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 cell surface (By similarity).
SIMILARITY: Belongs to the enolase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

CP000828; ABW28963.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001518280.1; -.

3D structure databases

ModBase

B0C9F0.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from electronic annotation from HAMAP).
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.

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

5682782; -.

GenomeReviews

CP000828_GR; AM1_3978.

CMR

B0C9F0; AM1_3978.

Other

ProtoNet

B0C9F0.

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`	`1 426`	`426`	`Enolase.`	`PRO_1000079119`
`REGION`	`364 367`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`207 207`		`Proton donor (By similarity).`
`ACT_SITE`	`337 337`		`Proton acceptor (By similarity).`
`METAL`	`244 244`		`Magnesium (By similarity).`
`METAL`	`285 285`		`Magnesium (By similarity).`
`METAL`	`312 312`		`Magnesium (By similarity).`
`BINDING`	`157 157`		`Substrate (By similarity).`
`BINDING`	`166 166`		`Substrate (By similarity).`
`BINDING`	`285 285`		`Substrate (By similarity).`
`BINDING`	`312 312`		`Substrate (By similarity).`
`BINDING`	`337 337`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`388 388`		`Substrate (By similarity).`
`MOD_RES`	`279 279`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 426 AA [This is the length of the unprocessed precursor]

Molecular weight: 45337 Da [This is the MW of the unprocessed precursor]

CRC64: A603741875A0D897 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MHETEIAAIE AREILDSRGR PTVEAEVILS CGAFGLAQVP SGASTGSFEA HELRDGDAQR 

        70         80         90        100        110        120 
YGGKGVLTAV TNIKDHIQPE LVGLNALDQA DIDQTMIDLD GSTNKSKLGA NAILAVSLAT 

       130        140        150        160        170        180 
AKAASEVLNL ELYRYLGGPL ANLLPVPLMN VINGGAHANN NVDIQEFMIV PHGADSFKEA 

       190        200        210        220        230        240 
LRWGAEVFAS LSQVLAAQNL LTGVGDEGGY APNLASNQAA LELLVEAIEK AGYQPGAQIS 

       250        260        270        280        290        300 
LALDVAASEF YKDGQYTYDG AAHSPKELID YLDGLASKYP IVSIEDPLHE EDWESWGNLT 

       310        320        330        340        350        360 
AQLGDRVQLV GDDLFVTNPI RLQKGIEQQS ANSILIKLNQ IGTLTETLET IDLAKRNSFT 

       370        380        390        400        410        420 
SIISHRSGET EDTTIADLAV ATRAGQIKTG SLCRSERVAK YNRLLRIEDE LGSQASYAGA 


VGLGPG

B0C9F0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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