ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A661FP60 | MISFMSKHILTSCLLLVAIITGCTAKKATEQQHLNKENYFIPGLKHGLIQSPINILSAEIEDLNGHEITLNFQDKINAVENLGHTVQLDFAQGSTVSSDGKLYQLKQLHFHTPSEHLIDGMTFPMEMHIVNQVPSVNKEDTPHYLVVAVLFKMGKKNKFISEFLDQVPKEENSKTELQADKVKLSDVVSDFLSTTPSFYHYQGSLTTAPYTESVSWFVLKRIIEASPEQIRAINKIEGDNARHIQGKYGRQID | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 253
Sequence Mass (Da): 28525
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A0A8T7J801 | MRPFSELLADNILDAIDAIGLPTDGRMIALNSYENRVYQIGIEDSQPIVAKFYRPERWSDEQILEEHQFSQELFEAELPVVAPMAIDGETLHHIDGWRIALFERKGGRSPDLGRRDDLQMLGRLMARMHLVAERHTFQHRPVVDIESYFEIPTSRLIAEHIPAHLCPQFETAFDTLRQQFNDKLTQSKWPQSIRLHADAHPGNLLERDGEIHMVDLDDCRSGPAVQDLFLFAGGHDDTESRAAWDAILDGYYEFRDFDYGELQWVEVLRTLRYSHYLGWLASRQADPTFITAFPDYDTEPFWQRWLGLFNEQCLKLS | Function: A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
EC: 2.... |
A0A6L7VSJ7 | MPTQCLLLDIRRVDSIAIRLQHVLYYSNKFKLSHYLKLIVAANGPLLQIVAAFAIVVFFTIYISAGFIAGAKLFESVFNLDYVWAWFLGAFIVMCYTVLGRFLAVSWTETFQALLMMLVLVIVPILAFSVGSPNENLNTTTPPVWDAGVYGILSVIGLLAWGLGYFGQPHILKRFMALKNPDDARSARVIGMSWMVISCLGAVAVAYAGLHLLPRIEDEETILIKLSEILLNPWIAGVVIAAIMAAAMSTVDSQLMVITTSIVNSRWLGDRAALFINRIGVIVVGTIALLLALDPHSKIFGTVSLAWAGNGASIGPCVLF... | Function: Catalyzes the sodium-dependent uptake of extracellular L-proline.
Catalytic Activity: L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out)
Subcellular Location: Cell inner membrane
Sequence Length: 399
Sequence Mass (Da): 43694
Location Topology: Multi-pass membrane protein
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A0A661C2K5 | MVLTTYSKNIYMTEVLDGIKVLVTRPEQQAEALCESIQNLGGTAIRFPVIEITPCRNQQAAKTVLDNIPQYDIGIFISRNAVNWTVKLLAEKTSILDKLTLIAIGTATAKTLEQILSAEVITNSGANSEALLELEALSEKDVRGKKIIIFRGEGGREYLATTLRKRGATVDYVEVYRRDCPQYDKDVVAKLWSSNSPDVVIVTSNKGLENLFSLLNDEQRNILLGKQLLVMGERMLDFSNGFGFTRPPILAEESSDEGILSTIVKWAASK | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A2D6JJB7 | MSDLFAKTMLKRKKLGFIGTGNLAQAIITALVEENSIARENIYITNRTPGKPTKLKKKFPEINYLSNNEELVETCDIVVFAMKPQDLQNAVEPISYVFDKSKLVISLAAGVTIQNLKRLVPEAGDIFRVMANTPARVKRGVFGYCSTNNNSANESYILELFSPLGLVVAAEEGEEFDALTVACSSGTGFVLELLHYWQDWLQDRGYEEEIAKKMAIETFIGAAELAKQAEHLSVEELRDQVTSKKGVTIAGLEKMREFEVEGNLAMSFEKAIQRNRQLAID | Pathway: Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.
Catalytic Activity: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH
EC: 1.5.1.2
Subcellular Location: Cytoplasm... |
A0A661BU70 | MSNPKQNIEEIKLGFYVTPEHECNYLPGKNAQTVFADPDFPMNENIYTTLASHGFRRSGNHIYKPQCQQCHACIAIRLPVTNFTMSRNQKRNWARNKDLKINKLFAEFDDEHFDLYQRYLAARHPDGDMGTSDLKGFISFLTTNWATTVFYEFRKKNKLLAVAVVDELVDGLSAVYTFFDPDESNRSLGRYAVLTEIEMALNRGLQWLYLGYWIADCRKMQYKDEYQPLEYYYQKKWHHKPPQDTD | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-aspartyl-[protein] = H(+) + N-terminal L-leucyl-L-aspartyl-[protein] + ... |
A0A843LYW9 | VTSPKVDKISFTGSIATGLLIASRAGMKKVTLELGGNDPLVVLKDADIDRAVNGVMNGAYLNAGQVCMGVKRIIVDESIADEFTQKLVRETKKIKMGDPMDKNTVLGTLIDEDAARMVEETVNNAVKAGAKILTGGKRDGAFYEATVLDNVTPDMDVVVNETFGPVAPIIKVKSTDEAIKVANDTEYGLQAGVFTENFRDGLRCANEIEAGTVFVNKQSTFRTDNMPFGGFKNSGTGKEGVKYAVEEMTKEKLIGLNLR | Pathway: Cofactor biosynthesis; coenzyme F420 biosynthesis.
EC: 1.2.1.22
Catalytic Activity: (S)-lactaldehyde + H2O + NAD(+) = (S)-lactate + 2 H(+) + NADH
Sequence Length: 259
Sequence Mass (Da): 27832
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A0A661BLD7 | MSGNTIGKLFSVTSFGESHGAAIGCVVDGCPPGLPLSEADLQPDLERRRPGKTRHTSQRREPDTVQTLSGVFEGLTTGAPIGLLVENVDQRPKDYAELRLAFRP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 104
Sequence Mass (Da): 11189
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A0A3M2DEX8 | MAQLKFALFGHPVAHSLSPQIHQQFAKHVGLDLDYQLIDVPSEHFEAVVTAFFANGGRGANVTLPHKQQALALAKGQTRIAAQSGAANTLFVDGDGRLWADNTDAPGFIEDIQQLGWQPQHSVLIWGNGGAARGIVAGLLAAGAQAVTICGRSQAKSEALARCFAAQAVKTIGWDEKNAVTCEWLINATSVSPDFARWLPNTPPSVYYDLNYASRAMSAVQAAKARGIVAHDGLGMLVRQAAFAFERWTQQPLTSEVVEHVVEWLRQLARP | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
EC: 1.1.1.25
Catalytic Activity: NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH
Sequence Length: 271
Sequence Mass (Da): 29245
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A0A6L8CKK0 | MTDALPMTTRLDRMPEWQSLNAHARAVADRRIGVMFRDDPGRFGRFSGEAAGIFLDYSKHNIDSATLELLLALARASDVEGWRERQFRGKRINVAEDRAALHTALRSDGDGGRVHAPGPVREEVAEVLGRIGTLAEAIRSGQWRGHTGKPVRTVVNIGIGGSHLGPALVCRALSRHDRDGPEIRFLSNVDSGHFDEITRDLDPEATLFVLASKTFSTQETLANAESARQWLGLRPGRDPGAENHFIAVTGHHERALAFGIVPENIYPLPDWVGGRFSLWSAIGISIAIGIGMEGFRALLRGARAMDEHFLAAPLERNLPV... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 557
Sequence Mass (Da): 60618
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A0A8T7DZP3 | DLFGGRTLMPLAYYREQLRAGAIDENQLRRALQLACPSDTLTLAARSFSRESLLWHQLTGGFETDDDAVNGNPGDWLDAAAAAASAADVYQERTRARHWEPARDLLTSWLDRRLDTDLTGVLEQRTVNFLQSFLFPDAAALPLPARGEGMFASFRALLAHDELMKRVQRRKNHVPGQLLPASATQAIAASLEALDLAGPAAERYLRRHLVAIKGWASFIKSRAEPDQRDAHATLTDLLAIQLVLERLLWEDLAEHLQLEISCEALLQEAGQETSAPDSEVDTERLARVGMWLGIEPRALREADSNEVGAVLACLHAVDDT... | Function: Part of an energy-coupled inorganic carbon pump.
