ids stringlengths 6 10 | seqs stringlengths 16 1.02k | texts stringlengths 117 4.4k |
|---|---|---|
A0A2G8KAW8 | MHFDSAGQAEILRSSQKDQFYISQLRSKLADVFQSWAGARAWIKWRAELDLVTDCLYFGLTTLSGLQTLGEEYVNILQVDHTRRAVPSLQRRTFLVFTHVVFPYLLDKFLSRLSYRLGANLSVPVLPLDWRERLKTTLPLIRHLLLLAHRTHMAFFYLSGVFYHIAKRSSAVQYLMVRRGLSRGSLNPSFRLLGIISLIQLALSVSWQLYQWKKVNGENEERPVSESFGRVSRCFVTMFTLFEQEKRYDCYPCGHLFCCIALWNGVLQNRNVLCAVNLFSRPD | Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Membrane
Sequence Length: 283
Sequence Mass (Da): 32865
Location Topology: Multi-pass membrane protein
|
A0A8S0H2N7 | MKCACATPDFHTGSPIPVGSVIVTSHDMVVPQAIGTDINCGMRLHKLGLNYEQFMAQKAKWTALVRGDLLEGTRNIPTSPTAMSALFASGLGDFWAQVQQQDPIGLFAGADFAQLQRELSGLHESSFARAAPTMHRRPCRTFRARSFATRAWVPWAAAITLSRSRWSPNWWIARPASPRACPWGRW | 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: 186
Sequence Mass (Da): 20594
|
A0A168PAZ4 | MLRSTLSKQSVLSRLIPKSTIRCSSMSNSKAIRPFSTPARYTPAHKKSNSLAAAKPWSELTTPQKVVVASKTTVNVGVILAGVGLTSAIVYYIGSELFGSQSATSIFSDAVDRIRSHEELVSILGEPIKGHGEPSRSKRRRNRRITSQTVEDQDGNPHLFMRFYVEGPENQGTVMLEMIKNEKQKWEYKQLYVDVPGQGLPSKRIYLERNM | Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Location: Membrane
Sequence Length: 211
Sequence Mass (Da): 23584
Location Topology: Single-pass membrane protein
|
A0A6I2XX59 | MTWGRELVEPLLLRTEPAALLPARRSQEAARIERPLDLIACVRLDDSRADLWYAIVRDARGVSYGVPCIVSGKALRRAIPGDGAAEALLGLLGRGSQGTPGEGSRDGHVGVIRWHAEPCAGERGFDVDQTNELVVVGERAVVKWLLHPTAEEQPAPRRLAALAEASFAGTPRPWGLVSIEDGRADVLIATVIDYVADAQDGWEWAVEDVRSLALGETDEANALRSMPVIGRLVAGMHLAFAAAGRSIATDDEAEDWLVEAAADLRDASLAAPTAGLVEQELALVTGFVGTTIIDIHGDLHIGQVLRTSPGDDLSIIDFDG... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the ATP-dependent phosphorylation of D-glucosamine (GlcN) to D-glucosamine 6-phosphate. May be involved in the phosphorylation of acquired extracellular GlcN derived from the hydrolysis of chitosan, i.e., in the incorporation of exogenous GlcN into the bact... |
A0A6I2YVT6 | MAVRGRTESVDQYLPVLGLLILGVIFGAASLLASSLLAPKKKPSTAKTSPYECGIVSESEPPMRFPVRFFLVAMIFIIFDIEIVFLFPFAVVFKQLGGFGIAEVFVFSIVVFVSLVYLRSSGGLTWGPIVRLTKGMPSRTSESTISRITAEPSSDRAA | 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 a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrog... |
R4ISW3 | YDDAFPISLIRFWVLQIIFVSSPSLVYMGHALYRLRAFEKERQRKKSHLRAHMENPGLELEEQQRIDRQLRRLEEQKRIHKVPLKGCLLRTYVLHILTRSVLEVGFMIGQYVLYGFQMHPLYKCSQPPCPNAVDCFVSRPTEKTIFMLFMHSIAAISLFLNVLEIFHLGIRKITRALYDKSGNEGTEDERRPPFHLKKYSVPQQCMICSPLSERISVLQANNQPQVTQVTVPKSKTLWQIPQARQLEVDTCCGKNDWAERDQHSGQLHNHSPCPWDDCVRIQHPGQQPGHSSFSTQNARSQSWLGMPMAPRHCPSYAIGT... | Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular Location: Cell junction
Sequence Length: 409
Sequence Mass (Da): 46824
Location Topology: Multi-pass membrane prot... |
A0A7V9NQR4 | PNVMIKVPATAAGVPVIEELLANGVNVNVTLIFSLERYDEVLGAWKRGLTRARDAGLAAPHSVGSFFVSRVDTEVDKRLDAIDTPEALALRGKTAVAQAQVAYDNFRRFVAADAPAPWQRPLWASTSTKNPDYPELLYVESLMGPDTVNTLPLPTLEALDENGEVARTVDADIDAARGMLSQVAAVGVDMDDVATVLERQGVAAFADAHEKLLSTLGPKLKA | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic... |
A0A533RRD6 | MPFFGLPGNPTSTYVGFEIFVRPSLRLMQGFSAIDRPVTPAVLGHDVKKKQDRRYYLRGRIDRGANGYVASLPHSQSSALLTAAHRGNCFVVLPEGEGFFAAGAPVECVRLDMEEGTP | 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: 118
Sequence Mass (Da):... |
A0A7N0VM40 | MLGGGSSRYPFTAAQWQELEHQALFFKFMVSGIPIPPDLIFSINGKRSQQPQHIGWTCFQMGLSNHKIDPEPSRCRRTDGKKWRCSRQAFGDSKYCERHMHRGKSRSTRNKPLESNNTNDNKPPPPLLHLQTFPSKSALESAGTQSNLSSSLTTCEMTHKPVKDSNFLTFLGIDSGWNQHKKVACDLSRDDESCVVERNEKRQRRTMYHQFIEESPPQEKTDSWLNLVI | Function: Transcription activator.
Subcellular Location: Nucleus
Sequence Length: 229
Domain: The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence Mass (Da): 26280
|
A0A522TKQ9 | MKDDLLGAVSFLTIFGGGRQPKESSKYWFSLAGVVVAIISGLVWQLMGHSTARLLIASVVVLVMLIITGAIHIDGLADAADGLLAHLDARKRFEVMSSPEVGTFGIVAVVMAIALYVVSISVLRPNLLLLIGVFSLSRELAALVMESVPYAKSDGIVSAFSSGSGVLARAKLIIAGEMLLSTFLILVSLGVKGIVLPVVMLAVQIVIVLRAKSLIGGYTGDVLGASIVATETFALVAGALMQR | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7.
Function: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-riba... |
A0A662DXF0 | MLDAIFWGAVQGLTEFLPISSSGHLVLIPALLGREGPDLTTVAMLHLGTLFAVLLYYRTDLVRMARFDRAGRRMMTIIAIGTVPAVILGLAFESKLEELIDRPTTVAIMLIMTGVVLLATTALRRGDRTAEGLDPKDSGIIGLAQSLALIPGVSRSGMTISAGLARGMDRVEAARFAFLLGIPVIAGAGLLSVAKAFSDGAGITTSTIVGMAVAAVVGYWAIAFLIRVLGRVGLAPFGIYCIAAGAISVILL | 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: 252
Sequence... |
A0A2G8JNL9 | MLITRSIRSRTLQALCQVEKKNDTKNLSEKEKTTLYRQIIVDDQRRFLFCFIPKVACSNWKRVIKVMQGTLDPESKGKMDHHSGMTFLQDNEQNLARLKLKHFYKFMFVRHPLERLLSAYRNKFGENIGDYRRRYGSKIIRAYRPKSKAREAFMKGDLSITFEEFLRFLIDSDTSTMDVHWKPMHELCQPCAVHYDFVGSFEQLREDADFVLGRIRGNSTVSFPKRQGYYRPTTPDTLISELSKVRPIVLQQLVDKYILDFALFGYSAPSLDV | EC: 2.8.2.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 273
Sequence Mass (Da): 32102
Location Topology: Single-pass type II membrane protein
|
A0A2R2X1G9 | FLLRNFSLLEVSFTTVSIPKFLGTIISGDKTISFNDCIVQLFFFILLGVTEFYLLAAMSYDRYIAICKPLHYMTIMNRRICILLVFSSWLVSFLIIFPGLMLLLNLDYCRSNIIDHFTCDYVPLLQLSCSETKL | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Membrane
Sequence Length: 134
Sequence Mass (Da): 15504
Location Topology: Multi-pass membrane protein
|
A0A6I3GSA5 | MKSIVVLNGPNLQRLGSREPDIYGTLDYTTLVSILEKHATELGVSLTAKQSDSESELISWLHEATDSGADVIFNPAAFTHYSYAIGDACKIHTESGAKLIEVHISNPHSREEFRKTSVVSPAATGVIAGFGIDSYLLALRQLTS | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Function: Catalyzes a trans-dehydration via an enolate intermediate.
