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
TTATTTTTTTAAATCCGCAACATGTTTTTTTAAATTATAAAATGTTTTAATTCCATCATA
TTCAGCTACTTTTCCCAGTTCATCTTCAATTGCTAATAAACGATTATATTTTGCAATTCT
ATCACTTCGTGACATACTTCCTGTTTTAATTTGACCAGTATTTAAAGCGACTGCTAAATC
AGCAATTGTTGAATCTTCGGTTTCTCCTGAACGATGTGAAACAACTGCCGTTCAACCTGC
TTTTTGTGCTAATTGAATTGTATCAATTGTTTCAGTTACTGTTCCAATTTGGTTTAATTT
AATTAAAACAGAATTTGCGGCATTACGAGCAATTCCTTCTGCTGTAATTTTTGGATTTGT
AACAAATAAGTCATCACCAACAATTTGAATTTTATGCCCCATTGTTTTTACTTGCAATTC
AAAACCAGCTCAATCACCTTCTGCTAAACCATCTTCAATTGAAATAATTGGGTATTTATC
AACTAACTTGTCTAAATATTTAATTAATTCTTCTGTTGTCATTGCATATTCTTTACCTGT
AACTTTTTCAATTTTCTTAAAGTGATATTTTTTATCATCAAAATATAATTCTGATGAAGC
ACAATCCATTGCAATCATAACACCATCTTTGCCTGGTTTATATCCTGCTGCTTCAATTGC
TTCAACAATTAAATCTAATGCAACTTCGGCTGGTGTTTTTGCTTGAAATGAAGTTAAAGT
TTGATCTTTATATGCTCAATTAAAATGCGGAGCAAAACCACCTTCATCACCAACAGCTGT
AATATCACCTTTATCGTGTAAGATTTTCTTTAAAGTATGGAAAATTTCTGATGACCATCT
TAAAGCTTCTTTAAAAGTTTCAGCCCCAACTGGCATAATCATAAATTCTTGGAAATCAAT
TGCACTATCAGCATGCTCTCCTCCATTAATAATATTTAACATTGGAACTGGCAGTTTTTT
CCCATTAACACCACCCAAATATTTATATAATGGCATTTCTAATTCAGAAGCTGCTGCTTT
GGCAACAGCCATTGACACTCCTAACATTGCATTAGCACCTAAATTCTTTTTAAAATCAGT
TCCATCTAACGCAATCATGGCATGATCAATTTCAACTTGGTTTGTTACTTCCATTCCAAC
AAGTTGTTCTGCAATTTTTGTATTAACATTCCCAACTGCTTTTAAAACACCTTTCCCTTG
GTAACGTCCTTTATCACCATCTCTTAATTCTAATGCTTCACGACTTCCAGTTGAAGCTCC
TGATGGTACCATTGCTGAACCATATCCGCCAAATTCTGTTCAAACTTCAACTTGAACAGT
TGGATTTCCTCGTGAATCAATTACTTCACGAGCATTAATTTTCTCAATTCTCGACAT


>protein sequence
MSRIEKINAREVIDSRGNPTVQVEVWTEFGGYGSAMVPSGASTGSREALELRDGDKGRYQ
GKGVLKAVGNVNTKIAEQLVGMEVTNQVEIDHAMIALDGTDFKKNLGANAMLGVSMAVAK
AAASELEMPLYKYLGGVNGKKLPVPMLNIINGGEHADSAIDFQEFMIMPVGAETFKEALR
WSSEIFHTLKKILHDKGDITAVGDEGGFAPHFNWAYKDQTLTSFQAKTPAEVALDLIVEA
IEAAGYKPGKDGVMIAMDCASSELYFDDKKYHFKKIEKVTGKEYAMTTEELIKYLDKLVD
KYPIISIEDGLAEGDWAGFELQVKTMGHKIQIVGDDLFVTNPKITAEGIARNAANSVLIK
LNQIGTVTETIDTIQLAQKAGWTAVVSHRSGETEDSTIADLAVALNTGQIKTGSMSRSDR
IAKYNRLLAIEDELGKVAEYDGIKTFYNLKKHVADLKK






















© Fisunov Lab of Proteomics, 2016.