Subcellular Location: Cell membrane
Sequence Length: 834
Sequence Mass (Da): 91114
Location Topology: Peripheral membrane protein
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A0A8T7JGR7 | MIGAFLWVMEKEGRPVIEHSERQFVRQTGEATVALLSKYMEKSASLALGMANTAESLPLKSDLFKQVFRHSLSESSIAAFVAGGGIWPEPYVFNKKKARSSFFWGRNAQGELEAFDDYNRDDGEGYHQEEWYVPAKFLKPGKVYWSRSYVDPYTLEPMITVSAPIYRNEGFWGVSTVDIQLSSIEQLLEQQASRLGGYAYLLDRSGTFLSFPDDGISKRSVTTASNDQKLQYISIQKAAESTPFLPVITDSLNVLEGMSRSNRELSVQAQALAEGSYQIDLDEAFRIASIMANPLAKRTIGSSFIKQINMENDPILNEPV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 959
Sequence Mass (Da): 107020
Location Topology: Multi-pass membrane protein
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A0A7C1X894 | MNNCFNKIGLIGKYGNPRVAETVHELGMLLQKRGCEIMLEHATGQLLTTRDLPCASLDEIGRNCDLTIIIGGDGTLLAAARTLVEYDIPILGVNLGRLGFLVDISPDDMEERINEILDGEYEEEHRILLNAEVQHKDSPPSESDAFNDVVVHKWEVARMIETETWVNGRFLNSMRSDGLIVSTPTGSTAYALSGGGPIIEPGVNAILIVPICPHSMSYRPIVVSGDSEIEILVKENMHSHAQVTCDGQINLGLVSGDKILIRKKDKYVRLIHPRQHNHFEILRAKMHWGEHS | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A2E4K1X2 | MVFGALEKIIMGNNATNKHSNLISTLRWCLVITIGCLPVFGFAQRLLLDRIIVVVDQDVVLQSELDARLQDIRANAAANNRPLPEQDELQSEVLDALILENLQMQFAERVSIRFDDDTINRVLLNMAENSNMSFDEYVTTLEEAGVYLMTREQVRKQLTIQELQRGMVNSRLAITEQEIDNFLSSEMGREVMAAEFVINHMLVQTSDSDSAENREAKLRYAADLAARIQEGEFFGEVFAEAQRARLFSVNSTQFDWRRADQLPNIFSEIVEDMEIADVEGPIEAGNGYHLIQLAQKRGGTDQVVKQTNLRHIMLMPNEIR... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
E4ZTM2 | MLFNVLFLASTATATCTHGLSMFKRATTEVNSFGFGPMNGPFNWAALAPENEACRTGRNQSPINIDGTIRPATAKPVLNIPAGPVEFENLGTTIEVIVNGTTDIGGTAFRLVQFHMHTPSEHHINSEYYPLEIHMVHQGVADNTQLAVVALMFEVSARRSSSIIRSLSAAVPKIATPGTTTPIAKGIDFSDVISTIRASNVLSYSGSLTTPPCAEGVTFLIVEKPLDISVADFNSIKRVVKFNSRFVQNTLGQDNILEVGARSGSAAPRANRSLPPSSPSVDTGARRNVQKRTPKY | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 296
Sequence Mass (Da): 31753
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A0A2E2HBV1 | MSLFLKNKRGRGASLRKKREPNALQQRLPQFRKALVSVLLLLVIVLAGLNSRTLIEDIAEQRIEYVVIEGELNRVTESDVQAAVFEFINRSMVAIDLIQIKAALESNAWINSARLRRKWPNTLIVNVTEEVPIARWGDNRLLNQEGRIFSPPSEQQLLNLAKLSGPEGSEARVMDQYQVFNQMLYPKNLRIASLSLNSRGAWSMQLSNEVTITVGSINPVARIRRFVRVYDELFGSQIAGIEGFDLRYEDGIAVRPKAQADTSLISMNSTEQ | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 272
Se... |
E7G2J7 | MSLWFLIAILKPTKEKSVLVKPSNGFNALWQEIESSTNACVKCAKCIPSCTIYRIHKDEITSPRGFLDLIAQVKQEGLELDNSLKKIFETCFLCTTCVQVCPLHLPIDAMIERIRHMSANKHGISWHKRAYFYLLKHPKLMDFVFSLCDVLAPCVFKREEDKLKWRFKGSKAWQKRVIFPFTRKSFLQTYKGLITPQNPLDTSTPPRKVGIFIGCLSNYNYTEVGQSLLSLLDKLNISALIPEQFCCGAPAYFTGDLDTAYFLAQKNITSLYSIASEVEAILVPEATCIGMLKKDYLHILESLSDEKDRMSWLEKFKVIE... | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
EC: 1.1.99.14
Catalytic Activity: (R)-lactate + A = AH2 + pyruvate
Sequence Length: 469
Sequence Mass (Da): 53142
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A0A962X582 | MEREAMEFDVVIVGAGPSGLAASIRLMQLAAEQEREITVCVIEKGSEVGAHILSGACIETRALDELLPDWKELGAPLRVEADGDEFVFLTENHAIRLPTPPQMHNEGNYIVSLGEVCR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
EC: 1.5.5.1
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Length: 118
Sequence Mass (Da): 12873
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A0A6L8EKQ2 | MAGQNHNPPEHTEAWRRLAGHRRQAAGLHLRDEFARDPGRAQRFSLGLERIFVDFSKNLITGETLSLLLELADQRGLDKKIRELFSGHEVNPTERRPALHTLLRTPDDGIQDTHVLSDVARQVRQERDRMFGFVRKLRAGEVGGATGRPISRVVNIGIGGSDLGPRLLADALSEFHREGIDIDFVANIDPFDIERVLANADPETTLFIIASKSFTTQETLVNANRAKRWLADNGCNDSGPHFLAVSGNAGAVERFGIVGDRYFRIGDWTGGRYSIWSCIGMSAAISIGEDQFRQFLAGAHALDSHFASAGFSANIPVILG... | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Function: Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
EC: 5.3.1.9
Subcellular Location: Cytoplasm
Sequence Length: 532
Sequence Mass (Da): 58358
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A0A3M1V4S5 | MSKPVRVLVVDDSAFYRKRIRQCLEKSPRIEVVGEAWNGEEASRLNRSLEPDLITMDVVMPVLDGIAAVRRIMRERPVPVVMFSSFTREGARATLDALEAGAVDFVPKVTSDNSEGETAGARLRDKVLGLVRTGDDEAPALAIEKASAPVAPPELLLIGASTGGPMAVQEVLAGLPADFSLPVLVAIHMPAAFTVTYAERLDALIPLRVREAFDGMPLRPGEVVIAPGGRQTLVERRGAALKVRVTEDEGLYRPSVDRLFSSAAKVTGERTLAIVLTGMGSDGTEGARRIHEAGGQVWAQDRDTSVVYGMPQSVVRAGVT... | PTM: Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity.
Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate resi... |
A0A2E0EZF6 | MWFKGCFLLVVIKMNSQLLKIKQNIILYDDTLISEVDENLFDLEFWANHEETQLINKGRGKVLLINCQGLPSVLKHYYRGGLVSNFLSETYLWQGERNARSIKEFMVLQEMFQAGLPVPRPIAARVNRQGIFYTADLITSRIDNSSSMGDLLRENSMSSDLWKNTGSCIASFHMKGFYHHDLNIENILIDSDQNVFLLDFDKALQMDPSNSMAQKNINRLQRSLNKNFSNPSKPFPKAEWEILIEEHSKQLHQD | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Catalyzes the ATP-dependent phosphorylation of the 3-deoxy-D-manno-octulosonic acid (Kdo) residue in Kdo-lipid IV(A) at the 4-OH position.