EC: 4.2.1.10
Catalytic Activity: 3-dehydroquinate = 3-dehydroshikimate + H2O
Sequence Length: 144
Sequenc... |
A0A538CSG9 | MDLPTRSRALQAPAPHRRPARRAPRGRLGPGERMPPRGRARRQGDGALPSNRTAARQPTAHDEGARQPDDRADGPAHHSADRDAARRRGPPHAGGHGVLEGGARRRPRRRARPRRPVRRLRTGAALSPPLGVVLAGGAGRRIGGDKCTVELAGQPLVLYPIHALRGLCEQVVVVAKQDTNLPQLAGEAEIWIEPDEPHHPLAGVVHALRTASARKLLVLACDMPLVPEELLRALLKAADGAGAVASCRDIAEPLCACYTREALKGLEHFEPDARAIDVVDALGVAHVEWDDCNAVLNVNAPEDVIRAQALL | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytopl... |
A0A4P5RK42 | MSSTGKFEAEIAPLLLNFNNETEIIPAIAQDFVSKEVLMLAWMNREALKLTAATGTATYWSRSRNAIWVKGATSGHTQEVQELKFDCDADAVLLLVKQIGVACHSGERSCFHNPIDLKEKS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
Function: Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
EC: 3.5.4.19
Subcellular Location: Cytoplasm
Catalytic Activity: 1-(5-pho... |
A0A7C3UIU4 | MSEKPFVHPYIPNAAPATKEAMLRELGLQSVDEIYAEIPERLQFKGRLDIPEPILAERDLKRHVMELLDRNRSCVDFLNFCGAGCWQHYVPAVVDEVINRAEFLSAYCGANYSDLGKYLTRFEFNSMLGELLDLDGVANPIYDWGDVAGRAFRMARRITGRDVVLVPGHISPMRLAEIRTLCQPEELPTSTKIRFYEWDRATGMVDL | 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... |
E3I376 | MRLLVTRAEQDAAPFAGELRELGHEPVLQPLIELRALDFDAAELENTDALIVTSGNTLRALEQAGAIGGLARFPIYCVGDATARRARHCGLQKPLAVADTGEQLAAAIVAQAAPGTRFVHVAGEHLSFDIVGELTSHGMPSRSLAVYVMQAAEAFKPDIADMIERGTLDGVTLLSPRTAEIYVSLCHRHRLAECAKKLSYFCISETVAQQLRTLEPRGVYISERPNRKALLDLVR | 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... |
D1KG51 | FHSPMYFFLSQLSLMDLMLVCTSVPKTATSFLSGRKTISFVGCGMQAGLLVSLVGSEGLLLGLMAYDRYVAISHPLHYSTRMSQRVCLQIACSSWAFGTLDGLIQMVVVMTFPYCGSRVVDHFFCEVPTLLKLACVDTSLFETLLFACCVFMLLLPFSIIVASYVRILGSVLHMHSAQAGKRALATCSSHMTAVSLFYGAAMFIYLRPKRYRTPRHDKVVSIFYTVLTPMLNPLIYSLRN | Function: Putative odorant or sperm cell receptor.
Subcellular Location: Cell membrane
Sequence Length: 240
Sequence Mass (Da): 26723
Location Topology: Multi-pass membrane protein
|
A0A7N0U8K5 | MGISSSNNRRRVSYQQNPSPYPVANPYYYYPSEPYSNQSSQQGYGYPSYPPPLPAASYPSYYGGGLPFDACNYVSPVVVNRGGNYGGGAGFYNAGQMSQWGASGRVPVVMAHPAPPYVEHQNAKRVRSCVNVHKESLRLVGDELNPGHFLVAFVFDALQDGSITIQYFAKEEPYCRFIPLFPEACPPLRISFHKGLGQSFRQPPGTGINLGFFEPDDLSKPSPAEDVFPLVISAETYLPPDDLLGAYVPSSSPNTQITQAVFVRSYDDPFQVRVTRQILWIDGVRYELRELYGIGNAAGGVGDSDSSKDCVICMTEPKDT... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 367
Sequence Mass (Da): 40593
|
A0A7X7PMT0 | MDGEALRITVIGSGSWGTAFGRLLCRNGHHVTILTQTAEEAARLTARRVNEHFLPGVAIPEGIGFAAIGDADLHGVEVVVYAVPTQAVRQVAAWVAPRRPRAALQLSLAKGLELRTVRRPTEIIAEETGSAAAVLSGPNHAEEVARDMPSATVVAAADDRVARALQRAVTSDTFRVYRNADVAGVEFCGAAKNPIAIAVGMSDGLGYGDNTRASLITRSLAEVARLGSRLGAQFETFAGLAGIGDMIATCTSQHSRNRRAGELLARGHAPAQLQGIIEQVVEGIPTTYALHDLAGSLGVQMPVTENVYQALEHGRSAPDC... | Pathway: Membrane lipid metabolism; glycerophospholipid metabolism.
Catalytic Activity: NAD(+) + sn-glycerol 3-phosphate = dihydroxyacetone phosphate + H(+) + NADH
EC: 1.1.1.94
Subcellular Location: Cytoplasm
Sequence Length: 338
Sequence Mass (Da): 35814
|
A0A7W0PI07 | MRSRISLGTGSVSSPPMKSPYSRSVAIAIARNLPRRLRGGRRSRVGVGHGRDQRGVDPWAPGSRHRDEADSDDHGNRRTLLYGQDGWFEGWFADHEIDVLFALPAMVIATIFVSIPFVAREVVPTLREIGDDQEQAARTLGASRWQTFWRITLPSIRWAVIYGVIVTTARCLGEYGAVAVVSGRIQGETETATLRVQERYESFDLAGAYAISIVLALMAILLLVAMTVIRPREETA | Function: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 236
Sequence Mass (Da): 26120
Location Topology: Multi-pass membrane protein
|
A0A7V9D945 | MDRLAVGVIFGGRSVEHDVSIVTAHQVMAVLAALHHVVPIYVTREGRWLHSEALNDLGVYRRRTWDEVAGEAFIPPSTGRGGLYLPGGRLKRARSVPLDVVFPAIHGTFGEDGTLQGLLELAGIPYVGSGVPGSAAGMDKVIMKAAFQAAGLPVVPHVMVEAERLEADAGRTLDEVESSLAYPVFVKPARLGSSVGIGRAEDRTGLARALDVACRYDRRILVERSMEGCIEVNCAVLGGAGVEPRPSLCEQPVPWEQFLTFSDKYLRGGKQQASKSSGMASERGSIQASKSSGMASQERRLPAPISDRLTKTVQDNAMAA... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
EC: 6.3.2.4
Subcellular Location: Cytoplasm
Catalytic Activity: ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + phosphate
Sequence Length: 407
Sequence Mass (Da): 43... |
A0A6J1A0T5 | MLGTRRLPFPAFAFDFIHCSRCLIPFYLIVVLSFCVCVCGVPLIYSYLYLPFLFGPNVKKIAFADATYFIEVDRLLRPGGYXVISGPPVQWPKQDKEWADLQAVARALCYELIAVDGNTVIWKKPDGDSCLPNQNEFGLELCDESNDPSNAWYFKLKRCVTTTSSVNGEYAVGTIPKWPDRLKRAPSRALVMKNGIDLFEADTRRWARRVAYYKNTLNVKLGTPAIRNVMDMNAFFGGFAAALISDPVWVMNVVPARKPLTLSVIYDRGLIGVYHDWCEPFSTYPRTYDLIHVAGIESLIKLPGSSKSRCTLVDLMVEID... | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 382
Sequence Mass (Da): 43285
Location Topology: Single-pass type II membrane protein
|
G5JGZ8 | LGAPHDKYVAHPFISGSLEGYFTMDLVAAL | Function: Component of the transport system for branched-chain amino acids.
Subcellular Location: Cell membrane
Sequence Length: 30
Sequence Mass (Da): 3221
Location Topology: Multi-pass membrane protein
|
K8E1S6 | MKKKLIISGAVFLGLLTAGCTNSSATVASTTAGKVTQEELYQEMKANYGESTLQTMLIEQVLAKKYGDSATTKKVNAKFNEVAEMYGGTEAFESILVQYGYANGAAYKATIKQNLLIEAAVKDKTNLTDADYKELWENSLYFQTILVADEDTAKEVITKLDAGEKFKDLAAEYSTDTTTSENGGDAGFYNISTGTTYDTTVTDAAAKLNDGDFTKTAISTDAGFYVVNMVVNPTSTSKTWQDYQSELTEMAVTANLADSTFTTEILTTLLKAANVQIKDSDLENALSAYLTPTTTSSSAVTSDSSTDETTTTSTKDSE | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cell membrane
Sequence Length: 318
Sequence Mass (Da... |
A0A538CVA4 | MRRFAASRRPRRWRSRASRARRLGPTTRRRGCSAPWIGSRRWRRSSTRPTRTRSRRTRWRRFPARSWPERRGSICPRRDNAGVPRRVIAHCDIDAFYASVELLRHPELKGKPLVVAHSGPRSVVTTASYEARTFGIDSAMPAARARALCPDAIFIEPDHKAYREKSTEVWDLVRARVPVVQQVGIDEAYLDVTAFEKPLPVLRELVAEVHDRTGMFVSVGVGPSRLVAKTVSGSFKPRAFKALSREQACELFADRPTRLLQGVGPKTAERLAAFGAHTVGDLQRMDEELLIEHFGDNWGTYIKARAWFHDDSPVAAPGPA... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A538I798 | MTPVALVILDGWGLAPPGPGNAVALADTPVFDALEARYPHTMLKASGEAVGLPPGQMGNSEVGHLTIGAGRILFQDLMRVNRSIGNGSFFESEALVSAFARARERSGAVHLLGLVSYGGVHSQIDHLRALLTLAERAEMVDRTWIHAFTDGRDVSPHAAVSDLAELPADRVATVTGRYYAMDRDLRWERTARALGVILRGEGVHAGSAIEAVQESYERGITDEFVEPVVIDDRPRLDPEQDAAIFFNCRPDRARQLSERLIEA | Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
EC: 5.4.2.12
Catalytic Activity: (2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate
Sequence Length: 263
Sequence Mass (Da): 28559
|
A0A6G0A8K5 | MTDVDTTEPAGPAPPGGSQAPVAAAFIVAIAGGAGLAVTYALGGQNQLEGLCLALALGGIGTGVVMWSKRFMPVRYESEPRAPLQSTPEERAAFEADLAAGGGTFQRRRLLTWLLGGGLGFLGLASIFPIASLGPNPVPGLKSTPYRKATDDPDGLRLVDESGNPIHHTEPNVNGVITAFPEGSVGDEQAQTLVIHLREPMREPLPGQEDWGIKLSVDGSETEIIAISKVCVHAGCPVGLFEEQSQLMLCPCHQSTFDLMEHARPVFGPASRPLPQLPIDLDDDGYIVARGDFAEPVGPGFWDMYK | Function: Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechani... |
A0A3A5VRX7 | MLLCCFGTNMGRDYDSNRGHPLDIKNKLIIEKSNLSGTVKLPPSKSHSMRWITLASMDSNPTNIEMWEVGEDVQALIDCFINLGLEWDGSKFTGGLLSQPDCILNCKNSGTALRFLIGQIATCDFEVTLDGDASLRARSSLQLLNPLEISFEKHQESELPFSLKGPFNNQKVNIDVSKSSQFHSSLLLMAPRTSGFQIVTKGQAVSRKHSQLTWDLCKITGATEPGKPWLVNCPDVKIPADASMMAFAKLASLDVSNKPNEEDSIGHSFGNSSLRDSNDLITPMAAWMALGEGGIISDASHAALKESNRITKTVEMLSKF... | Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
EC: 2.5.1.19
Catalytic Activity: 3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate
Sequence Length: 394
Sequence Mass (Da): 42960... |
A0A7C3YL82 | MADEARKEALRYLFERVVRPLGYKFTPDEELADFLLEQEVKLEREHGAPFCP | Function: Catalytic subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
EC: 1.8.7.2
Catalytic Activity: [thioredoxin]-disulfide + 2 H(+) + 2 reduced [2Fe-2S]-[ferredoxin] = [thioredoxin]-dithiol + 2 oxidized [... |
A0A3D3Q8Z7 | MSSSGHLILVPWLFHWSILNNEQLNKTFDVALHLGTFVGAVVYFRKDIATYLGAWVRSIRQRGIRTTDERLAWYIIIGTIPGAVAGALAEDIIDKKLGQPWLIAIMLAVFGVLLYVVDRRARQIREIRDLRLGDVVFIGLAQAVALQPGVSRSGVTITAARG | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
EC: 3.6.1.27
Subcellular Location: Membrane
Sequence Length: 162
Sequence Mass (Da): 17937
Location Topology: Multi-pass membrane protein
|
A0A7M3WSC0 | VAERWLTRAMTLASMWVLYLVSAAFEMGMWTNDNFDGSWGAVVWFGITFFIGLGIYSIATHNSWGGWSNRSDDAPSGARTFWSAHWSQVMIAAAFLVAFVIRSQWYIIPAMNGYGTGDWDLTGGSDPWYMKRVVDYIMMQNAHLVFDADRFYPLGGINPRPPLFVWSIALLAMILEPFLTTPEDAVWWAMVSIPAIFGALTVFPVAAIARDHVSKPAAVVAAWLIAMMPGHISRSTWANADHDAFVMFFMALGFMWFLRAMASGGDERLTRSTDARPYSVLRAFGDVATHRRFAVANAALAGVAFGVVALGWKGFVVAPS... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A538HJK1 | MSRTTIALVGSTGSIGTQAIEVVDAEPDRYEVVALGAARSVEALAEQARRLRPRCVAIADESLVSDLRARVPAGVDVTAGAGALAAIATEADVVVNGVVGFAGLPVTLAALRAGRRLALANKESLIAGGPVVQRARATPGAEIIPVDSEHCAVHQCLRAGSVAEVRKIVLTASGGPFRGRTRAELASVSVEDALAHPTWSMGPKISVDSSTLMNKGLEVIEANELFGV | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 228
Sequence Mas... |
A0A2G8LGL1 | MKENWQQFCTSTVKSRFKSLVQFPKTFTCPEARCRVLLKYSDAAIDIKGADIVLFSNTLNWLTDETWKWAHGNRSEGQLWMFISRESPIHSPGLRPPEEFVDSTYHWIASYKFDSEIYLPFGFYEPFTNLNQERFDLTAFSVNKSKLAVWASDSCKSLQWDRVGFVNSLNDIIRIDKLGACGHRKKAIPWTNDLVLGQLFQPYKFSLSLENSCCDDFITENFWTALKFGSVPIVVGASYLQYSRIAPLNSFIHVDQFETMEELAVYLTFLDENDEKYLEFHKWRNLGSITSYNVDEKYVEPLTLETHCEIYRNI | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 314
Sequence Mass (Da): 36652
Location Topology: Single-pass type II membrane protein
|
A0A089N5K0 | MKNGQNVEYRNTDVYTQVNTTAALVAGVMETEVTIRDLSEWGDFGLGCTKGMQESVLLLDNQTYVNKVVKDDQKIGLFLLAFFEETNPVRLQQTMDLNDLRAYIDSALPTPNIMYAVKCKGKFESIQTSIPLSFQKPYPRVVPEMTDQSINVEVDNISGTIIAFWLPSFLSGINGGAGGLHAHFISDDRKFMGHVIDCKMTEGVLWIDAKHQLNLQLPKADPAFYEVDLNGNEAMSRRVSEWIKEGIGGKEILPGATIKA | 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: 260
Sequence Mass (Da): 28910
|
A0A662TAD4 | MIKIFVTGPPGIGKTTCVYKVFEMLRLYEYRVGGFITREVREGGKRIGFRIIELDEGLEDWLANIHGTSRYRIGKYYVFIDKLDSIINSIEKRIMSYDALIFDEIGPMELLSSKFNTFIQRTLNIRVPTVYTVHHKISNELNKRFNTRYENVLYILTTDNREGMPLIIWRALSKYLTRDTT | Function: Has nucleotide phosphatase activity towards ATP, GTP, CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower efficiency.
EC: 3.6.1.15
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Length: 181
Sequence Mass (Da): 21289
|
A0A6V8EEL0 | MDNENGTVSAKDPFYGLLAIPVTIAIMLAMMVAATWNAVDYEASDWNTLLMMTTVLMAGGLLGKAPRIIFEPVGTRPSLVSLGFAAVIGAVGMIHYYDGAALLGLAFSTMAIGVHLFDRSRRHEEEVIVVGIVAGFLYAIQVAAAGHGWSAEAVLATQGQYDIIDVNRAVTGSLFFTWWMISILSSMLIALALRGRLQEGGSGSWFNQLPAVLGKEFNPLYAGLGVWLAAHIFSLWHLKSLESADAIFLTQHVGFFWALFTGLIAMFVAFCWAEHWRTMGLIISLNWLLYSIGTWQSKAMFGLHEIGFLNGDLGGLSWFL... | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine.
EC: 2.4.99.21
Subcellular Locat... |
A0A7N0RE91 | MLCGVFEVMGRGGRRRRMGVSSGCGIGGFVVGLIVACMFVGLSGEEEQLRLPKFAVPKHYSIRLQPDLVHLKFNGSVEIQVEIVENTTRLILNAAVLDIAKSSISFHNSKKLFRPVKMDTDAESERITLEFGERLPLGIGVLGMNFGGNVSYDIQGLFRRTYTFKGEERNMIATQFESIYARRCFPCWDEPAFKATFSMTLDVPSHLTALSNMPVLEEQINGLSKTVYFQKSPLMSTYLVAVAIGQFDYVEGHSSDGIKVRVYCPIGRTSEAVFALNLGVRALDFFREYLSMPFALPKLDMIAIPDFPQGMENYGLVIYG... | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Membrane
Sequence Length: 920
Sequence Mass (Da): 104368
Location Topology: Peripheral membrane protein
|
A0A0F2IVB0 | MFDTQVKRIHEYKRQLLNALHVVSMYNKIKQNPNADFQPRTVIFGGKSAPGYFMAKLIIKLINSIADIVNNDPDVGNTLRVFFIENYSVTVAQRLIPAADLSEQISTAGMEASGTGNMKFALNGALTIGTLDGANVEIKEEVGDENIFIFGLTDTQVNALKTSGYNPRHYYETNFELKTIIDMISGGFFSHNDRNLFKPIVDSLLNHDTYLVLADFKHYVDCQNTVSKVYKDQDKWTKMSILNVANMGKFSSDRTINEYAKDIWNIKPNKINK | Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
EC: 2.4.1.1
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + phosphate ... |
A0A6L5FZI1 | MPGWGLRRLFGGGAVSLLEWGVDGSPAAMAPPTGLVERVWARDPSAWGPGEDDPASRLGWLDLPATMQEQIDDLTAFATEATADIDHAVLLGMGGSSLAPEMLAQIYGGRGRISLEVLDSTHPAQIAEVTSRIDPTRTLFLVSSKSGGTIETMSLYRYFRRLAPPDRFAAITDPGTSLQALGEAERFRRVFINPPDIGGRYSALSLFGLVPAALLGIDLGALCASASAAADECRKDGGSNPGLAIGAALAEWADAGRNKLTFRTSADLVSLGDWAEQLIAESTGKEGKGIAPIVGEPVLEAGYGPDRAFAHLSRDASPVE... | 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: 510
Sequence Mass (Da): 53211
|
A0A6L5G2V9 | VTYVGRLDGALVALPWSEGSFLREVWDTQFYMLDYHANLTTLHGYQSPPWSWPVVKRPVSYFFDSSGGTYREIMAFGSPFVWWSSLLALVFVGYRWIRARSIGSPEGVILGAFFFTYVPWLVQPTGRAAVFLFYLLPAVPFMCLALAYVAVRIGDSTEARLAIGIFAAATIASFVYFMPLALNRPISEDQWRSRIWFENCTKPEGYEGSPNGWCWI | Pathway: Protein modification; protein glycosylation.
Function: Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.
Catalytic Activity: a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+)
EC: 2.4.1.109
Subcellular Locatio... |
A0A2G8KJ52 | MNRAKYRHYKLEGYEELLRMGIWDFLINLSGADLPLRDVDDVSAMLAAYRGYNFMRQNGNWNDRSGKATDYTVWYGCGGHVYNISKRGQRPEWSDMHSASQWAVLNRKYIDYVLNANERLDKMNYLQFYSMTCIIPDESFFISMMKISPFRNTFIHNNMHHLKAFARRDDKGFCRHTDDIDFCGQGPGTIVAADSNNLHLMALNFFFSRKYTGDPEEKAG | Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.2.26
Subcellular Location: Golgi apparatus membrane
Sequence Length: 220
Sequence Mass (Da): 25681
Location Topology: Single-pass type II... |
A0A4D6Y4C4 | MQILFYLLATCSIISTLLTIFQKNPIYAIIYLLCSLLCISSILFLFGSFFAASVQIIIYAGAVMVLFIFIIMMLNIKHISDLNLTYFKKIYLFIGLFIIFIILKKTLNPIFNTFNNKNIHISIVDTQLIGGNLFTNYIVLVELISILLLSALIVSLYIEKNLF | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy i... |
H6Z006 | TLYFIFGIWAGMVGTSLSLLIRAELGXPGSLIGDDQIYNTIVTAHAFIMIFFMVMPIMIGGFGNWLXPLMLGAPDMAFPRMNNMSFWLLPPSLTLLISSSIVENGAGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAINFITTIINMRLNNLSFDQMPLFIWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILXQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A0N0JVG4 | MPDIDDAAPAQSAAAGTDFARRIAHLDMDAFYASVELARRPELAGLPVIVGGRGDPESRGVVTTANYEARKFGVHSAMPMAKAVRLCPQAVFLPVDFAEYRRVSRLFKAAIIEIAPVMEDRGIDEVYLDLTEHEEPTRVLGLALKAAVKEATGLNCSIGIAPNKLLAKIASDLEKPNGLTIIRTQDLATRIWPLPARKINGIGPKASEKLAALGVHTIGELAACDPAWLVGHFGKSYGAWLHRAANGIDERPVETESERKSLSRETTFDTDLHPVRDWQALARLLAELSREVAADLAKHKLRGRTIGVKVRNDKFEIATR... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5'... |
A0A2N0KVF4 | MSITGLGFILAAYLWGGIPTSFLVARYRFGIDIRNYGSGNVGASNALSQMGSVTGILIGTFDCVGKGILPVLAARLLDQSLAVQVGVGLAAVAGHNWSPFLKFTGGRGVATAIGLLLVFWLWPDWLILGIVLGGLGRLIFKDTGFWTFVSLIALPVMAYLFQRPTEIMVMSILIAVLLFAKRLTANWEPPDRRQGRYLVYLYRVLWDRDVARKDQWTQRLPDVPDKF | Pathway: Lipid metabolism; phospholipid metabolism.
Function: Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
Catalytic Activity: an acyl pho... |
Q9G0H1 | MSSFSMDYEHKKHQPCQSCGSSDGAYPYEDGIYCHVCKTKTFNDDGDTQVTEQKTLPPIRGKIMAVPSRGLNKATAEKYRALTSDDKISLLYTTEGKVTSFKERGLSEKTFKFNGPAQTDLFGQSAFSKGGKSVTITEGEFDAMAAYQMLYMSEPCVSVINGSSGAVKDCKRNYEWLDSFEKINIAFDNDKAGQDAAMAVAELFDPRKVRLVTMTLNDPNDYIKQGRERDFIDAHKKAAPFTPDGIIAGSSLYDLVSTPPEYDCVPYPFSGLNRMTKGLRTGELITFVAGTGVGKTQVMREILYSLIQQDKGNVGTLFLE... | Cofactor: Binds 2 Mg(2+), one of which is catalytic.
Function: ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination. The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ... |
A0A7K0VJP0 | ELANVGVEQALNHPTWKMGPKITIDSSTLMNKGLEVIEAHELFGTPYDQIDVVVHPQSVIHSMVEFTDGATIAQLSMPDMRLAIGYALAYPNRIATPFGRIDWTALARLDFEAPDVATFRCLTLAYAAGRVGGSAPAWLSAANEEAVDAFLAGRIRWSQIAEICDAVLQQHHETTDITNMTVDDIVQADALARRIAHEELAR | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6.
EC: 1.1.1.267
Catalytic Activity: 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + H(+) + NADPH
Sequence Length: 202
Sequence Mas... |
A0A1E3GPQ3 | MALMKKNSCYLRQDLAQAWADKPVFDAVANIDGEIFRDKEGRRTLRFELNDRSYFLKYHQGVGWTEIVKNLLQMRLPIISARNEWQAIHFLEKHGIETMTLAGYGEKGINPATLRSFVITDDLVNTMSLEYVGEQWQQRPPSFATKQALIRKLANMAGTMHKNGMNHRDFYLCHFLLDERFAEHNTFEDKTPVYLIDLHRATIRHKTPKRWQIKDLGSLYFSASRVPLTKRDKLRFMQIYSGLPLRTLLKEQADLWREVQHRAQRLLAE | Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Function: Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core.
EC: 2.7.1.-
Sequence Length: 269
Sequence Mass (Da): 31638
|
A0A2E6LFZ2 | MKILKLNGERKTLSQSEINEFFNSIKLKFTKTTFEFDTVKINVQPENWVEAHEILKNEFKLNFFNWLSAVDWDNEVAVGDPPKEQVTPMFEIMSCLSQTDSNNLVIISTNISKEIPDIESLTPVYRGADWHEREAYEMFGINFLNHPNLKKLYLPDGYEGNPLLKSFELISREVKPWPGDVDVEAMPEDKVATKEEK | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 197
Sequence Mass (Da): 22846
|
A0A3A5VXH4 | MEPITVVLIGLALVVCAYMAWNIGANDVANAMGTSVGSRALTLKQAVIIAAVFEFSGAFFAGDAVTDTVRKGILTVDFADGTVDAVLSQDIAFGFIAAMMAAATWLTIATRMGLPVSTTHSIIGGILGVGLILEVKHSTSLIDWEVVQKVVMSWVASPLMGGLIGFFSFMIIKKLILESENPIDRSRWLAPALAFPTFFVLGLALQFKALKGFISRAASEGWIENKYDWLPVKEDGVFDPWASNAWIPINSILLAAFIGAVSSIALYMVLRRIDINEEKRGFRGVERIFVWLQIITAAYVAFAHGANDRSNAIGPMAAVW... | Function: Potential transporter for phosphate.
Subcellular Location: Membrane
Sequence Length: 392
Sequence Mass (Da): 42154
Location Topology: Multi-pass membrane protein
|
G8DLJ5 | TLYFIFGIWSGMVGTSLSLLIRTELGNPGSLIGDDQIYNTIVTAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGTGWTVYPPLSSNIAHGGSSVDLAIFSLHLAGISSILGAXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A223DNV5 | GSLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQLSFSPTTLWALGFVFLFTVGGLTGVILANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNQTWLKTQFFIMFIGVNMTFFPQHFLGLAGMPRRYSDYPDAYTLWNIISTIGSMISFLSIIFFILIIWESMISQRLVMFPLQLN | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A6J1B422 | MALKCAPNWVCSRMPHSHLGTPDLGSTRSRIVLEVRPPKWKCCALGFSAPRASSAIEGKPYGTEVETFQTGKTDQAQDTESKEFHKDLSLLPKPLSTTDLSTYDDDGSNIRVAYKGMPGAYGEAAALKAYPNCETVPCEKYEKAFKAVELWLVGKAVLPIENSIGGSIHRNYDLLLQHRLHIVREVHLAINHCLLALPGVRMEEMDRVLGHPQAFAQCEMTLSNMGFIRINSDDCASAAQIAVLTGARNVGAIASARAAEIYGLHILARKIQDEEHNITRFLVLAREPIIPKTDKPYKTSIVFSLEEGPGMLFKALAAFT... | Pathway: Amino-acid biosynthesis; L-phenylalanine biosynthesis; L-phenylalanine from L-arogenate: step 1/1.
Function: Converts the prephenate produced from the shikimate-chorismate pathway into phenylalanine.
Catalytic Activity: H(+) + L-arogenate = CO2 + H2O + L-phenylalanine
EC: 4.2.1.91
Subcellular Location: Plastid... |
A0A3A5W2G4 | MDSMWRCDEMDMYNHSWLGRTMTVTASTDSTLVGRQGLVVDETRNTISLVDGENTLVLNKASITFTLGDSDVAIHGAMVGQRPEDRIHRTYRKA | Function: Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
EC: 3.1.26.5
Subcellular Location: Cytoplasm
Sequence Length: 94
Sequence Mass (Da): 10548
|
A0A7V9IFG4 | MSQAQATMTPSSSHSRIRNSCSRPGTEKRAQGQVADVVRKWRAADLAPGPCDELLHAPQVGETLVVPPAQHRRSIRSEVMNDREIVELHIVSDSTGETAARLVAALEAQFPEQPFEEIRHPRVESIDDLKLTVSRAKGRPAVMVYTLVDREMREAMRTLCRSARLHYCDLLGHPIESIAKVSGMAAQMTPGARPPLDSTYFKRMEAIEFAVKFDDGVGTGLRDADVVLVGVSRTSKTPLSIYLGYLGHKAANVPIVKGITPPPELYEIDPLKVVGLTIDAERLAEIRTARVRGMGTTNRRYAELLEIYSELEEADAIHRR... | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
EC: 2.7.11.32
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-... |
A0A537W4T8 | MRRCLGKIGLSLLTAVACACAAAVPAAGQIAFAPCADSNNFACGHLAVPLDPTGLTPGTLTLAIRRHRAPVEGGSSAVIALAGGPGQAAIPLTEAFLELVGPVSATRDLIVFDQRGTGLSHPLACRPPKRRRHRPASLGQAVVQCAHGLGPTRSFFTTPDSVADIEAIRRAGGYDKLVLYGTSYGTKVAEQYAQAYPAHVEALVLDSVVTPNGPDPLNRSTFAAVPRILHQLCRYNECLHVTPHPVADLARVVARMRRGSIVGRLIDRRGHGHPESISSDDLVGILLQGDFNPLLRSEFVPAVRAAADGDDAALARLLAR... | Catalytic Activity: Release of N-terminal proline from a peptide.
EC: 3.4.11.5
Subcellular Location: Cytoplasm
Sequence Length: 684
Sequence Mass (Da): 70802
|
A0A4P5RKM2 | MAAKRKSAKKKIAKKKIVKKVAKKKAVKKTAKKAAKKTASKGGSKVTLGGNPVSTSGKLPKKGAAAPSFTLTTGTLQEISNKDLRGKRVILNIFPSIDTPTCATSTRTFNSLASSLNNTEVYCVSADLPFAQGRFCGSEGLANVKTASSFRSNFGKAFGVSLTDGVLKGILARAVVVLDEKGKVLHSELVSEIANEPNYEAAINSLK | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
EC: 1.11.1.24
Catalytic Activity: [thioredoxin]-dithiol + a hydroperoxide = [thioredoxi... |
A0A7N0V2L2 | MALRRSLPHRLAVSEPHLHQPSSLATSNTEQSRSYITSPDPAPNPTFFQRLFPRRSLYQSSSRLPELFSIPVGDKLREKLKRVNSVSVNDRIRWLAPPPPVTDAARVSVDDARRLLRLAQVERMKLALRKIERSAISYGEYVRLCVEECGDEEQGREFSKLMDATGNVIVLGNTVFLRPEQVAKTMETLISQSISTAGDPRRAKLEQMEAELSAIDEKARALVRGEMYCGLGFVILQTLGFMRLTFWELSWDVMEPICFFVTSMHFVAAYGFFLRTATEPSFEGLFRRRFEVRRRRLMAARGFDFLKYEELRKVVTGGVK... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes a pore-forming and calcium-conducting subunit. Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cel... |
A0A1C9G6P8 | DDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWMLPPSLSLLLISSLVENGAGTGWTMYPPLASNIAHGGSSVDLAIFSLHLAGISSILGAVNFITTIINMRSNGITFDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTS | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytoc... |
A0A538N7E6 | MSSTPSITSRLAVLGYAVIAYGAFLLSVGWAIGFLADRGAPTSIDGAATRPAWVALVIDAALLLAFAVQHSVMARAGVKRRLIRLIPAPAERATFVLTASLLLFALFGWWQPVSAVMWHVGPPWSAAMWMVQAVGWVIVAWSTFMVDHTDFLGVKQAYRHLRRLGYRPPDFTRRWLYAWCRHPMMLGLVIAFWVTPRMTIGHLFFAAAATAYIAVGIRFEERDLRAQFGAEYREYASRVPALMPAPRSLPRPGRPTTEERTT | Function: Catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS).
Catalytic Activity: methanethiol + S-adenosyl-L-methionine = dimethyl sulfide + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.334
Subcellular Location: Membrane
Sequence Length: 262
Sequence Mass (Da): 29230
Location Topology: Mult... |
A0A6I2WWH2 | MAISRVKIIGSGLIGTSIALALAEKGAQVAMVDRSPASAALAQALVGGKGDLTGKFELTVIAIPPAAISDEFLAEISTDVYSTFIDVASVKSNLLSRVASIDGLAGRFCSTHPMAGREVGGPASARADLFQGRNWIVLNGSTLEADRLAAVNELISICGARAVVMAPDEHDRALALLSHLPQVLASILAAQLKDVPVEILDLAGQGMKDTIRIAGSDPKLWREIISANSDEIAPLLKAVRNSLDEAIVNINDPAAIEALIESGRNARSRIPGKHGGVSRNYSYIPIVIPDKAGQLGALFNECALADVNIEDLSIEHSPGQ... | Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Length: 357
Sequence Mass (Da): 37299
|
A0A2H0IK24 | MNKPFLVGITGGIGSGKSTVCRIFETLGVPVYYADDRAKLLLKEDEVLRNEVISCFGKKSYLSNGGLNRVYLADRVFKVDSELQKLNSLVHPAVARDFQRWAQLNEHKILLKEAALLIENQTYKSMNYLITVLAPEKLRIERVLMRDAHRSKEQIRDILSKQVDDELRKSKSDLLVHNDGNRLLVPQVLKAFEKLQELALAKEGNAI | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Le... |
A0A925KMD1 | MSPERLFPHSSPPHSSRTVLAFDFGLKRIGVATGDSQLRIAHPLETIPTSQRFERIARLLEEWEPALIVVGLPHAEGDREKDEREITRACRNFAHELRARFGVEVEFVDERFTSSEAAAALRDAGVAGIRQKPLLDQVAAQQILQSYFDAAPRR | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 17314
|
R7QPI9 | MHPRASRQGHSVETADSDVAVRATNDDALESKYCAMHAGYFEDAFLDALASHLLRDDVAPPSRPPLINRGTAARVAFKSDLIHALLGAAWASSETVQIVSLGAGYDSLPFSLFEMGQSMTKMSLHYVELDFAPIVQAKAAAVEAQLVLRGLFRDIMTDGESLQGIVKGGTQSRYVLSAFDLRDTPRISDVLRATGLKCNCPTIILAEIVLVYLDPVISDAVIREIGHFFTRERAFVNIEHSHPHDSFGLQMVKNIAARGSPLLGISKYPTLAAQKSRFVREGWPCVEALTMLQGFQRKFSTEEALNLNRIEHLDEIEEWD... | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
EC: 2.1.1.233
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl es... |
A0A0G1KKE3 | MTKSFWLYSIIVSSAIRIPAKIGFVHKVTVSTEEVKKIAKLASLKLPDNEIELFSQQFTETVDVINQLNEIDTSTVPETYQVTGLSNITREDEVDENRVLPQEVALREAKLIHEGFFVVPRVIDTDETESVI | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
R7FKL8 | MEKFRIGFSVDIHQLSEGNGIYVGGIYIPCNKKSVAHSDGDCLLHAIAESILGALALGDLGKFFPPSDESIKGIASSKIAEFAVSKMFEQNYKINNIDCSIVLESPKLAKYMDEIKTNIAKLLFTDITNVSIKAGTNEKIGELGQGKAIQCFSTVMLVSDNK | Cofactor: Binds 1 divalent metal cation per subunit.
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP... |
M3HVD3 | MSDLDQQLRIFRDQIDSLDREIVKAIQTRAEFASKIGEIKRERNEPVFRPDREKEVYEKIKSLSSGLLPDKVMLAIYREIMSGSISVEKGLEVGYLGPAGSFSNQAVRTRFGASVNALEFNSIPDVFRAVETDKIDYGVVPVENSSEGLVNSTLDQFLISDLLIYSEHYLRINISLLGFEHDLSKIKSLYGIKIANSQCKNWLAANLPHVEIVETSSTAKAAQIVAEKKRLVRPLPPPLRRKFTGSV | 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): 27726
|
A0A1W1VC00 | MFLQWPGREAVLRVPIEGQDREAEETLAEAAEILSLLNAAHRAVQQGGRGAERLPPAARGRTPGTCHPHRAGRHLRSAGRDFRLRQCRPRGGRAARVSLAPMTPAAPPSFAQAVTERTRRLQTRLCVGLDPRSGTYRDAAHLRSHTLDVLEATAPYAACVKPQLAFFEALGLPGFTLLEEVCAAARTLGLPVILDGKRGDIGSTAEAYAQGWLSGPHAGDALTVNPFLGFETLTPFVGAARANGGAIFVLVKTSNPDQADLQGSGISERVAAEVARLGETEGGEYASVGAVVGATHPADLGHFRALMPRALLLLPGLGAQ... | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2.
EC: 4.1.1.23
Catalytic Activity: H(+) + orotidine 5'-phosphate = CO2 + UMP
Sequence Length: 373
Sequence Mass (Da): 39060
|
A0A386HTB2 | MGLLTPDFGLFFWTLLAFLLVLFILGKFAWKPILKMLDERESTIADSIATAEKARNEMAALKSENETLLQQAREERTKMLKEAKDASDKMIADAQSKAKSEYERIVADAQSAIAQQKNAALTEVKNKVGSLVIEVAEKVLRKQLADKTEQESFIADLVSDVKLN | Function: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Subcellular Location: Cell membrane
Sequence Length: 164
Sequence Mass (Da): 18320
Location Topology: Single-pass membrane protein
|
A0A8H3EG82 | MSVEQLTSAIALGRQIAQGELDLAELDNKSLALRGKMKYRGAQRTRKREHDSGDLEDKKIRLGEAGAKGTKATTKKVCQSDIRVSMIRATSTSEPGKQLNLPSPPATPAPIDVELRRLIDSSELSFFRQRVLLALCQVPSGRFTTYAAMSEYLNSGPRAVGNALRNNPFAPRVPCHRVVASGGGIGGFGGEWGAQGKHTPEKVKLLRQEGVRVSKKGERVLGQAQQVNELYLTVHTRGVGNAVGTLGFADELIALVACPFWGVISDRIGVRAVCVLGYTIIALALVLFVQAQNVFPQLLFARLFFSIGGAASSTMVTAIL... | Catalytic Activity: a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]
EC: 2.1.1.63
Subcellular Location: Membrane
Sequence Length: 778
Sequence Mass (Da): 82770
Location Topology: Multi-pass membrane protein
|
A0A962ETL4 | MKQNSRPLSPHLDIYKFQITMAMSIFHRITGVGLYMGMALIAWWLVAAATSNKALNLVYWVLGNWFGQLILIGFTWALFHHLLGGLRHFVWDTGKGFDEKSRFGFAWFTLIGGLVLTALVWVLFVWL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 127
Sequence Mass (Da): 14575
Location Topology: Multi-pass membrane protein
|
A0A7X9AFC8 | MTGTAGLLRTPLYEVHRREGARIVEFAGWEMPVEYTGIRQEHQATRTGTGLFDLSHMGEIEVTGPGATAYLNYMVTNDVERLEPGQCLYTCMCGADGGILDDLLVYRFPDMQGGERRFWLVVNASNRLKVVEWMENHLSGDAQLNDLSLDTALLAVQGPEAQEFLQPGTEANLEELGYYHLLETKVAGIPAVLSRTGYTGEDGFELYVAWERVEELWNSLRQVGGIVPVGLGARDTLRLEAGYSLYGHEISELTTPLDAGLGWVVRWSKPDFLGKAALSRQKEKGARTTIVGLEMLGRGIPRQGYPVEGPEGPVGVVTSG... | Function: The glycine cleavage system catalyzes the degradation of glycine.
EC: 2.1.2.10
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + (R)-N(6)-(S(8)-aminomethyldihydrolipoyl)-L-lysyl-[protein] = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NH4(+)
Sequence Length: 372
... |
A0A6S6U1J7 | MNITATKTDAANVLVVATIDATDIEKNLNKAAKQIAKTASVDGFRKGKVPIAKVKQMYAEQLQQDSENQAIQDVLEQAKKDLDINPADIISDPVFKKYDKTDGNIETEMVISLRPTVEAEGYKDLAPTYDEPSIEDAEIEEKLKTLLAANAPYASIEEKRAIQNDDQVNFDFLGKVDGVEFDGGKAEGFDLVVGSGQFIPGFEDQMLGLNIEETRDLSVTFPEDYQSDDLKGKEAVFTVTINDIKTKTEPELDEEMIKKLIPNEEGATADTVKEKIAEQIKSEKVSKLYNETLKPALIEALVEKYDFALPQNIVDQEIDA... | Function: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
EC: 5.2.1.8
Subcellular Location: Cytoplasm
... |
A0A0A2T7B9 | MDTKLHLAKELYELGSLQVSYDQPFTWTSGILSPVYCDNRLTMSNVKVREQITEYFASYISTYYPDVDVIAGCATAGIPHAAWVSSQLELPMVYVRDKPKGHGKENQIEGRVQEGQKAVVIEDLISTGKSSLNSVRALKQSGVEVVGVIAIFSYGLTTSERAFREENIPYVALTNFEVLLDYMLQANIITKKQHNHLLTFKEDPATFSLTYQQ | 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... |
A0A0C1V0H5 | MSDWEIVVGLEVHVELATETKLFSHAPNRFGDEPNTNITPVCLGLPGSLPVLNRRAVELAMTIGLALGCDIRPSVFHRKNYFYPDMPKDYQVSQYDRPICADGALDLPNGTRIGIERAHLEEDAGKTTHIGGSDGRIHGAEEALVDYNRAGVPLLEVVSRPDIRSAEDARAYVEELRAILIATKASEARLEEGSMRVDANVSVRPVGSQELRTRCEIKNLNSLRSLQRAVTYEAERHINLYEAGEEPVQETRHWSEEGRTHTLRSKEEANDYRYFPEPDLVLLDPDPEWITKIATAMPELPAQLRKKIVAEAGVDIDTAA... | Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an ... |
A0A4R4WLR4 | MRQVQAEGGTPVGSPRRRLFAVLIVLAAVIYAADLVTKTVALRTLEGEAPLVVIQDVLQFRVIFNPGAAFSIGTGMTFIFTIIAAGVVVAIVRTARKLGSRAWAVTLGLLLGGAFGNLTDRLLRYPSGIGRPTQFQGHVVDFIEVFPGHFPVIDYFPVFNIADSAIVCGGILAVLLAWRNVQIDGSKEVAGDD | 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-, ... |
A0A8C7FGW0 | MSCSLSPVPLPLFLSPSPVPLSLSPVPLPLFLSLSGSSVSLSCSSTSVSLALLFPCFSLLFPCFSLLFLSLSPVSLALRFLCLSLLFLYLCFSRSLLFLCLALLFLCLALLFLCLALLFLYLCVSLLFLYLCFSRSLVPLSLSPVPLPLFLSLSGSSVSLSCSSTSVSLALLFLCLSLLFLCLSRSPLPLSLSLSSSSVSLALLFLCLSLLFLCLSRSPLPLFLSLSCSSVSLALLFLCLSRSPVPLSLSLSCSSVSLALLFLCLCLSRSPVPLSLSPVPLFLSPSCSSVSLSIYAPPPLSHPLSTGGLQVSLVKMRSHI... | Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 443
Sequence Mass (Da): 47727
|
R7Q7V5 | MVRVHVGTTLPFPSPPHPIRSTILTTMSPFSPSLLSTTRCFSCKIDRYTHTSPTLGSLPATFSVILPPTATAAIYWLSGLTCTDQNFVIKAAAASHAHEHSVAIICPDTSPRGAGTPEEDDTWDFGTGAGFYVDATTEPYKKHYRMASYVVHELPLVVKEVLGDKVGEAKAIMGHSMGGMGALSLALRNPGLYTSVSAFSPIANPVNCPWGEKCYSKYLGENREAWGGYDPSVLMKKRGEPLVSRILVEQGGADEFLEKQLMTNRFMEACTEVGQKVTLNMAEGYDHSYYFIQTFIGKHVEFHAEQLRKAGKTSSGGV | Function: Serine hydrolase involved in the detoxification of formaldehyde.
