GCW_02860

Uniprot: A0A0F6CKZ5
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 221 221 Proton donor. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-1}.; ACT_SITE 364 364 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-1}.
Binding site: BINDING 171 171 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 180 180 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 312 312 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 339 339 Substrate. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.; BINDING 364 364 Substrate (covalent); in inhibited form. {ECO:0000256|HAMAP-Rule:MF_00318}.; BINDING 415 415 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 312 312 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00318}.; METAL 339 339 Magnesium. {ECO:0000256|HAMAP-Rule:MF_00318}.
Nucleotide binding:
Site:
Gene names (primary): eno
Gene names (synonym):
Mass: 51,157
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 15 144 Enolase_N. {ECO:0000259|SMART:SM01193}.; DOMAIN 155 452 Enolase_C. {ECO:0000259|SMART:SM01192}.
Motif:
Region: REGION 391 394 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400-2}.
EMBL: CP006916
ProteinModelPortal:
MEROPS:
EnsemblBacteria KO: AHB99767
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
680357-681785(-)

>nucleotide sequence
TTATTTTTTTGATTTTGCTTTTGTTGTTTTTTTAGCTGGACTCTTTTTAGGTGTTGCAGC
AGGTGTGCTTAGGTTATAGAAAGTTTTACTTCCTAAATATTTAGCTTTATTACCTAATTG
CATTTCGATTGCTAATAAACGGTTATATTTAGCAATTCTTTCAGATCGTGACATTGAACC
AGTCTTGATCTGACCTGTACTTAGAGCTACAGCTAAATCAGCAATGAAAGCATCTTCAGT
TTCACCTGAACGGTGAGAAACTACAGCCGTTCAGTTTGCTTTTTTAGCAATGTTAATTGT
TTGGATCGTTTCAGTTAATGTTCCGATTTGGTTTAACTTAATTAATACTGAGTTAGTTGC
TGATAATGAAACACCCTTAGAAGTTAATTCAGGGTTTGTACAGTAAGTGTCATCACCAAC
GATCTGTACTTTTTTACCGATCTTTTTAGTTAGTGATTCCATCCCTTTTCAGTCGTTTTC
ATCTAAACCATCTTCGATTGAAACAATTGGGTATTTTTTAGTTAAATCTTCTAAGTAACT
AATTAATTGTTCAGTTGTTTTAGTGCCTTTTTCTTCAGAAAGAATTCCAGCTTTAACTGC
TTTTTTAAAGACATAAGCTTGCTTTTCTTTGCTGTAGAATTCACTAGCTGCACAGTCAAG
TGCAAACGCAACATCCTTACCTAAAGCATACCCAGCATCAACAACTGCTTGGCTCATTAG
ATCAAGTGCTTCTTCAGCTGATTTTAAGTTAGGCGCAAAACCACCTTCATCACCTTTGTT
AGTATTAAACTTCTTAGCTTTAAGTAGTTTTTGTAGTGAGTGGAACACTTCACTAGCCAT
TTGTAACGCTTTAGCCATCGTTTTTGCACCAACTGGCATAATCATGAACTCTTGGAAGTC
GATTGTGTTATCAGCGTGAGCTCCACCGTTAATTACGTTTAACATAGGAACTGGTAAGAT
GAAATCAGCACCCTTAACTTTTGCTACTTTCTTAGCAATGTATTGATATAAAGGTAGGTT
TAATGATTTAGCAGCTGCTCTACATACAGCCATTGATACTGCTAAGATCGCATTCGCACC
TAATTTAGCTTTAGTCTTAGTACCGTCTAATTCAATCATGAACTCATCAATCTCAGTTTG
TAAAGTAGCATCAACACCTAAGATTTTTGGACCAATCTTTTTGTTAATATTATTAACAGC
TTTAGTTACACCTTTACCATGATATTTAGTGCCACCATCTCTTAATTCTAAAGCTTCCTT
TTCACCAGTTGAAGCACCAGATGGAACCATTGATAATCCTTTAGATCCGTCGTTTAAAAC
AACTTCACAAGCAACTGTAGGAAACCCTCTTGAATCAAATACTTGGTATGCAAAAACACT
CTTTATTTCTAATTTATTGTTTTTGCTAGTACTGTTTGTCTTTGCCAT

>protein sequence
MAKTNSTSKNNKLEIKSVFAYQVFDSRGFPTVACEVVLNDGSKGLSMVPSGASTGEKEAL
ELRDGGTKYHGKGVTKAVNNINKKIGPKILGVDATLQTEIDEFMIELDGTKTKAKLGANA
ILAVSMAVCRAAAKSLNLPLYQYIAKKVAKVKGADFILPVPMLNVINGGAHADNTIDFQE
FMIMPVGAKTMAKALQMASEVFHSLQKLLKAKKFNTNKGDEGGFAPNLKSAEEALDLMSQ
AVVDAGYALGKDVAFALDCAASEFYSKEKQAYVFKKAVKAGILSEEKGTKTTEQLISYLE
DLTKKYPIVSIEDGLDENDWKGMESLTKKIGKKVQIVGDDTYCTNPELTSKGVSLSATNS
VLIKLNQIGTLTETIQTINIAKKANWTAVVSHRSGETEDAFIADLAVALSTGQIKTGSMS
RSERIAKYNRLLAIEMQLGNKAKYLGSKTFYNLSTPAATPKKSPAKKTTKAKSKK