Catalytic Activity: an alpha-Kdo-(2->6)-lipid IVA + ATP = a 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + A... |
A0A2E5IMS3 | MFNYKKILIVAFEKNKSNTALSEIKEILTENKLDHEIYDESKDNNFYLSFDLVLVIGGDGSMLSAAKLFSELDVPFLGVNLGKVGFMADLGANNLKDDLVPILSGKNLIEDKETIKCSYDGREYTAFNEIVLHTQKSYKLMEFEVEIDKNFVYRKRADGLIISTSNGSTAYSLSAGGPILTPETNAFVITALNPLSLSARPLIVPSKSMVSVSLSKAVDDLESLIIIDGNQEIKIKDSINNFSVTKNNQSFKLLHPKNHDFFKTCRDKLNWSLSKYENSSN | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
EC: 2.7.1.23
Subcellular Loc... |
A0A6L7VME0 | MPSTMSSLPNLLTGLRILLLVPIAWTMWSGHYLPCLIMLIVAGVSDALDGFLARRLDSISRFGELADPIADKLLAFVVVVMMLATGLLPLWLGVIVIAREVVIVSGALAFRSVVKRLDIEPLLISRINTVVQVFVLCTIIAAQTEIAYLAVITSGFVNLVGYYLMAIFAVASGVAYVYGWTVRLQSHLAQLDERTEAADP | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 200
Sequence Mass (Da): 21731
Location Topology: Multi-pass membrane protein
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A0A3D5IUZ6 | MIIIPAIDLKDGKAVRLTKGLMDTAKIYSDEPWQVAKKFEELGSEWLHLVDLNGAFAGKPENLEQIKKIIENTDLKVEIGGGIRDEETIKMYLELGVNRVILGSIAVKNPNFVKEMAKKYPVAVGIDAKDGYVAVEGWAEVSEMKATELAKEFANAG | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho... |
A0A661FAZ7 | MSLSSALFTNGISDALTHYISLDPDAAIWLAPLSGKVVAINLQPFNQLAYLQVHDSGLQLLEAFQGEADTTLTGTPIAFGLMGLSNNPMRSLFSGEIEISGDSHTGRQFQKLFKNLNIDWEEQLSKVTGDVAAHKISNQLKSAQEWAMEATETFNLNTGEYLQEETRDLPSRPEVDCFYEEVDLIRADADRLEARLKLLASKIAN | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Required for ubiquinone (coenzyme Q) biosynthesis. Binds hydrophobic ubiquinone biosynthetic intermediates via its SCP2 domain and is essential for the stability of the Ubi complex. May constitute a docking platform where Ubi enzymes assemble and access... |
A0A351MCL9 | MNVGAGRDRELGAANRRTALTLGAVVLGMFGFGYALVPLYEIICDLTGLNGTTRRLDAATASTALVDGNREVTVQFLGQTNGLPWDFYPLTKVVKVRPGEATPIEFFAHNRGRTAMIGTAVHSVSPSEAARYFVKTDCFCFSEQRLGAGESQVMPVRFVVSSHLPKSVSTMTLAYTFFLKPIASHPGAIQRGLALLNESPIRRLEQILCRRGESAG | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 216
Sequence Mass (Da): 23394
Location Topology: Single-pass type II membrane protein
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A0A2D4PAG2 | FMAHSVNLTVFLETEDANQVLRRSRRAAFMFFEEILQGDLERECLEERCTYEEARETFENTEETDKFWSLYFGGIRCSSSPCLHNGICRDTIRSYTCNCRDDFEGVNCASAKNECRHEIHTGCQQFCYPEFNFYRCSCAQGYQLGEDDKSCIAQDECACGRFQETLTCPLNPAEREFPWQVLLLNSEGKWICGGVLLKTNFVLTTAECAMLSPVSVLVGINQLQGLNQVIPVKESNIHLRYDNTTGENN | Catalytic Activity: Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
EC: 3.4.21.6
Subcellular Location: Secreted
Sequence Length: 249
Sequence Mass (Da): 28455
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A0A6P1MIT3 | MTLPQAMILGIIEGLTEYLPVSSTGHLILAAEAMGLGGFAHDENNELIHGPLGPIMAPNPAVNAFNIVIQIGAILAVTGIYFKRIKEMSLGLIGKNKDGQKLLINLIAAFIPAAVFGLLFEGIIERYLFSPLTVAIALAVGGIAMLATVKLYKRDNKHVRDIHDITIWCALIIGMVQCLAMWPGISRSMATILAGLCVGLSMTAAAEFSFLLALPTLGAATVYKTITQWDALASTVGLDSLITGIFISTIVAAFSVKFLIHHLTRHGLGPFGVYRIALAAGVLYYFAG | 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: 288
Sequence... |
A0A2A4MK19 | MFIRCVACVGMLLLAQGVSASDRISVGVGDASGDIDAYRIGFQRDFKKRWWRDRPWGLSGYWEASANYWVDNDSISALAFSPVFTLSLKRSSSVTPYFEAGIGVALISNSEIERRNLSTAFQFEDRIGVGLRFGGQQKHDINFRFLHYSNADIKMPNDGLDIFMLSYGYAFR | Function: Has lipid A 3-O-deacylase activity. Hydrolyzes the ester bond at the 3 position of lipid A, a bioactive component of lipopolysaccharide (LPS), thereby releasing the primary fatty acyl moiety.
Catalytic Activity: a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxi... |
A0A352K0V1 | MNSLKLGIKCALSALIFSNLVGIANARVIDKIVAVVDSGVVLASDVETRLNDLKTQAESRGNAVEINDELREQVLERLILEQAQVEVAKRRGLQIDDARVNETLLQIAKNRETDLLGLKNAIESEGKSFAVFREQIRRELLINAIRDREVKTRIRISDTELERFMETTGGQVSTAPELLLSQIVVGLPNRPSPEVIQQAEQKAVQIRDALLKGAPFGQMAVRYSDAPEASQGGDLGWRNILELNPSFADALTEAKKNTLVGPIRSPGGFHLIAVRDRRGDQSVVVTEYKARHILIKPDAVRSLEKAEQLAQNVRRELEGG... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A932P1L9 | MTKKAKVATSKGRKALSPKGLWNKKSRFQTIELVEERGGLLLKLNGWPQVHSKEEAKYHENVATMPMMLAQKVDRCVILGGGDGLAARNILRFRDVKKLTQVELDPGVIKLCSEQPDFVRMNEDVFHNPRLELIVGDAIEWFLKAEGPFDVIINDIEVMFTKQPQKMTLERHFQLFEAMADKLAPGGVAVVTVPDDFDDSILQGFFEIYGDYLPYETRQAFMKSKNVFARARVLLATLFPYVMQWTIRFPVLGPHTTFYLSHRPMTRLRRSPNPPAKYIKDDMITRVLK | Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putre... |
A0A7C7Y634 | QFNSEGLLKLPQLVQVKGQKVVIFRGEGGRERLHDRLVALGARVDYVECYQRSLPEQIDTRTITMWRNGEIDVVTLTSNTAADHLLQILSLSDHDLFENSVIATVSTRIEQYCRQLGCTGQILVSAGPGDEALVSRINDWRAQAQRQ | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
Function: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
EC: 4.2.1.75
Catalytic Activity: hydroxymethylbilane = H2O... |
A0A2A4MLA5 | MKHAYFTVSRLGLNLLCASILGFSGAAAVLAADGVIPLDGIVAVVNDDIITITELGAEVQRISQELRRRNTQAPAPDILQKQVLERLVNRRIQLQTAKRANIVVDDKMLNLALTNIASESNLTLSQFRQVLVRDGVSFEQFRENIRDEITLNRFYQRQIDSRVSITEADITAFLETQQAQGNISVEYQLGHILIAIPEDAAAEEVKASRKKAEDIVSRLQGGADFAETAVAESDGSTALDGGNLGWRGANELPTLFTPIVPGMNKGDTSKVIKSTSGFHIVKLLDTRDTDTQIVKQTQARHILVANKDRNKEEALALAQE... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A357IAX5 | MVSAGEASGDMHAALALNALAKHDVSFSSFGMGGPKLQALGTELVLDCRELSVIGIFEVIVQYRKLRRKLETLRDSLRREKPDLLVIVDYPDFNLKLAETANALGVPVLFYISPQVWAWRAHRVHRIGKLVSMMAVIFPFEVPFYRDAGVPVRYVGHPLVDEVGSTLSKAEARAAFSLPNTGAIVGLLPGSRTGEVKRVLPTMLAAYTRVRAQHPETHAILPCAPTLDR | 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-hydrox... |
A0A962W188 | MLQSPDPELLREADRCVKCGLCLPECPTYRLTRDENESPRGRIALIEGLARSQLDPRGRSTTHLDSCLACRRCERVCPSQVRYGGLIQRAYVDFAVRTPRPLDSMLADPRVLRLAGRMARTLPAALSRPFAKLHRMQRVARALGDGGIAPTPGEYTCRATSPRGRVGLFLGCATAAYQGRALGAAVTLLTHAGFDTVVATGQRCCGALELHAGNPAAAARRADVNRIAFDAALDAVVSVASGCGIHLDAYDPPLPARHFDILRFLLERGGLTTHDFLPLRAAVLLHTPCSMENVYRGGDWAPALLGLIDGLEVVALGERG... | Cofactor: Binds 2 [4Fe-4S] clusters.
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate.
EC: 1.1.99.14
Catalytic Activity: (R)-lactate + A = AH2 + pyruvate
Sequence Length: 402
Sequence Mass (Da): 43316
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A0A2E6A225 | MTYVKICGLRNPADAEFAARIGADAIGLALHPASARRVSAVQAREIADSVRGDVEIVTFVVNRDEAFVRRVLEMVRPDVLQFHGSEPEVFCASFGHRYWKAIHVEDVDTLTQAALTYVSADALLAEAPTQSHGGSGKTFDWSLIPRERNARLLLAGGLSPXNVAEAIXTVAPWGVDVSSGVEVTRGVKSRELIAAFLEAVRGA | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 203
Sequence Mass (Da): 21846
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A0A8T6J4J1 | MAAGESKLKILIVTADYYEELGELLETGARERFLEAGVAEDRIVLRRVPGCWELPLEVRRLV | Pathway: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2.
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 + phosphat... |
A0A352KRE3 | MSVTAWDKDPRWQRAQTSEVRVPGRRWPWRRENRRIAPTVQVWKHWLLLISKLFLIGLVAAGLIWSHLMLKDPKIFPIELVRIEGDWRYLEPDQIRESLQPQLAVSFFSLDVRQIHQTLQRIPWVDSVSIKRRWPGRVEIQVQERAPVAIWQNAKLLDTELKVFTPNQIPQGLRLPKLNGPSSQSEAMYILLQEFNRQLSPLNLTIDQLIMDDRHSLELWLDNGVHIKLGAESVRKRFYNFIRIYPHLNAEEETIIDSIDMRYPNGMAVQRSSRLMPEVGDGAVIRSSE | Function: Essential cell division protein. May link together the upstream cell division proteins, which are predominantly cytoplasmic, with the downstream cell division proteins, which are predominantly periplasmic. May control correct divisome assembly.
Subcellular Location: Cell inner membrane
Sequence Length: 289
Se... |
A0A351MEH5 | MLDYRVRVGIESLQDRAPTRFYARNLVLTPSAALTRARIVYELDLLGYVPRGKPAGPGEFSLGRHDLELWPRTASADCRFPLRLTFDDASRLQRLSGQDGEPCSAELEPFEFANLADATLADREYLPLGRIPPQLVAAFLAIEDRNYYRHPGLDPFALLRATWVNLRAGELLQGGSTLTQQLAKNLYTGGERSWLRKLSEFAHVIVLEWRYDKQQLLEAYLNDIYLGQDGSRAIRGVARGARHWFGRPLVELELHQIALLAGMARGAAAYDPRRSPERARLRRNEVLDALSSLGWASAAAIARARSRPLDVTARPLVRAG... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 2.4.1.129
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [... |
A0A351SI61 | MENHKLSNKKIVLSLSLAAIVMFGFGFALAPLYQLICSVTGLNSIGGTIDARKTISDYKNIDQTLSERKITLQLDTTLEKGLDWQFKPVEKQLKVQVGEVSQTSFTFTNTFDYSVVTQAVPSVTPWQAAEHIKKIECFCFNQQTLAAGENKVMPLTFVIDPDLPKDIKTVTLSYTLMAVDNKIAENTKQNF | Function: Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
Subcellular Location: Cell inner membrane
Sequence Length: 191
Sequence Mass (Da): 21317
Location Topology: Single-pass type II membrane protein
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A0A1F5DSM3 | MWRLLDLGAVDGYTMTNLYEAVAKTVSEGSSPNTVILDHPANPFVNIGYHQMMEKEINIEYAREMGFSLVRRTIGGGAILDGPWEQDYFAVVNRKSPDCPPTIPEFYEKFTRPAIYALKCFGLEAQLRKPNDLTVGGRKISGNGAITIDQANVLAGDILMQTPADLMSKIIKAPSEKFKDKLADSMTQWLTSLERELGEVPNREDVRSRLVEGYEKEIGVTLILGTLTEKESGYLEELLEERRGEDWIFSKDLELRHLLSDEGRGAKVKEGVTVLESVYKAGKMVRVTVVARDNKIDGISISGDFFTQPFMGAISKLEGA... | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 366
Sequence ... |
A0A352KLW2 | MAVRVKICGITRPKDAQIAVAAGADAIGLVFYPGSRRYVNIELASEIVEGLCPLVLLVGLFVDQSPAEIEQVCQAVPLNLLQFHGKESVTDCERYSLPYIKAIGVARGVDMVGIASTYTSARAILLDKFDTEAHGGTGQSFDWSQSPCLTLPVILAGGLTAENVESGIKTVKPSAVDVSSGVESAPGIKDAEKVKRFIEVAKSVV | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.
EC: 5.3.1.24
Catalytic Activity: N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate
Sequence Length: 205
Sequence Mass (Da): 21648
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A0A7D7VI17 | MKDWWEALQSRERYMVFIAAVLVAIAILYLAIWTPIASSRDDKQKRVEAKHETVAWMSQKKQEVDHLKRINPNMFNQANDGRSLLAIVDTGAKNMGIRPAITRIEPKGEDSVQIWLEDMAFDYLIVLLGELERRNNIEVSDASLNRSDQVGKITGKVTLIR | Function: Inner membrane 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: 161
Sequence Mass (Da): 18437
Location Topology: Single-pass membrane protei... |
A0A964X822 | EMDGIHPMTAERRGRYLLLCDPLDGSSNIDVNVSVGTIFSILRAPDDAAEPTEADFLRPGTEQVAAGYCLYGPSAMMVLTTGQGVSMFTLDRDIGEFLLTRENVTIDADTKEFAINASYQRHWDGPIRRYIDECLAGEDGPRGKNFNMRWVASMVAEVHRILTRGGVFLYPCDRRIRAQGKAGKLRLMYEANPMAMIVEQAGGAASDGRQRILDIEPAELHQRVPVILGSRNEVERLVSYHD | Cofactor: Binds 2 magnesium ions per subunit.
Catalytic Activity: beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate
EC: 3.1.3.11
Subcellular Location: Cytoplasm
Sequence Length: 242
Sequence Mass (Da): 26919
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A0A3P7EQM0 | MGTLIPLIVCLFHVARRLYECLFVHIFSDSKMSIVHYLTGHFFYLSLPVCIVCSEHPTDRGFTSSTVFLSVIILLETGQNLAMRQLASLRPLESKGMTARYLPPTGSLFRHVTCPHYALEIAFYTTVHIYLGLRLVPFSALTGFVLVNQVCSARKNHQWYSEHFPAYAKHRTSIFPFIL | Pathway: Protein modification; protein glycosylation.
Function: Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-gly... |
A0A661G8B5 | MTESQPTRRSIRSFVRRTGRMTPAQNRARTELWPLFGLEYAEETLDLDSIFGRTAGKILEIGFGNGESLVLAATEDPDSDFLGIEVHEPGVGHCML | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
EC: 2.1.1.33
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Length: 96
Sequence Mass (Da): 10667
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A0A3M1WYJ6 | MKHILQSLTLLLLGLAAWAAAHAEDELLPPKQAFALEARMTAPDRVEATWKIADDYYLYRKNFHFESKTPVVEIGTPDMPPGDTKNDEFFGKIQVFHKQVTIGLPLKGTLEPGQEVHFKFIAQGCNEKVGVCYPPEPYDVTLKVPAGAGAQGPGESAGPLAALKSLASQVAGSDDELLPPDQAFVFSLEVAAEDRLRAHWDIAPGYYLYRDKLRFSLRDSPGNRLGPINLPPAKTKHDELFGDTPVYVHELDIDLPLIRDPDASDRITLVAEYQGCNEPRGVCYPPVRKEIAFSLAQRLGKPDAVEQELIEAAETARAGT... | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction step... |
A0A2E2WUT3 | MKILLIGGSGQLGLEFLSLKIPNNLSFLSPDSNQLDIRNRVQIKNFVEKYNPDIVLNFSAYTNVNKAEENLEDCLEINHLGVKNLVTCLNNRSIPLIHISTDYVFGMYDKGPYNALDKRGSVNNYGYSKLLGEDEIIKFSKKAIIIRTASLYGLFGDNFFKSFFKTLNEKKEMRVINDQKISLTWSYDLSICILDLLKKIERSKSWKDKNSIDIIHLTNKGYTSWFQVAKIISDSINNKKYKKDITKVHPIKAIDWKNSAERPSDSRLASSNIVDGLDIIEMPLWRDSLEKAIKIYLKGKIYE | 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(+) + NAD... |
A0A8T3RTR2 | MSISKLNTFSECKSVAHFNINFIQYLNEDGQLCAEAPAFCHDKILMLSLYRAIKLLHLFDLKVLNLHRAGQMGTYTGTLGQEAVGIGAASCLTDNDVFVPYYRSAPDLYWRGVKLHEILMYWGGDERGSDFADPRLINDFPIPIVIASQLLHAAGVASAIKLRQQKNRAVLTLVGDGGTSEGDFYEALNVAGAWQLPLVIIINNNRWALSEPNTRQTACQTLAQKAIAGGIEGVQVDGNDVIAMRAVTEAALAKARAGGGATLIEALTYRLCAHTTIDDATRYVASEELDQAWQREPLKRLKTWLITNEMLDAAQDANLE... | Function: The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
EC: 1.2... |
A0A1A8IGJ0 | MRKAEGGVLLRLLLLFMLHATGTSYSPPGKPTLTRCRSPEKETFTCWWEPGSDGGLPTKYALYYRKENSDKVFECPDYRTAGENSCFFNKNDTSVWVNYNITVVATNALGRTFSDPVDIDVVYIVKPNPPENLALTVLWDQTWPYLHVSWESPQKADTRSGWITLIYELRIKLEDEDEWEEHPAGQQKTFNIFSL | Function: This is a receptor for the anterior pituitary hormone prolactin.
Subcellular Location: Membrane
Sequence Length: 195
Domain: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
Sequence Mass (Da): 22434
Location To... |
A0A3C1PVN3 | MNLLIDFGNSLLKWCLWVDDLVIEQGQIDPIALESGLRSIDWSLVKSVAICSVADPELTHAVSVHCDSLSATECGFRQINLTELPSWFSLGTTSAKQVGQDRVVA | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
EC: 2.7.1.33
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Length: 105
Sequence Mass (Da): 11474
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A0A920M9R9 | MRHLIFIFLLCSFLNKVKPKAAIFFETEIWPNSIHLCKEMEKPSIVSNGRLSKKSFKKYMKLNIFLKKVFSNLDLVMAQGDEDKNYYHQLGCKNIHVTGSVKFDQGLILVNQNH | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of 3-deoxy-D-manno-octulosonate (Kdo) residue(s) from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4'-bisphosphate precursor of lipid A.
Catalytic Activity: CMP... |
A0A2D7FXH0 | MITDPTQNPFYSLDYLDYLVEFVLDRYSALFSAEELCQLTQYQALPQPSRALYARLTQRKGPYFRLDRLRYKEIIDTEQAAVQLVATKFAAWVGSIRPDLQLALRTKAELKSLGVLAAYDLEQAAKPAIDQALLAQHCQLPTLSILQLECGGLIALCEYLFFGNRHQTLSEFVVTDLGLHRYENVDLVKSSAFASRSMLNANRLVDQLRAWAHLLEQESKTLKQHPDETRKARLISGLQGLKSMVPSAEDVLNYALTRGLDKLHLSLGQSLERVGHLTEALMCYEQTERAPALERRARIAFKQSRPEEAVGVCRAILKDC... | Function: Nuclease required for the repair of DNA interstrand cross-links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions.
Catalytic Activity: Hydrolytically removes 5'-nucleo... |
A0A0V0J762 | MAGILARIFRLRYILFGAGVGGAYTVNQKYEEFKNSLPSFGYLKNYLPQESEVQSLFTSIRESLFRTSDKSPVRPWGPSMKVFWKTVNAEQHDSEESSVSPTDLNPGATAPTPEDVEKTRKESEKVMEELRKELIKTKLQYQKSIRELQSEIKSLRTQLLLRYQKTSQPDRIKKTLIEMYSEVLDELSSLDTEYNAQDHLPRVVVVGDQSSGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPYHVASFNDSTKEYDLTNENELASLRNEIELRMQALVANGKTISTEVISLSVKGPGLQRMVLVDLPGIISTQTT... | Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
EC: 3.6.5.5
Subcellular Location: Membrane
Sequence Length: 962
Sequence Mass (Da): 109579
Location Topology: Single-pass membrane protein
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A0A352KS34 | MNMNNRICFVLMVALLLPACAQKIELPIEDFSPSSPEQVTAMSINHGAIYQSVSARTWFEDKKARRVGDLITIVFNEQTDASKTASTSASKDSFTSMANPTIFGSSLQFNVPGVVPLQTNIGNNLQTSIDTSADFAGSGSSSQSNSLSGSVTVTVSEVLGNGNLRVRGEKRVRLNQGTELVQVSGIVRPQDIRTDNSVLSSQIADAHINYKGQGIIADVNTNGWFGRIFMSKYWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Subcellular Location: Cell outer membrane
Sequence Length: 236
Sequence Mass (Da): 25530
Location Topology: Lipid-anchor
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A0A7K5C6M3 | PLRSPAGLTAVVFAPQENPALIRWAYAKSQNVYPTFRPTPTTSFLGAVYGLGPLLFWIFVLKADRDHKEKCIQEGKHKRSPFSVFF | 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.
... |
A0A2A4WMP2 | MIDGLTNVNLSRRSIPNIITSIRLFLLIPLSFYLSNEDYTTALYIFFVAGVSDALDGYLAKKYNWTSHFGSVLDPLADKALLVISMAILTLNGKIELLLFSLVALRDVYIVFGAYLYHRKFGKYKMNPSIYSKLNTFFQISMVTLLLVSLGYQHLSASIFVTLNWIIYLTLFVSTLHYTIIWGGRYFSNHSPGELPQHSDK | Pathway: Phospholipid metabolism.
Subcellular Location: Membrane
Sequence Length: 201
Sequence Mass (Da): 22883
Location Topology: Multi-pass membrane protein
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A0A920S9E4 | MRGRNIVVVGAQWGDEGKGKVVDLLTKNVGAVVRFQGGHNAGHTLVIGNEKTVLHLIPSGILHDNVDCLIGNGVVLSPSAVLEEIAQLEARGVEVRERITLSPHAH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2.
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
EC: 6.3.4.4
Subcellular ... |
A0A967VW98 | MKGYIQVYTGNGKGKTTAALGQAVRSAGAGLRTFIVQLMKEYPYSELVGLEPLADAITLEQYGGDAFVYRGEAPGEDEKAKAAAALARAVEALEAGRHDVVVLDEVCAAIYFGLITTADVLAVLDAKPDGVELVLTGRYCPDEILDRADLVTEMKEVKHYYRQGVKARKGFES | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
Function: Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids... |
A0A0X3NXS6 | MTLVGECDFKLKDFVAGPVEAFWPHYGTCKNGDITSWTNLNSFANFIRKSTNGAGVSVVMADGGFDVSGQQNLQEVLSKRIYLCQCLCALTVLRPGGHFITKMFDVFTEFSADLVRLMSYVFREIAFIKPVTSRPANSERYFLCKGLLSTASSMTGCPAASPSVENSLASPQKRLQPSTAPADKPKHKLPGSGRRLKAPVSATSSFGQCEQPADPVDTESAIGVLIRHLLDVNEKLRRLENEEKGEKPCTVLRLCHPEVVNEDGRFSNFLRQCNEDMARKQCKYLSKLLTFAEDATLNDDRQKDIKEACLRKWQIPAVPR... | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucl... |
A0A2E7RN19 | MIIAGVDEVGVGCLAGPVVASCVILPEQINEIFKDSKSTSESLRSKQFQFLRRNTYASIGLCTPQEIDEMNILNATHLAMKRAINNIQIKPEKILIDGKYVPSGLLNAEAFIGGDKVHQQISAASIYAKYFRDNLMGRYAQIFPKYYFEKNKGYPTQMHKEAIIEFGLSKIHRKSFKMK | Cofactor: Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Subce... |
A0A0H5R6S0 | MYCNELKSIIAKYFTNIITVMTILRLRCKTPSGSNIVIAIDDEQTIADLYNTVRSSAGVNSEFQLSLGAHPKNGSPLGDPHNTQLRFCANPKIQTADTLTISLMPTEDYMEIFQIPDDNSCLFNAIRHALSSTRSQDTLDDPAMMRSVVAAMISSDSERFSPALLGKPVVEYCNWIMNTDSWGGEIELAILSEYYQIQLKVIDIRTQQILSYFNSVEIAYLLYDGIHYNILQRKSGRCVFSVDDAFALTQAKNIALQALQDRKFTDVNAFQLRCEVCKCGLTGQAEAVQHMKVSGHTQFAEYK | Function: Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of u... |
A0A349EIT8 | MDTINSSDFNYIRDLVRRHSAIALEADKAYLVETRLAPLARQAGLASLQELIGLLRIQPAHPLHRQVVEAITTHETSFFRDIHPFEALKTTILPALLARRRSASLTIWCAACSSGQEPFSIAMLMREHFPTLAARQIRIIATDLSSAILARAREGLYSQIEVNRGLPAALLTRYFDKQGLHWRIKSEIRRMVEFQQSNLAEPWPLIPPADLVFMRNVLIYFDVNTKKAILAKIRHVLKPDGYLFLGSSETTLNLDATFEPISLGKSTCYQLRQTKTP | Function: Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP.
EC: 2.1.1.80
Catalytic Activity: L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine
Sequence Length: 277
Sequence M... |
A0A348UP75 | KPGAAEAVARGRMPARSEGFFMFDRQRTLRNVVQCTGRGRAHAAVVRVTFKPAPANHGVVFVRVDLHPTARVPASLAAVAGGSFSTSLSHAGVTVAGVSPVLAACAGLGLDNLLIELDGPELPMMDGSAAPFVFLLEAAGVVRQAVPRCYLRVAKPVRLQEGEAWAELRPHPGLHLDYALEFDSPCGERKRRAAAVELSATSFVRDLARARSPLLAPESTDAEGREWLRHKLMSAVGDLSLLGQGLIGAFSGFASGHALHRALLERFLSDPEAWEQVMLAASDEGDSNTDLVNGAEVPELA | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step... |
A0A2E1F7S2 | MNKILTALALIFCTSSFAKIEVLDRIAIIVDDGVVMESQVKNTIREITNRYDDQGLQKPPDDVIKEQVQEKLIIEELQLQMADRAGVXISDAXLNVTMSRLATNNQMSLEEFIAFIEENEDSYEELREQMRREMRIQRIQRGRVNSSIDITENEFEAFLATDESLGALEPELLVRQILVRDIQTANKILQLIXXGDDFSEIAKEFSISSNASAGGLINWRKLIDMPQLFEEALVKKSVGFISEPLESGSGFHVLKLEDKRGEFVKYEDQWQSRHILLIPSTIRNEEDSEKELNEIRQRVLXGEDFASLADEFSEDPGSAK... | Function: Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associat... |
A0A660L0F8 | MAETMVRMGELATSAVAGDVLVSLGLGSCIGLALLDRRLGVAGLAHVVLPSSGGNAPLGSWKFADYAVPELVDRVVKLGARRPMLEAVLVGGASMFAVSKSSLEVGQRNEAAVRELLREQHINVIAKETGGSRGRTIRVYVGSNKVTVKEAGGTEKPLIAGASVVAA | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
EC: 3.5.1.44
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Length: 167
Sequence Mass (Da): 17205
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A0A1X6P9P8 | MARGRLARAYLLLYNAAACALWAAAAARLATAPGGLGGAYAAAAPPIRAAQTLALAEIVHAAVGLGGGSPPLVAVQVLGRNLVLFGVLGALPAVAATRVAGALLAVWTAVEVVRYPYYLGGLVGVVPGALTWARYSAFLPLYPAGMAAEVGCYVAALPAIDAGGLYRVALPNAANFAFDFGTFVRAALPLYLYFGPALYVHMLRQRRRKLAA | Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 4.2.1.134
Subcellular Location: Membrane
Sequence Length: 212
Sequence Mass (Da): 21794
Location Topology: Multi-pass membrane protein
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A0A2E3WVH2 | MISLKSPAYEQEIDRQKILGHLQNVLTRSDIGFKDVTHREDIWKASQARADQVKGDLTDLALVGIGGSHLGVEAIHNALHFGDLQVTFFDNLDPIYFKRKWSGLNSIENTHWVITSKSGTTLETLALANFIEQSLKAEGLDLASRCTVITEFKSNPLYTWAKAAGVEVLELSEDIGGRFSVLTPVGVLPAAIMNLDIEGLRKGATWALANEDFVCDLAIQFLHSLKDEKFISMMWIYSDQLNTFGEWWQQLWAESLSKKVSLSGEPGPTVSTPIACRGANDQHSLLQQVIEGQRDKLVGFLTVVANNDYGEAMQGDLFGV... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 406
Sequence Mass (Da): 44721
|
A0A2D5I477 | MSIYITYLIKRSLVITCFVFGLFILVDFLFNLIGELEDLSLTYTFIKAFNFSLLSIPDRAYAFIEGSCLLGFMIAMGLSQEEGNLNVLRSSGISPLKIVILSSIGPLSIAFFFLLGSEFLFKEIGNKAEINKAIATSSSNSTQEESVWLIDGNKFLNFERKIGDQIFGIQYFELKNNKVMLAQMAPSAKIKNSEIKFDDSLYTTINKNPSQKFNEKMLNKSFNFPKVISKNLRDIENLTIRESYSLNQILSGDIGKQDRFFKAHVEKKIYKFFFMLISITILILFFGYFIFGSLRDSSPGSKIVISVLGAFVYQIMQDLT... | Function: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.
Subcellular Location: Membrane
Sequence Length: 354
Sequence Mass (Da): 40247
Location Topology: Multi-pass membrane protein
|
A0A8H6YYD6 | MDKRLGGLAGRWWRKTRVVYERTSQSAQRSQIRHHSNMDHSTLKTLYTTSPAFSPLVPVGLLPYLAFVLLLLTFTLGFYVSTIPKATIPVRELGIASLASILGGFGVVALFCAVGVNV | 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 ... |
A0A5J4L2C2 | MVQGAKWAVDEGYGFAEDIDMTEERGCLEGADPSAVSKHAIQRGRKQLGSLGSGNHFCEVQMVDHIYNQDAADAMGIGRKGQIVVTLHCGSREWDIKWPKTTSS | Cofactor: Binds 2 manganese ions per subunit.
EC: 6.5.1.8
Catalytic Activity: a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + GTP + H2O = a ribonucleotidyl-ribonucleotide-RNA + diphosphate + GMP + H(+)
Sequence Length: 104
Sequence Mass (Da): 11367
|
A0A3M1K3Z3 | MDLPLMFRYAGRWARGAVVGWLVSSLAGGAWADTNLPEPAENRAVTYVTAQEKQLGAAWLRQLRGQVSTLDDPWLTEYLLDLVYRLYPASGMQDGHISLVVVDSAELNAFAVPGGVIGVNGGLLLYTQKEDELASVLAHELAHLAQRHFARRQEEAGKSAALNLAGMLASVVIAAAAGSDAGLAAMAATQGYSAQSQLAYSRDNESEADRLGMRILASSGFSPQAMPDMFRRMAEANRYSTRPPEYLLTHPLSETRLADAQSRARQYPETPRSSGLEYAFVQARMQVHYAERPSVALDTWRSRLEKQGAAAVDARVDVWR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Functions as both a chaperone and a metalloprotease. Maintains the integrity of the outer membrane by promoting either the assembly or the elimination of outer membrane proteins, depending on their folding state.
EC: 3.4.-.-
Subcellular Location: Periplasm
Sequence Leng... |
A0A534AFM4 | MRRRAMRCASRASRLRSQTLLKARPGTKSALLRARSLQPAVASRRRWRLRPTGRWPKPGIKARRVNDTKPGTAAKTALRWLHGIEEWALTVLVLVLVVLAGAQIFLRNAIGGGFSWADPFLRTLVVWAAMLGALAAVREDKHIAVDVLQRFLPRGAQRVARVLTMLFAAGICAAMTWYSIGFVGIDFSTPANATGDGVPWLPPWLLESVLPFGFGMMALRFVLRAFAEPSHVPGLATTELLHAPPAVGENDEGRA | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 255
Sequence Mass (Da): 27944
Location Topology: Multi-pass membrane protein
|
A0A962TAB1 | AKDHGEGGNIVGHPLEGRILIIDDVITAGTAIRESMDIIVAAGAKPAGVVIALDRQERGKGERSAIQEVEGDYGIPVAAIVRLQELVEYIGQSDEAAAHLANIEAYRREYGV | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidi... |
A0A2E5V9X3 | MRSRPVLDLRWILFLLGIAVFLLIYFFSIKPIPYANKLSFFKRFKFKYRDKLVEEKDDYKAQENLNDNDKIDDIDIKDAQSSIDIDKQKVITLRLIGKNQLDSLSVFKCLQENDFTYGRFGIFNYYEKNSNNPIISIANLTEPGTFDIENKENLVIGGLTLFMQIIGNSDGVSRFDFMVGLAKSIAEELDIEILDENGSSWSIQRERYIREEIIAFQHDVNK | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 2... |
A0A0H5R231 | TSLLGGRRFDVVIADESSQATQAVMLLPLQLASRFVLVGDHYQLPPLVKDPFGRESGMDISLFLRLSEAHPQAVSQLYLQYRMSAPILLLCNELVYSYALKCGSEAVANATIVIPNPDKFPSLAEKYVNFPEMDWIKSALELQRKVVFLDTDLIPAPESLRGEQNQFEAEIVIHLLYSLISSGFSPNDIGVISPYRSQIRRIRHLATSLQVELDIDSVDKFQGKDKSCIIISFVRSNDKNRIGEILQDWRRINVAVSRAKHKLILIGSPNTLRESPIMNSLLAVVRREQWMMTLPCGALEAYENIHAFSGGWSQGEMESM... | Function: Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA... |
A0A2G6LDB6 | MRIPMNSTSNQRLIQLANKFKHIHFNRLMSPERAKEFSLTADGLYLNYARNPLNEQVMQALLQLAEDSRVQEKISAMFAGEHINQSEGRAVKHWLLRAPENPSDPDSVAVHQVLDKMALLVDKIHHDTLLSEPVTDVICMGIGGSELGSRLVYEALTMGRKKPINVHFVANIDALAAADAMVNCTANTTLFLIISKTFTTFETTKNFHTVKKWFCQQEGLTEADFWQQSCAVTANIAGALAAGVPESQIFTFWDWVGGRYSLWSSVGLPIAIACGMPAFRQLLAGAQAMDEHFRTTECKQNLPVVLALLHIWYSNYLGYP... | Pathway: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4.
EC: 5.3.1.9
Catalytic Activity: alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate
Sequence Length: 388
Sequence Mass (Da): 43242
|
A0A0V0X228 | MNVYSYDGAFVVILLAVCTCAYFRRIPRLKKWFFSDKSGIWGVCYKASVIGIRLHALLYFCSAMVQHKVKQKISLPANAKSRSDRHRQRKVKNKSGMKKGKWTIKPKNSKDLQHFKKEIAISKVINEENEELITARAVV | Function: Involved in the early part of the secretory pathway.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 139
Sequence Mass (Da): 16032
Location Topology: Single-pass type I membrane protein
|
A0A6P2BEQ2 | MSPDVIDAPLELASWLARIEPDHVEGFALRMREGTLHLLAGEPELGALAIDFTRGASGFRGPRARSERLVRACGVRDGSRVVDATGGLGTDAWLLASAGAEVELIEQHPVVAALLADGLLRARVQHPDIAARIHLQGADSRAVLAPQMAAVTAVYIDPMYPPRRKSALGDRRLRLLAALCAMSGQPGDDVAGLLAAALTARTKRVVLKRPLREALPNGVPDPSYSLSGRSTRFDVWRRTGP | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.242
Subcellular Location: Cytoplasm
Sequence Length: 241
Sequence Mass (Da): 25753... |
A0A7W7ZDB9 | MSLGKYRRLSIIGLALFGAALGAVGGYWLCHVSRLRAANVALSTYASELVDHANEYGAELRAIKLAFNPSAFPFCSTEEISKLRELAFHSLQVKDIGRLQNGKLVCSGWLGKLADPWSMPQLTMTLPGGTQIYADIPLAIAGHQRGVVLAQQGVDVVLSPNAFERWDRPGMRNMVVMVNFTTRQIVRITGDAMELDPALILSEGHAEIGGKTYYARCSRQSALCVVAEGSTQIAASDTPWLQFEYIVMGALAGFGLSLAAAQFYLQRIGLARQLRRAVRHGRLSLVYQPIIELPSGSCAGAEALLRWSDDDGNAIAPDFF... | Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
EC: 3.1.4.52
Subcellular Location: Membrane
Sequence Length: 538
Sequence Mass (Da): 58823
Location Topology: Multi-pass membrane protein
|
A0A389M5E7 | MQGATIHSWLNISIFEHDFDLGVEEHNLRTQDIDNNGALVAFQGMVRVFDQAIALKSLFIEHMPLVTEKEIGKIAILARKNWNISQCRIIHRVGMLAKNEKIMLIIVTAKHRSEAFNAAQFIMDYLKTAAPFWKREFFEDGSSIWVEPKTSDTIAAARW | Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 2.8.1.12
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Lengt... |
A0A968D864 | ATALAFMTVLTFIQVILRYIFGTGWVWSLEATTYTFAWLVLIGMSYCVRERAHIAVDLLVSKLPAVTRRIVMLTAIGLCVVYCALMIYGGAIFVDRLMMLGNNARDIPLPRWLLTSILPIGFGLLAIRFLQVGWRVLDKDSAAAGFGERESAPHIREE | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 158
Sequence Mass (Da): 17652
Location Topology: Multi-pass membrane protein
|
A0A968CY28 | MLASILFGMGLPTVVCYVLLATTVAPSLIDLGVTPLAAHLYIFYFGMLCMVTPPVSFAAYAGAALAKADPMKTGWTAWTFALAGFLLPYMFVYNNSLLLMGSVTNILFSVLTSMI | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 115
Sequence Mass (Da): 12299
Location Topology: Multi-pass membrane protein
|
A0A0V0WI76 | MAQINIIVAICEKYGIGKKNSLPWHLSKEIQYFKKMTTSVSDPNKINAVIMGRNTWYSIPEKYRPLSGRFNIIISGTMPQLSDEDVIVISNWREAIEIVEHPLSKKPIETFWICGGAKLYNDVIESGLWNRLYVTWIMKEFDCDAFFSFPHKNTIKLVEDDRIPSDIQVEKAKPTTYMATATALANENSNPMLPPNSGPNDRDSKK | Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate: step 1/1.
EC: 1.5.1.3
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + H(+) + NADPH
Sequence Length: 206
Sequence Mass (Da): 23515
|
A0A7D7ZK12 | MNMNKILLILLTICMISGCGFHLAGEGEFASELSHTHIKSASSSKELLRLLDKNLRANQINIVGIDSATALLHILNEETEKVVLTVDNDGKAREFELLLRITFDVKRQDNTILLGQQTIDLNRDFVFDKSDLLGTNEEEQELFDEMRKDAAKLIVYRLQTI | Function: Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Location: Cell outer membrane
Sequence Length: 161
Sequence Mass (D... |
A0A2D9ILB2 | MQPKIFSKSIFEDSRGFFIENFKKADFSEQFVQDNLSFSKNKGTVRGMHFQKGEFAQTKLVTVLKGSILDVVMNMQTKEVYSYELCSKKMDSLLVPNDFVHGFMTLENDTLVSYKVDNYYNKESEGSINWKDEVFQGIWPEFEEYFLSEKDEKAPFIRDLEI | Function: Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
EC: 5.1.3.13
Catalytic Activity: dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-beta-L-rhamnose
Sequence Length: 162
Sequence Mass (Da): 19016
|
A0A3A2ZJ90 | MSATGRSSENVSGQSTRAAARTKQRSPPSPFYVPLNITLYIFLISNGIAAFNAPIQDCDEVFNFWEPTHYLDHGYGLQTWEYSPVYSIRSWLYISAHAAVGKIGSLFFSNKVLEFFAIRFFLAVICAACQTRLYSAVCRTLSPRIGLLFLMIAAFSPGMFHASASFLPASFTMYTSMLGLAAFLDWRGGQKIPQGIMWFGLGAIVGWPFAGALVIPLLLEELAIGFIAGSMRTVVSNILNGILRCLAIMWAEIAVDYVFLKKFTVVPWNIVAYNVFGGQGRGPEIFGTEPWAFYIRNLLLNFNIWFILAISAAPLLVLQA... | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
EC: 2.4.1.-
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 550
Sequence Mass (Da): 61740
Location Topology: Multi-pass membrane protein
|
A0A661GB52 | MRENILTASVGEFWFAIVLLVVLALLSFYGLFRFFTRARLIEDTPTSKIRSAAQGYLELNGVADLLPGTPVVAPLSQLQCVWYRYKIEEHQPRAHSFGSRRDRNRWNVVEKGTSDALFRFADDTGDCVVDPEGAEVTPALHQIWYGSSHYPGGAPLASRDGGWMARLGVGISFGMGRYRYTEERIMPATDLYVIGQFRTLGTGGGGDRDADVGAVLRAWKRDQAELLKRFDQDGDGKIDLAEWDAARQAAEAAVDASLRDRQQTEPVNVLANPRVSRRPFIISVESQREMARRLRLFAGASLAGFLGGGTAVVWALGVRL... | Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
EC: 2.3.2.27
Subcellular Location: Membrane
Sequence Length: 323
Sequence Mass (Da): 35594
Location Topology: Multi-... |
E5AC32 | MSSSIPNDVYQFSTISAIHAGFNTGQPCTSDLTTHGTHGIGIYEDGTLLLLKDSRAFSITKTGLAKSAQPDARLPWAMVTVYEPSFKVTVFSLTIDTFDALVSGDDLGPVKGVNTLMPFLIAGHFSSLEFRDGPRRNAIDGTLFGFVVPMWMKGICGPRIHAYFLDAGEEVGGRVEDFRMEGGGVLGFAKCGRFHLGFPQGEEWEALKM | Pathway: Polyol metabolism; (R,R)-butane-2,3-diol biosynthesis; (R,R)-butane-2,3-diol from pyruvate: step 2/3.