Catalytic Activity: H2O + S-formylglutathione = formate + glutathione + H(+)
EC: 3.1.2.12
Subcellular Location: Cytoplasm
Sequence Length: 318
Sequence Mass (Da): 34633
|
W7USH2 | MRIGIYGGSFNPVHNGHIHLAETAVAEFGLDRLYLLPSKKSPHRSSAEYAPDEDRLEMLRLASRHNEKLFVSDYEIKSDRVSYTIYTVEHFRREFPDAELFLLVGSDMLLSFDTWYRYEQILENVTLCVVSREKGDLPELRKKAGELGKIGKILVSETAPTVVSSTEVRKKIAKNKDFTCYLDENVVQYIRLKGLYSVRGEGELLYNPDDKKKYLKAHLSAKRFAHSMNVAAECRKLAEKYGEDPEKAYFAGLLHDICKELPDDEQKALVLESGYTVCREEMETRSLWHGIAGAYYIKKEFGVEDIDILNSIRFHTVGRA... | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide... |
A0A1X7H1C0 | MKSIFNKIRYYFEKQKLFNRVSLEQSNFSILDTETTGLNVSKGDKVISVASLKINNFKIQEDLFLDELVNPQIKIPEESTMIHHIKDEDVRDKPTLIEIEDKILKFLKKSVLVGHNIDFDINFIKNNAKGTNLANRMKVIQPIDTIFLTAGLYPDLESYELSNLCEHFNIQTDDQIRHSALGDCRITARLFLFLLNKAKDQGVNNIAGLVKLCKRGLSLHHIIKNAKNIH | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)... |
A0A8I3ZZ32 | GGGGLAWLGLAWPVRARAAAAPAPCPCSTGRRRRPSPAVTARPIRFQRTSATAWRRRKRRRRRRAAGLGQGLAEAVARGALTAPSRGFCSWGSGAVASPPSRSFYLTSIYDHSIFEAFSKVVQKLIPQLPTLENLLNIFISNSGIEKAFLFDVVSKIYIATDSSPVDMQSYELCCDMIDVVIDVSCIYGLKEDGSGSAYDKESMAIIKLNNTTVLYLKEVTKFLALVCILREESFERKGLIDYNFHCFRKAIHEVFEVGVTSHRSCGHQTSASSLKALTHNGTPRNAI | Function: Guanine nucleotide-binding protein that plays a crucial role in the cellular response to amino acid availability through regulation of the mTORC1 signaling cascade.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Subcellular Location: Cytoplasm
Sequence Length: 288
Sequence Mass (Da): 31617
|
A0A956TCZ7 | MLARLPIRVSLPVLMTIPVLVAVTLLSLVVAIYGQQAVESLSQESLSQVHRQIEHQLRLLMDEAEQVSALDRDMVHRGVLDTRDLGAWLPTMVQQTQVFQRISSVSFGGADGRAAWLSRYPDEKMRGFGYKKDGQARDVIMTPLTPEGELDTPRAEQYAYSIASRPWYQQAIASPHPTWTTPYIWVRRHRPAPSVGMGFVCQVTDRAGKFLGVIDIEVTLHDLSAYLESLQIGRHGIAFLMDQEHHVLAISNGELVTNSKDELISAEEAHDPRVVLAARALEGHDLTQEFRSQFWHDQKEQLLVVTPFRRTGLNWRIVTV... | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 752
Sequence Mass (Da): 83733
Location Topology: Multi-pass membrane protein
|
A0A9D5GFI5 | MTATRLFVTTNGPGEVMGWVRPFLRRIFARDPTSKVTVVLLPCAYASGHETQALEKMFPSAAVIGPDAYARFLIGRQTAGMQRGNGVLQYLGGDLFHAITIARRLELEPMTYKFTKRSYANRFQRFFALDERNAQQLRNEGAPPDKVRVVGNLVYDAVAESLQRPPPPPGEGSGVCILPGSRPYELKFLLPFFLSIARELVRLRPDVPVSFVVSPFSSDDELRAGIEHAGDPHLFGTAGRFDAARDVIHVDGCQFSIDRSMDYRSMAQSQLVISIPGTKCIEAAVLGRALLVTVPTNRLDELAMNGVAAYLHRIPLIGRP... | 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... |
A0A936N935 | MTRWRLDVAYDGSGFRGFAVNIGIRSVAGELNAALGRMCGHDVTVTCAGRTDAGVHARGQVVHFDTDKEGLEAARLMRSLNRMLGPEIAVTDAQIVPTTFDARFSATWRRYRYSVVTSVWVDPQVARFVWHREGELDPSPMATAAQAFVGRHDFSTFCRRTPPAPGQVERSRVRNLHEFDVRCDGPHRLDFWVLASSFCHHQVRSMVGTLVQVGEGRRNVDSVARALESLDRQQCGPVAPAEGLTLWQAGYG | Function: Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
EC: 5.4.99.12
Catalytic Activity: uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA
Sequence Length: 252
Sequence Mass (Da): 27969
|
A0A9D5GC98 | MSGETRTSVTTNEKLLLIDVYALVYRAFFALPPLNTSSGQPVNAAYGFQRMLQRVLNDEKPTHVVACFDAGIPAERFEAVPEYKANRSETPADLRPQFALVRRILEAYGIPIIEVQDEEADDCIATIVTQATARRLDSAVVSGDLDLLQLVNEHCTVVVTRRGISEMARYDAAAVHERYGLRPEQLPDFRGLKGDPSDNLPGVPGIGEKTAAKLIAQFGSLDALLANVDSVSPQRIAELLRAHADKARSCRDVSLAKRDLPIELLWDRWRFEPPSAERMAQLYSDLEFKSLLSRLSTPAFAGAAGDSEMGAALSMPAAAF... | Function: In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 913
Sequence Mass (Da): 99006
|
A0A950L1V5 | MALRQIVLSRAAGPHDAADRIGGDADRVAPAPRLRAHAAAVERHALNRRPRRIGLDAGVARRADAHVERRAAHRHRAAGVVGASAGANRRDLLRRAALRAGAVRDAVDAELRRDEHEAAAVRDALRRRVVDRRERRRRSRGARAFGVRHDRDRRPFRPDDQVAVRERGQLARAADLRDRADQEAGRNVQVRIGGRRRRNARRAGRRRGRNGGRRRGRAGRAADDPHYDTGRLIVAARRRGRAAAGACGERGGKQRGAGERSEKLVHSQRIAVIDYGGGNVGSLLAALERRGASFALTEDPREVVSAGAAILPGDGAFGAT... | 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 HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthe... |
A0A7C6LZX9 | MKLEDLSLKQKVGQMLMFSFHGTEYNEQLDFLLNDLSIGGVILFKRNITSLKQVSKLNSKISKDKKVQPFIALDQEGGPVQRIEAGITPLLAAMGFAACGKDPYELYKQAGRDLKHLGFSINFAPVADVNNNPYNPVINSRSYSDNPKEVAKFVLRASQGFMDAKLIATVKHFPGHGDTSVDSHLGLPIVSKSLEEIEKIELYPFKKAIENKANGIMMSHIVYKCLDEKNPASLSYNIITKLLKEKLGFKGLVVTDSLTMKAIWDNYSIKEIVKKGVLAGNDILCFCGKADLEEQQEIYHTFVSLVEEGEIPIARVDEAV... | Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
EC: 3.5.99.6
Catalytic Activity: alpha-D-gl... |
A0A3N5FKI4 | MPAPTVYRLFHAGPIAAGATLRLDAETSHHALRVLRLGAGDTVEVFDGQGRRCAATLLDADPRGATVVAGEPADARTESPLAVGLAQALPAGDKMDWVVEKAIELGASAIQPLFSRRSVLKLDEARAAKRLAHWRRIAIAACMQCGRDVLPPIAEPMPIERWLMRPGGPGRPGSRGERAASASGSDAPLRLLLSPRGEGGLAALAAPVGGAWLLAGPESGLDDDEEARAVAAGWQPLRLGPRTLRTETAGLAALAALQARFGDY | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
S... |
