ACL_RS02010

Uniprot: A9NF93
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:0000255|HAMAP-Rule:MF_00318}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00318}.
Pathway: PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00318}.
Active site: ACT_SITE 205 205 Proton donor. {ECO:0000255|HAMAP-Rule:MF_00318}.; ACT_SITE 340 340 Proton acceptor. {ECO:0000255|HAMAP-Rule:MF_00318}.
Binding site: BINDING 155 155 Substrate. {ECO:0000255|HAMAP-Rule:MF_00318}.; BINDING 164 164 Substrate. {ECO:0000255|HAMAP-Rule:MF_00318}.; BINDING 288 288 Substrate. {ECO:0000255|HAMAP-Rule:MF_00318}.; BINDING 315 315 Substrate. {ECO:0000255|HAMAP-Rule:MF_00318}.; BINDING 340 340 Substrate (covalent); in inhibited form. {ECO:0000255|HAMAP-Rule:MF_00318}.; BINDING 391 391 Substrate. {ECO:0000255|HAMAP-Rule:MF_00318}.
Calcium binding:
DNA binding:
Metal binding: METAL 242 242 Magnesium. {ECO:0000255|HAMAP-Rule:MF_00318}.; METAL 288 288 Magnesium. {ECO:0000255|HAMAP-Rule:MF_00318}.; METAL 315 315 Magnesium. {ECO:0000255|HAMAP-Rule:MF_00318}.
Nucleotide binding:
Site:
Gene names (primary): eno
Gene names (synonym):
Mass: 46,517
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: CHAIN 1 431 Enolase. /FTId=PRO_1000079120.
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP-Rule:MF_00318}.
Protein families: Enolase family
Coiled coil:
Domain [FT]:
Motif:
Region: REGION 367 370 Substrate binding. {ECO:0000255|HAMAP-Rule:MF_00318}.
EMBL: CP000896
ProteinModelPortal: A9NF93
MEROPS:
EnsemblBacteria KO: ABX81023
UniPathway: K01689
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

422406-423702(+)

>nucleotide sequence
ATGCCATTTATTACAAGCGTATATGCTAGAGAAGTACTTGATAGCCGCGGTAACCCAACT
GTTGAAGTTGAAATCGTTACAGACTCAGGTGCATTTGGTAGAACATTAGTACCATCAGGT
GCTTCAACAGGTGAACACGAAGCTGTTGAATTACGTGACGGTGATAAATCACGTTACTTA
GGTAAAGGTGTTTTAAAAGCTGTTGAAAATGTTAATGACATTATCGGACCAGCAATCTTA
GGAGATTCAGTTTTAGATCAAGTAGCTCTTGATAGAAAATTAATCGCTTTAGATGGTACA
AAAAACAAAGGTAAATTAGGTGCAAACGCTATTTTAGGTGTTTCAATCGCTGCTGCTAAA
GCTGCTGCTGATTTATTAAACCTTGAATTATACCAATACTTAGGCGGATTTAACGCTAAA
CAATTACCAGTACCAATGATGAATATCATCAATGGTGGTGCACACTCAGATGCTCCAATC
GACTTCCAAGAATTCATGATTTTCCCAGTAGGTGCGCCTTCATTTAAAGAAGCTATCCGT
TGGGGAGCTGAAATCTTCCATGCTTTAAAAGCTATTTTAAAGAAAAAAGGTCTTTCAACT
GCAGTAGGTGATGAAGGTGGATTTGCTCCAAACTTAGCATCTAATGAAGATACAATTGAT
AACATCTTAGAAGCTATTAAAAATGCTGGTTATAAAGCTGGTGAAGAAGTATTTATCGGT
TTTGACGTAGCTGCTTCAGAATTCTTTGATAAAGCTAAAGGTAAATATGTATTCAAAAAA
TCTACTAAAGAAGAATTTACTTCTGCTGAATTAGTAGAATACTATGCTGGATTAGTTCAA
AAATACCCAATCATCTCAATCGAAGATGGTATGGATGAAAATGACTGGGATGGCTGGAAG
TTATTAACTGACAAATTAGGTTCAAAAATCCAATTAGTTGGGGATGACCTATTTGTTACA
AACACTGAATATCTTGCAAGAGGTATCAAAACAAACACAGCAAACTCAATTTTAGTTAAA
GTAAACCAAATCGGTACATTAACTGAAACATTTGACGCAATCGAAATGGCTAAACGTGCT
GGTTATACAGCAGTTATCTCACACCGTTCAGGTGAAACAGAAGATACAACAATTGCTGAT
ATCGCTGTTGCTGCAAATACAGGACAAATTAAAACTGGTTCAGCTTCACGTACAGACCGT
GTTGCTAAATACAACCAATTAATGCGTATTGAAGATCAACTAGGTGAAGATGCTGTTTAC
TTAGGTAAAGATTCTTTCTACAACCTAAAAAAATAA

>protein sequence
MPFITSVYAREVLDSRGNPTVEVEIVTDSGAFGRTLVPSGASTGEHEAVELRDGDKSRYL
GKGVLKAVENVNDIIGPAILGDSVLDQVALDRKLIALDGTKNKGKLGANAILGVSIAAAK
AAADLLNLELYQYLGGFNAKQLPVPMMNIINGGAHSDAPIDFQEFMIFPVGAPSFKEAIR
WGAEIFHALKAILKKKGLSTAVGDEGGFAPNLASNEDTIDNILEAIKNAGYKAGEEVFIG
FDVAASEFFDKAKGKYVFKKSTKEEFTSAELVEYYAGLVQKYPIISIEDGMDENDWDGWK
LLTDKLGSKIQLVGDDLFVTNTEYLARGIKTNTANSILVKVNQIGTLTETFDAIEMAKRA
GYTAVISHRSGETEDTTIADIAVAANTGQIKTGSASRTDRVAKYNQLMRIEDQLGEDAVY
LGKDSFYNLKK