEARKLLGNGYLIGKSVHSAKEALQSEQDGVDFVVLGPAYETPSKQQYGPPLGIDVIREAVRHCTIPVYAIGGLTPVRVEHVMAAGAVGVAVISSVFQAASPREAVATYSTQLRKWRPQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole: step 1/1.
Function: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
EC: 2.5.1.3
Catalytic Activity: 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate + 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + 2 H(+) = CO2 + diphosphate + thiamine phosphate
Sequence Length: 221
Sequence Mass (Da): 24378
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A0A0S1SL72 | MKPALLIVGLGNPGSSYESTRHNAGFRALDALHSVFGGGEWRDRPKFQASIAEMMIGTVPVLLVKPKTYMNRSGEAVHKLVDYYKADPTFQLLVLSDDCDLPLGEVRFRSQGGPGTHNGLKSVVENAGEGFPRLRIGLGQAPAGADLAEWVLSVPSAEERTLLDAALRTELPRKVEEFVLGSSQQ | 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: 185
Sequence Mass (Da): 20029
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A0A7W0EN28 | MKEIQDYYFKKAQKEGYPARSVYKLEEANLKYGFLKRGSKVLDIGSYPGSWSIYAAKIVGPQGLVVGVDLQAGKRRAESGRAPIEFVRGDIMADETVVAVTAYAREFQVVLSDMAPQTTGNKWADHQKSLVLCRRALALACQVLAKGGVFYCKVFDGEDCRDFVEEVRGCFGKVKIVKPKSSRPESRELFVFGQGYKGTMISSTI | Function: Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(2552) in 23S rRNA = 2'-O-methyluridine(2552) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.166
Subcellular Location: Cytoplasm
Sequence Length: 205
Sequence Mass (Da): 22758
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S0NS21 | MISKRIIPCLDVRDGRVVKGVNFAGLKDVNDPVTLAKFYNEQGADELVFYDITASAEGRGLFTDILQAVASEVFIPLTVGGGINELKDFERVLNCGADKVSVNSGAIRNPQLIAEGAKRYGSQCVVLSVDIRRVGDAWHVFAKGGREDTGIDALEWIRQGETLGAGELVINSMDTDGVKEGFDLPLLKAITEVSSLPIVASGGAGKVADFTELFQLPNIEAGLAASIFHYGEVKIPDLKAQLAEEKIAVRL | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9.
Function: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
Catalytic Activity: 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + L-glutamine = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate + H(+) + L-glutamate
EC: 4.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 251
Sequence Mass (Da): 26890
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A0A849WEG9 | MQAGFQELGYLTQEIPGIGGVIKSKPDDFQVKEIPLYPASGTGEHLYLYIQKQNITTMDLVYQIARQLRISPNDVGYAGRKDSFAVSWQYLSVPATCESSLSEVKIPGVSILSHQKHTNKLRIGHLAGNHFAILIRNIQENAEKNVKDVLDILQRRGVPNYFGEQRFGLQNNTHEIGKAMLLGNHEKTCDTFFQSNCNLESSAIEQAISFYKQKKYQEAMMVLPASFSTEKHLLKMLASGSGCKKAVERIPWKIQKFYVCAYQSFLYNSTLNSRLACLDKIELGDLAVKHPGSAVFLVEDPSLEQKRCDAFEISPSGPIFGHKMIEPKGRQGEMEKQILQEEGITLDSFESFHLKGERRSYRVSLKDVQYEKTQDGLWISFVLPKGCYATVALREIMKAPAFSIPEDEDLE | Function: Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs.
EC: 5.4.99.27
Catalytic Activity: uridine(13) in tRNA = pseudouridine(13) in tRNA
Sequence Length: 411
Sequence Mass (Da): 46388
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A0A849WJU4 | MLYYFCWELFEKPIEWLQFTSHITVRAALAFFTAFTLGILFGPFVIRRLAKMQFMDATDKSPCELLRENKKKKNTPTMGGVMIFFSFMMSVFLWARLDNHYIWWAILSTFGFALVGFLDDVVKAFSSKNGLSPRGKMALLLIVSTSLSIVLWKTLKDTPELLYLYFPFMPDLKINLAVGGGILFVSFATLVIIGSSNAVNLTDGLDGLAIGCTIIVSATLTIVCYVAGRKDFSSHLNITYIPGAGELAICCFALVGAGLAYLWFNGFPASVFMGDCGSLMLGGFLGYVAVAIRQEILLGIIGGIFVLEAISVIIQVFFYKLTKKRVFRCAPIHHHFVLNGLEESKVVMRFWIIEIFLAIFALSTLKLR | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
EC: 2.7.8.13
Subcellular Location: Cell membrane
Sequence Length: 368
Sequence Mass (Da): 41038
Location Topology: Multi-pass membrane protein
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A0A7J5VPQ5 | MSIPPSIDKPVLALVGPTAIGKTALSLLLAERFNGEIISVDSMQVYRFMDIGTAKVSPEERARIAHHLIDIVDPDTEYDAASFVRDALQVIEDIHHRGKIPLLTGGTGLYLRSLIDGLFSEIGHFPEIRDSLQQRLLADGPQKLHEELLIKDRSSALRISVNDSHRLIRALEIFQGTGKPWSEHIADHQLLKKTQFSNILQVGLTCDRKILYQRIDLRARLMLQSGFEQEVRDLLTRGYGPELKSMQSIGYRHMNNYINNLWDMAEAERVLARDTRHYAKRQYTWFNGITDLQWFDVQDQDLILDKIELWLN | 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: 312
Sequence Mass (Da): 35809
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L0PEA5 | MLKYERYDPVVNKTSKNTRDFVLSKLNEKIKRKHKENQENEEQQCKKKQKKNILNEDNEQKKSCLDALEVEFVSDFQKNDTNKLNVECSSQNNQLIENHNQEAEKVPETTETCNNIFGLFSNTMKVASNSKLPLDDHSIHLSNEFKYQLRSRNYTELFPVQKVTIQLILDNPSSCKEDLFIGAPTGSGKTLAYVIPIIQTCWKYKTLVYFLSLIKYINLNSFAGGQSLVDILICTPGRLVDHIQNTPNFSLQHLKYLVIDEADRLLSQRFQNWIEIVMNEIEKPKSYKDSNYKLATDLPDAVNDPLKLIFHDDFVVEKKSYITQKLIFSATLTCNPEKVISLRLRNPRLILIEESKSSLSKYFSENKVSIRNDDICKFFVPSALNEYAVLIESDAKPLFICSDIMARGIDLPQISHVINYDIPQTPRQYIHRVGRTARAGKSGQAWTLYQEFEFKKIQKILKNIGREKEVIYEKISATIFTNEYMI | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 486
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): 56328
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A0A849WA08 | MSQEEKAKQETSFRKLHHLEICLKEKVQSHETTKIEDFHLVHRAICDLDFDEIDTSLVLWGKKLQLPLVAAAMTGGHPDVRKINENVAIAAQKYGFAMGVGSQRAALEKNMPYITESFEVVRQLAPDVLLIANLGAAQFGKKWNYREEQIEKAINLIKAQAIAIHVNPGQEVIQIEGDTYFQGFWQRLNGIAEKIKVPIILKEVGSGFSREDAQKVENSPLSGIDIGGLGGTSWIGVETLRLEKETSSLNYEMGNLFWDWGIPTAISLVETRSVTNKTLIATGGIRNGMQAAKMIALGADIAGMALPFLEAAAQGLEELDILVKKFQKELKITMFLTGCKNLEELRSIPVVVSGYSKDWMEQRGIDLSMPWRKKI | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
EC: 5.3.3.2
Subcellular Location: Cytoplasm
Sequence Length: 375
Sequence Mass (Da): 41750
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A0A834GKN4 | MALQLLAPISAKLILVVFLLFCGGISLPLRCSGDGSKEKEKTLAIIKPDGLAGNHTNKIKEIILDSGFSISKEMVVQLDEDLVKRFYVEHSSKSFFPSLLKYMTSGPVLIMVLEKENAVADWRAMIGPTDARKAKITHPYSIRAMCGLDLQRNCVHGSDSPDSAARETSFFFKESSSGGPKDKLSSRGIDLRRIVNYSDDLCVLEEENPQPEFFNWMQTKFNGVQGSTSTAKPSNPVPAPRQPKHEPPKEEFSDWPHGLLAIGTFGNQNTNQTSDQRQQNPQQHQSPSSSDEDELADFTPEEVGKLQKELTKLLRRKPAAPATTKVEGDIQNAADLPLHRFLNCPSSLEVSRRISTAGCSVSGDKDDEDIDRTIRVIIDRCKDVCMEKNRKALAKKSVSFLFKKFVCSSGFGPSPSLRDTFQESRMEKLLRTMLSKKMNPQNCSRASSVKKIFEDRPTPKMIKGKEEEEEKRKKTSDGSKWVKTDSD | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
EC: 2.7.4.6
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Length: 487
Sequence Mass (Da): 54364
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W7DKS7 | MILGLDIGVASVGWGIIDAENGGVVDAGVRLFSSRDASENESRRTSRQSRRLSRRKKHRRERIKELLLAHDMDICDIVNENPYQLRVKGLNEKLEVSEIYVALTHLAKRRGVSYLDDVVEEGGAIKSEHLNKNMEEIKSGKMPCEIQLERFEKYGQVRGMIEINQDTEESSFLVNIFRTSDYIKEAKTILATQQKFHKQITNEFIDEYINIMASKRDYFIGPGNEKSRTDYGVYRTNGDTWDNLFEILIGKCSVFPEETRAARSSYVAQEFNLLNDLNNLKISNLESGKLSASQKHDIVEKVKNSKKFGTKDLLKYIASICECKIEDIVGCRVDKNRKPIMHTFENYRKVHNALNEAGVDLRLSEADYDELMKIMTLNSETLEIKKQCKEKLPHLTEEYLDVCLVLNKKGAFSGWHALSLKAMKLMMPELYGTSKNQMQIIHTLQLGKAYLKPLNQQKYLNSEAILEEIYNPIAARSIRQTIKVTNAILKKYGPLDSVIIEMPRDYQTSEDERKMIEKMQKENEKEKKAALKRAREEYPFPDEAFRNHKELATKLRLWYQQDQFCVYSGRKISVVDLVRNPNQFEIDHIIPQSVSLDDSLNNKVLCFSEENQKKGQQTPFYYHKGKTGNWTYEQYKLFVEKLFDKKKISNKKRELLLFEEDINKWDVRRGFIARNLVDTRYASRVILNSYQQYFGNHEMGTKVKVVRGKFTSQLRKKWKIFKDRNESHSHHAIDALIVAATANLRLWKKNTLGVSDEGKVYDKETGEILPFEKLTASEYNEMMNKEPFFKF | Function: CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). In type II CRISPR systems correct processing of pre-crRNA requires a trans-encoded small RNA (tracrRNA), endogenous ribonuclease 3 (rnc) and this protein. The tracrRNA serves as a guide for ribonuclease 3-aided processing of pre-crRNA. Subsequently Cas9/crRNA/tracrRNA endonucleolytically cleaves linear or circular dsDNA target complementary to the spacer; Cas9 is inactive in the absence of the 2 guide RNAs (gRNA). Cas9 recognizes the protospacer adjacent motif (PAM) in the CRISPR repeat sequences to help distinguish self versus nonself, as targets within the bacterial CRISPR locus do not have PAMs. PAM recognition is also required for catalytic activity.
EC: 3.1.-.-
Sequence Length: 791
Domain: Has 2 endonuclease domains. The discontinuous RuvC-like domain cleaves the target DNA noncomplementary to crRNA while the HNH nuclease domain cleaves the target DNA complementary to crRNA.
Sequence Mass (Da): 92019
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A0A969K6Q2 | MHRDDFDRCRYPATIELALLFDWYDLARQQAIAADVPLLELDWLVLQLTSLDRLALRLRSTQGSMISACIPLSEFEQRWQQRCCDRVPVQYLAGFTTWRSLELRVTPDVLIPRPETEAIIDLVIEAAGDQLDGHWVDLGTGSGAIAIGLAGELKARQAIATVHASDTSVAALAIARQNAADCGICDRLHFHHGSWFEPFHDSDIRFRALISNPPYIPAATVDQLAPEVRDREPRLALDGGETGFDCLSILIDQAPNWLEHDGIWIVEHEASQGRELRDRLCQRGYREVRTVRDLAGLDRFAIARSPL | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
EC: 2.1.1.297
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-homocysteine
Sequence Length: 307
Sequence Mass (Da): 34497
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A0A286X872 | MGAAPVSGPLWPPCPAMLTLRPGSCSFLSWHRGSWAVAFCSTSADAFDNDLMQSTLKHIVEGRTVEVPTYDFVTHSRLPETTVVYPADVVLFEGILVFYSQDIRDMFHLRLFVDTDSDVRLSRRVLRDVHRGRDLEQILTQYTTFVKPAFEEFCLPTKKYADVIIPRGVDNMVAINLIVQHIQDILNGDLCKRHRGGANGRSHKRTFPEPGGHPGALAAGKRSHLESSSRPH | Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uridine: step 1/1.
EC: 2.7.1.48
Catalytic Activity: ATP + cytidine = ADP + CMP + H(+)
Sequence Length: 232
Sequence Mass (Da): 25966
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A0A834GJU3 | MSPLSSCLARQLFFSFAGRRADLRLRLLLLTTIFMIERLFSFFVFGSPTFYRICMNKTVEEFKPDPYIGAVINCIFWVFYGIITPNSTLVITINSIGLFLELVYLAIFLYFSKQQRRKICLFLLAEVGVTAVIACIALLAIDSQSKRSILVGVFSVVFGLILYSSPLTIMKKVIDTKSVEFMPFWLSVACFSNGLIWAAYALIKVPPTMRIDWYILTANGLGAICAAAQLILYAMYFGSTPKSKTSDDPKKPKGSKPEVQLSEV | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 264
Sequence Mass (Da): 29609
Location Topology: Multi-pass membrane protein
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A0A0C3NWY2 | MGYAFTFPAVTWLTRGAVPTGAYVHYPTISTDMLARVPAESWKMWAKRAYYRLMMYYYALSLSHARFLMVNSSWTRNHIASILSHEHFGPMMCWACRLTPLLAVELALSSRALQTTMLVVGSYPTAGSQGVQTVEPEIVYPPCDMREMVKFRLDNREPTILSVAQFRPEKDHAAQLRAFAQLLMDHPEYKCSPKSKVHLVLLGGARNAGDLARVGELRSLASELDILNHVTFVVNASYPEVLKWLSRGSIGLSTMVDEHFGINIVEFMAAGLIPLVHASGGPLHDIVVPYQSGPTGFHAKAPGEFATAMHEILTLDPVQTTALRERARRWATERFSEEEFVKGWEKSGWRSHIP | Function: Required for N-linked oligosaccharide assembly. Has a role in the last step of the synthesis of the Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide on the cytoplasmic face of the endoplasmic reticulum.
EC: 2.4.1.131
Catalytic Activity: alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP-alpha-D-mannose = alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + 2 GDP + 2 H(+)
Sequence Length: 354
Sequence Mass (Da): 39690
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R7LVZ2 | MIIPAPNDVAFNLLGLPVYWYGVTMALAIFVAMMLANSLFNKVNPDLKKDTIIEFAPYIIIVGILGARLYFCILNAQYYFTHPLEILDIREGGLSIHGAILGGVLSMIAIAKRIKIPVMSLVDAISCTTILGQSIGRWGNYFNSEAYGLPVAGQKWGLFVPLSKRISEYSDYSLFHPTFLYESILDFLAFGILLFVYLKFGNKFRGITFFVYLIIYSVIRFFIEQIRIDSALNFGTVPVAELVAGVLFVVGVIGVCVTLFQKSFNK | Pathway: Protein modification; lipoprotein biosynthesis (diacylglyceryl transfer).
Function: Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-cysteinyl-[prolipoprotein] = H(+) + S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[prolipoprotein] + sn-glycerol 1-phosphate
EC: 2.5.1.145
Subcellular Location: Cell membrane
Sequence Length: 266
Sequence Mass (Da): 29675
Location Topology: Multi-pass membrane protein
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