A0A133VPH3 | MFERGVGKNDDYSFDSDSLSNLGLPESLLREDLDIPDLTEPEVVRHFTRLSQMNYGIDSGIYPLGSCTMKYNPKVSEELASLEDACCLHPDQPEETVQGALEIMYRLEKLLSEISGMDRVTFQPAAGAHGEFLAMLLVRAFHESNEEGEKRSEVIVPDSAHGTNPASAAMAGYKIVEVPSSDRGRIDLDALKSVISERTAALMLTNPNTLGLFEDNIEQIVEAVHGAGALLFYDGANLNGILGRSRPGDMGFDIVHFNLHKTFATPHGGGGPGAGPVGVKDKLIKFLPDPTITYDEEEDLYHLGESGKYSIEKVQAFHGN... | 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... |
A0A3Q9XVS4 | MLTLLAPAKINLFLRVLNRRSDGYHNLASLIQTINLHDTLHFALGSQDVLMCEHPSLPKDSSNLITAATHLFRKKTGLNFGLKVVLEKNIPMQSGLGGGSSNAATTLWALNQLHGFPVPLEQLIEWSSEIGSDVPFFLSQGTAYCTGRGEVVRCLNPLPIQRLWIAKPYEGLSTPLVFKQLDLTKISSYDPELALQSFFSNQPFYFNDLEEPAFELKPYLKTVKEELLKSGYETVSMTGSGTAFYCLGRVAPPIIPQVTFYPATFINRPAERWYPFDSARD | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C... |
A0A956PG22 | MDKTVVLIGLNHKTAPVEVRERFSFSPEQVTETLNALQAEAALVECALLSTCNRTEFYAVPKKSVEAGMDTLTKFMSRNETLPPSEMDKLLYRHQGAVAINHLFSVSSGLDSLVVGENQILGQVRRAFMQAQEASCTGPVLERLFPWAIRVGKRARSETDIARGASSVSAAAVELAQKIFGEMKGRNVMLLGLGKMGKKSLKLLHKAGVNEVKIVNRTYEKAEELAEQCGGTAVPYEMLDEALVNVDILMASTGAPHYILTKDRISKVIRQRRGKPLFLIDIAVPRDIDPACGDVDNVYLYNIDDLQAVVDKNLARRHSE... | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
Function: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
EC: 1.2.1.70
Catalytic Activity: (S)-4-amino-5-oxopentanoate + NADP(+) + tR... |
A0A1F8MF36 | MTKRKVAVALSGGVDSAAAALLLTRAAYEVIGIHMRLRDSPSFDDHAHRAADICRILGIPYHQLDLQKEFESCVVDYFCREYRHGRTPNPCVACNHYVKFGLLLDKALSLGADYLATGHYAKVEHSRHGHRLLKAADTRRDQSYFLYTLTQEKLGRVLFPLGEHNKDEVKQMAMQAGLPTATKSSQDICFISRKNYGAFLSQRFPTLPGEVVDTRGRKLGQHRGIAFYTVGQRHGLGLASGKPLYVIRIEPESNRIVLGHEEELYSRKLTAHNLNWISGKIPRESITARAKIRYKSKETEATLSFRNDSVDVHFAQPQKA... | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
EC: 2.8.1.13
Subcellular Lo... |
A0A3A0EMC8 | MSSLAVAAAAMAALLLLLALGLEIAYSLALVGAVGLLVLGGQQAVIGSLATIPYSNVASFTLVVLPMFVLMGELAVAGGMAQQAYAAARAWLGRLPGGLMMTGIGASAVFGAVSGSSVAATVTVGRVSIAEMRRYGYDGGLAAGTVAAAGTLAALIPPSALAVFYALVTNESISRMLMAGLVPGLLSTALFMTTAYLIARARPALAPPVREPIRWRERLAVLRMTGPFGVLVLVVLGSIYSGLATATEASALGALAALALLALARRLSWAGLNAALAATTRISCMIFMIIIGGMLFSRFLAFSGITLGLGEFIRGLQLSP... | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 434
Sequence Mass (Da): 44950
Location Topology: Multi-pass membrane protein
|
A0A1E2UUZ1 | MIVPVILSGGSGTRLWPLSRSAYPKQFIPLMDDNSLFQATFARVAKLPDSTDALVVCNEEHRFMVAEQVRKLDKKCLAIMLEPVGRNTAPAIACAALYALQQNQDALIMVTPSDHIISDLSRFSESMEKGIEAAKNGGLVTFGVVPDKPETGYGYIRKDEDNQHLGTYQVAEFVEKPDLQTAIKYLDSGEYLWNSGMFVFQAQLYLQELKKFQPEMVKAVTSAFEKQSVDLDFIRLDKEAFLACPSESIDYAVMEKTEKSMVVPMDAGWSDIGSWSALSDAAVTDSEDDNVFLGDVLAKDVTNSYLRSENRMIAGIGLDG... | Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
EC: 2.7.7.13
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Length: 484
Sequence Mass (Da): 54067
|
R7FLN3 | MASEVVKYLLLLFVFSFSLLLSYFINKIIIKIEKKRDIHQQIHRLIVSTHKKKKDTPTLGGIAIFLSIILITSIFNFNFFQSKKGIFITILFTSYFFVGLVDDLKKLKDKNESGLPPLVRIGFEIAFALCGLLVLGYDQRTSWIINFPFDIGYINLNFLTPLFLIFIIVGSANASNLVDGLDGLSAGITTIALSPFIFFSFFKGDFILMTFLITVIGSLLGFVLLNLYPASIFMGDCGSLMLGAILGSIAICLYRIPELALIGGIYVIECASVIVQVSYYKAFKKRVFLMAPLHHHFELKGWGETKVVMFYYLIGVIFAV... | 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, yield... |
A0A8J4PN07 | MPKKILLLLGIIFLSAFISFSTYISLFRDNQRIFNHEIIKTTELQNNNFNINRLMNNPKSVDISNSGATDNNNNNFIYFNQNQNQIKSTPPPQHENYLKKSRPPRPPPLFKREKKVEQKLDDLVPKTKYSTSMLTKECLNGGIGFQDKCICSFNYHGDQCQHMGEDRCSNPKFHFEDDKHIQHTTGLETFKNATVPFCCWSKHRHQTNLYRNKLRDNQIDSHHDQLKQILTNYGPWNENDKVFLNHLFSQADPYSADDSTHQYKLIMQQDRKKDKFPVSKSRKSHLAFVLLFHRIEMDEVQQLLKYIYRSKHYYVIHIDK... | Pathway: Glycan metabolism; chondroitin sulfate biosynthesis.
Catalytic Activity: L-seryl-[protein] + UDP-alpha-D-xylose = 3-O-(beta-D-xylosyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.2.26
Subcellular Location: Membrane
Sequence Length: 598
Sequence Mass (Da): 70848
Location Topology: Single-pass type II membrane protei... |
A0A2P9H7G4 | MFAFALAYPYLPGAKTDAFKGLSVLVGIMVSIGASGIVGQATSGFILMYTRTFRAGEYVRIGDTEGTVDGVGVFTTRIRTGLGEELLLPNSLVLQHVTRNYSRAVPGTGYVVDTVVTIGYSTPWRQVHAMLMEAARMTLDIATAPAPYVRQTALSDFYVQYRLVAYTPAERPAQRADVLSRLHANIQDVFNSYGVQIMSPHYMTDPAEPQSVPKARWYVAPADLSEGPPQSDDPKR | 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... |
A0A6P8BKD2 | MAPSSKRGGNTVLTLGPGLNYPIEITKLYKSPGDRIKRQEPLFQYSNKIWVEEGDFDTGEYKRVLKPTRVEWSAPNDGKLSKWHLKVGDVIGRDGECVTIEEDCTHEIQYQKMCALCGQDMTRVDWSASRPSTSRATINMTHDNTGLLISRDAAARTDLEMQKRLVAQRKLVLVVDLDQTVIQTACEPTIGEWQKDPSNPNYEALKEVRSFELPSEDGPRRNYTYYVKCRPGTHEFLNKVSNMFEMHVYTMATRAYAEHILKIIDPKKNLFGNRVISRNENKGIEKTLQRIFPTSTKMVAVIDDRTDVWPQNRSNVIKVV... | Function: This promotes the activity of RNA polymerase II.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
EC: 3.1.3.16
Subcellular Location: Nucleus
Sequence Length: 871
Sequence Mass (Da): 96725
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.