EC: 4.1.1.5
Catalytic Activity: (2S)-2-acetolactate + H(+) = (R)-acetoin + CO2
Sequence Length: 209
Sequence Mass (Da): 22675
|
A0A0X3PN02 | TSKSAAPHRFTVSLKCAFDNVRSLCGSRSSLWFFYFCRLYTRTSWHPSILSIKKDSAQLMSERPGVQLQVPPDVVSVHPLTCLINGHLASGCFLFNNSSPLVSFDLLKDWFEVVGHVELTNRTLVWRQTDDRCPQFDDQPYDPTGTYLEFASVNTEARRHVMLISADSNVPVSSQWDPKGHYYPIQIAQFGLNYFSQLKHMQLASTIPPSSGAKPESLDVFDIKTDIKPRSTHSAIWKCLTRAPGRPCLFGQAHDDVTATAGTIVFDLSPYARITPPPYLFLNGTSWHANSSLVFRLTLRPSGSWDTPVSVELQYTCSSH... | Pathway: Glycan metabolism; heparin biosynthesis.
EC: 5.1.3.17
Catalytic Activity: [heparosan-N-sulfate](n) = [heparan-N-sulfate](n)
Sequence Length: 720
Sequence Mass (Da): 80601
|
A0A496WRD8 | MAWPLFSMGQTQTTVGSLLAVVVVLVGTLFLSRYAHRAVSGYFQLVASNDDIAVDDIAVSMYGSVARIIVWFIGVEIALHILGIHLSTLFAAGGFFALGAGFALKNVVENFISGGIIRAEKTIQAGDLIIIEKQWLTVKHIGIRTIEAITKKGVDIIIPNSIVAQSMVENLTRRSHVYRIKANVGVAYDSDRVQVRKTLEETVNRLEWISKQQAPTVHLVEFGDSSINYDINVWIDEVREARPRNSDLHEAIWQALNEAGIAIAFPQLDVHLDKNELPQ | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A0A6P2BJN5 | MTCVLPDWPQPGEPLFRGRYRTTPEAFRVDELPGWAPSGAGEHLLLRVAKRGANTAWVAQALARRAGCQPSDVGYCGEKDRHAVTTQWFSLREPRQALQWSGDEVGDGWNVLALARHDRKLRRGDHAGNRFSLRLELEHAPAPEAVAQARARLEEGIPNYFGPQRFGRDGGNLARAAAWVDGARLPARGPERGRILSTARSLLFNEVVAARVRAGCISAVLDGDVVEDAANRQGAPTGPMWGRGRSATGGAAAALEAAALAPYQRWCERLEYAGLKQERRALVVRPGDAVLDAKGSSLQFECVLPPGVFVTSVLAALGTF... | 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: 345
Sequence Mass (Da): 36830
|
A0A3D1A155 | MEGDMTFGEMDIFHRQVDGEIRFSLANAVEPGTFDLAAISEFSTPGVTMFMRVHELRQPVVALDEMLAVADAIALELGGEVRDETRSVMTPQTIEHCRESIREFQFKHAG | Function: Essential cell division protein that stabilizes the FtsZ protofilaments by cross-linking them and that serves as a cytoplasmic membrane anchor for the Z ring. Also required for the recruitment to the septal ring of downstream cell division proteins.
Subcellular Location: Cell inner membrane
Sequence Length: 1... |
A0A0D8J161 | MMERKNGMRLPAVVLLAALAFSCFAPAALATAEEPPEDLPAAVSAQDGAQEETTLPGADAAQQDSAAGTGAANPHETIATSVQENPRFAKPQLDIPCRNAILISIDTGDILYEKEPDAEVPMASITKIMTLLLTLEAVEAGKISMTDIVPISEHAFNMGGSQIWLEPGEQFTLDELIKAICVCSANDAAVAVAEFVGGSEPVFAEMMNARAAELGMTHTRFVNACGLDAEGHYSSARDVAAMSLALLRHPKILEYSGIWMDTLRGGETQLTNTNKMLKSYAGITGLKTGTTNGAGVCISASAVRGGMGLLAVVLGSPSSK... | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
EC: 3.4.16.4
Catalytic Activity: Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanin... |
A0A2J8RF45 | ANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEMADPDLLEESSSLLEPSEMGRGTPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTAESHSFVQAGVQWRNLGSPQPPLPGFKQFSCLSLPSSWGLQGDYVHKSVFIIFFQGDQ | Function: Essential component of the vacuolar proton pump (V-ATPase), a multimeric enzyme that catalyzes the translocation of protons across the membranes. Required for assembly and activity of the V-ATPase.
Subcellular Location: Membrane
Sequence Length: 195
Sequence Mass (Da): 22342
Location Topology: Multi-pass memb... |
A0A5D2PRY0 | MTGVQQEGDDQSVGEVGELSEIFQWKGEVPKGLPDWKEDEKVHLGEELSDVLLYLVRLSDICGIDLGKAALRKVELNAIKYPASKNYGTNDDSTAEMCG | Function: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which it may even have a higher efficiency. May protect DNA or RNA against the incorporation of these genotoxic nucleoti... |
A0A3A4VZ27 | MDAVLDRQQLLTRARALVQQMETGDMQQAEQLIDEISQLRESGLFQQVGKLTRELHESLNSFRFDERIAELAEQDIPDARQRLNYVISMTEQAAHRTLTSVEAALPLSDDLRDKAGALKDRWQRLLRRELDAQQFKVLSGEVADFLDLAEQNCAMTHQHLSDVLMAQDYQDITGQIIRRVISLVQGVEESLVKLVRISGQRMAPVRVNGAHKHELEGPQINSHARTDVAANQDDVDNLLSSLGF | Function: Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
EC: 3.1.3.-
Subcellular Location: Cytoplasm
Sequence Length: 244
Sequence Mass (Da): 27605
|
A0A1X6PDZ6 | MPSAAVRRRRRGSGGAAPAAPPPPPHLPAAAAGAQPFLPAARPPPPPPGARRGRGGGGGGGDGGGGGGRRRRARGAGGPPPAAAAPAAATGAPAAAAAAAAAPAGARRRRRQRPSPAAAGGAPPTGGGGPLGAPTGAAGAAGAAAAAVPPAAAPAADAALAALLHPVPPRVFYADHWEQAPLLLRWADRAGGGDGKDDDNDNDDDDDGDGDGGGGGGGGGGGGGGGSAAHVGGLSQAAWRSRWARLLAIDDVRGWVVGGRLRYGADVDCTRYVGGERATYNAVAAEVGAPAGGGAGGGGGGTALPTRGGAAATATTAATA... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 698
Sequence Mass (Da): 68146
|
A0A3B9NQ15 | KDLGDFEGTSVVAIAGIHYPDRFFNGLAAKSIELETLAFSDHHQFTSGDLPADRTVLMTTKDEVKCREFAQKSWWAVDQETILPDQIIEKIERTIGQRVANG | Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form te... |
A0A524AUN2 | MGNQPTNVVLVGPMGSGKTSVGRRLACVLKRDFFDSDFEIVARTGVAIDHIFDVEGEKGFRQRETQMLKDLCEIPNIVIATGGGIVIKEENRALLKHNSFVVYLSS | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
EC: 2.7.1.71
Catalytic Activity: ATP + shikimate = 3-phosphoshikimate + ADP + H(+)
Sequence Length: 106
Sequence Mass (Da): 11652
|
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