FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity).
CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H₂O.
COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer (By similarity).
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 (By similarity).
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5 .
SUBCELLULAR LOCATION: Cytoplasm. Secreted. Cell surface. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface (By similarity).
SIMILARITY: Belongs to the enolase family.

Copyright

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Cross-references

Sequence databases

EMBL

AM286690; CAL16612.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_692884.1; -.

3D structure databases

ModBase

Q0VQD6.

Enzyme and pathway databases

BioCyc

ABOR393595:ABO_1164-MON; -.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from electronic annotation from HAMAP).
GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0000015;	Cellular component: phosphopyruvate hydratase complex (inferred from electronic annotation from InterPro).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from HAMAP).
GO:0004634;	Molecular function: phosphopyruvate hydratase activity (inferred from electronic annotation from HAMAP).
GO:0006096;	Biological process: glycolysis (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00318; -; 1.
PBIL [Tree]

InterPro

IPR000941; Enolase.
Graphical view of domain structure.

PANTHER

PTHR11902; Enolase; 1.

Pfam

PF00113; Enolase_C; 1.
PF03952; Enolase_N; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001400; Enolase; 1.

PRINTS

PR00148; ENOLASE.

ProDom

PD000902; Enolase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGR01060; eno; 1.

PS00164; ENOLASE; 1.

Genome annotation databases

GeneID

4213348; -.

GenomeReviews

AM286690_GR; ABO_1164.

KEGG

abo:ABO_1164; -.

NMPDR

fig|393595.12.peg.1175; -.

Phylogenomic databases

HOGENOM

Q0VQD6; -.

Genome annotation databases

CMR

Q0VQD6; ABO_1164.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 430`	`430`	`Enolase.`	`PRO_0000266992`
`REGION`	`368 371`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`209 209`		`Proton donor (By similarity).`
`ACT_SITE`	`341 341`		`Proton acceptor (By similarity).`
`METAL`	`246 246`		`Magnesium (By similarity).`
`METAL`	`289 289`		`Magnesium (By similarity).`
`METAL`	`316 316`		`Magnesium (By similarity).`
`BINDING`	`159 159`		`Substrate (By similarity).`
`BINDING`	`168 168`		`Substrate (By similarity).`
`BINDING`	`289 289`		`Substrate (By similarity).`
`BINDING`	`316 316`		`Substrate (By similarity).`
`BINDING`	`341 341`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`392 392`		`Substrate (By similarity).`
`MOD_RES`	`283 283`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 430 AA [This is the length of the unprocessed precursor]

Molecular weight: 46032 Da [This is the MW of the unprocessed precursor]

CRC64: FE68747AD14300CE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKIVDIKAR EILDSRGNPT IEADVILESG ASGSACAPSG ASTGSREALE LRDGDKSRYL 

        70         80         90        100        110        120 
GKGVTKAVGN VNSAIRELLV GMEVSDQKAL DQAMLDADGT ENKGNLGANA ILAVSLAAAK 

       130        140        150        160        170        180 
AAAVDQGKPL YEYISDLQDD DNEYSLPVPM MNIINGGEHA DNNVDIQEFM IQPVGAPTVA 

       190        200        210        220        230        240 
EAIRYGAEIF HALKGVLKKR GLNTAVGDEG GFAPNLPSNE AALEAIMEAI EIAGYKAGDD 

       250        260        270        280        290        300 
VTLALDCAAS EFYKDGKYVL AGEDRSMNSE EFADYLAELC DRYPIISIED GMDESDWDGW 

       310        320        330        340        350        360 
KILTEKLGKK VQLVGDDLFV TNTRILQRGI DEKVANSILI KFNQIGSLTE TLDAIKMAKD 

       370        380        390        400        410        420 
AGYTAVISHR SGETADTTIA DLAVATAAGQ IKTGSLCRSD RVAKYNRLIR IEQELGRAAY 

       430 
HGRKEFKLLG

Q0VQD6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools