SPM_000750
  | Uniprot: A0A037UL32
Description: enolase EC number: 4.2.1.11 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O. {ECO:0000256|HAMAP-Rule:MF_00318}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00318}; Enzyme regulation: ENZYME REGULATION: The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. {ECO:0000256|HAMAP-Rule:MF_00318}. Function [CC]: FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. {ECO:0000256|HAMAP-Rule:MF_00318}. Pathway: PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|HAMAP-Rule:MF_00318}. Active site: ACT_SITE 205 205 Proton donor. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-1}.; ACT_SITE 360 360 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-1}. Binding site: BINDING 155 155 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 164 164 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 308 308 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 335 335 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 360 360 Substrate (covalent); in inhibited form. {ECO:0000256|HAMAP-Rule:MF_00318}.; BINDING 411 411 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}. Calcium binding: DNA binding: Metal binding: METAL 258 258 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00318}.; METAL 308 308 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00318}.; METAL 335 335 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00318}. Nucleotide binding: Site: Gene names (primary): eno Gene names (synonym): Mass: 49,952 Subunit structure [CC]: Gene ontology (GO): cell surface [GO:0009986]; extracellular region [GO:0005576]; phosphopyruvate hydratase complex [GO:0000015]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; glycolytic process [GO:0006096] Gene ontology IDs: GO:0000015; GO:0000287; GO:0004634; GO:0005576; GO:0006096; GO:0009986 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the enolase family. {ECO:0000256|HAMAP-Rule:MF_00318}. Protein families: Enolase family Coiled coil: Domain [FT]: DOMAIN 4 134 Enolase_N. {ECO:0000259|SMART:SM01193}.; DOMAIN 139 448 Enolase_C. {ECO:0000259|SMART:SM01192}. Motif: Region: REGION 387 390 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}. EMBL: AGBZ02000001 ProteinModelPortal: MEROPS: EnsemblBacteria KO: KAI92629 UniPathway: CDD: Gene3D: HAMAP: 3.20.20.120;3.30.390.10 InterPro: MF_00318 PANTHER: IPR000941;IPR020810;IPR029065;IPR020809;IPR020811;IPR029017 PIRSF: PTHR11902 PRINTS: PIRSF001400 PROSITE: PR00148 Pfam: PS00164 ProDom: PF00113;PF03952 SMART: SUPFAM: SM01192;SM01193 TIGRFAMs: SSF51604;SSF54826 |
146435-147812(-) >nucleotide sequence TTCAGCTACTTTTCCCAGTTCATCTTCAATTGCTAATAAACGATTATATTTTGCAATTCT ATCACTTCGTGACATACTTCCTGTTTTAATTTGACCAGTATTTAAAGCGACTGCTAAATC AGCAATTGTTGAATCTTCGGTTTCTCCTGAACGATGTGAAACAACTGCCGTTCAACCTGC TTTTTGTGCTAATTGAATTGTATCAATTGTTTCAGTTACTGTTCCAATTTGGTTTAATTT AATTAAAACAGAATTTGCGGCATTACGAGCAATTCCTTCTGCTGTAATTTTTGGATTTGT AACAAATAAGTCATCACCAACAATTTGAATTTTATGCCCCATTGTTTTTACTTGCAATTC AAAACCAGCTCAATCACCTTCTGCTAAACCATCTTCAATTGAAATAATTGGGTATTTATC AACTAACTTGTCTAAATATTTAATTAATTCTTCTGTTGTCATTGCATATTCTTTACCTGT AACTTTTTCAATTTTCTTAAAGTGATATTTTTTATCATCAAAATATAATTCTGATGAAGC ACAATCCATTGCAATCATAACACCATCTTTGCCTGGTTTATATCCTGCTGCTTCAATTGC TTCAACAATTAAATCTAATGCAACTTCGGCTGGTGTTTTTGCTTGAAATGAAGTTAAAGT TTGATCTTTATATGCTCAATTAAAATGCGGAGCAAAACCACCTTCATCACCAACAGCTGT AATATCACCTTTATCGTGTAAGATTTTCTTTAAAGTATGGAAAATTTCTGATGACCATCT TAAAGCTTCTTTAAAAGTTTCAGCCCCAACTGGCATAATCATAAATTCTTGGAAATCAAT TGCACTATCAGCATGCTCTCCTCCATTAATAATATTTAACATTGGAACTGGCAGTTTTTT CCCATTAACACCACCCAAATATTTATATAATGGCATTTCTAATTCAGAAGCTGCTGCTTT GGCAACAGCCATTGACACTCCTAACATTGCATTAGCACCTAAATTCTTTTTAAAATCAGT TCCATCTAACGCAATCATGGCATGATCAATTTCAACTTGGTTTGTTACTTCCATTCCAAC AAGTTGTTCTGCAATTTTTGTATTAACATTCCCAACTGCTTTTAAAACACCTTTCCCTTG GTAACGTCCTTTATCACCATCTCTTAATTCTAATGCTTCACGACTTCCAGTTGAAGCTCC TGATGGTACCATTGCTGAACCATATCCGCCAAATTCTGTTCAAACTTCAACTTGAACAGT TGGATTTCCTCGTGAATCAATTACTTCACGAGCATTAATTTTCTCAATTCTCGACAT >protein sequence GKGVLKAVGNVNTKIAEQLVGMEVTNQVEIDHAMIALDGTDFKKNLGANAMLGVSMAVAK AAASELEMPLYKYLGGVNGKKLPVPMLNIINGGEHADSAIDFQEFMIMPVGAETFKEALR WSSEIFHTLKKILHDKGDITAVGDEGGFAPHFNWAYKDQTLTSFQAKTPAEVALDLIVEA IEAAGYKPGKDGVMIAMDCASSELYFDDKKYHFKKIEKVTGKEYAMTTEELIKYLDKLVD KYPIISIEDGLAEGDWAGFELQVKTMGHKIQIVGDDLFVTNPKITAEGIARNAANSVLIK LNQIGTVTETIDTIQLAQKAGWTAVVSHRSGETEDSTIADLAVALNTGQIKTGSMSRSDR IAKYNRLLAIEDELGKVAEYDGIKTFYNLKKHVADLKK |
© Fisunov Lab of Proteomics, 2016.