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

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

Cross-references

Sequence databases

EMBL

CP000453; ABI57183.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_742673.1; -.

3D structure databases

ModBase

Q0A7K4.

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

4269207; -.

GenomeReviews

CP000453_GR; Mlg_1839.

KEGG

aeh:Mlg_1839; -.

NMPDR

fig|187272.6.peg.1750; -.

Phylogenomic databases

HOGENOM

Q0A7K4; -.

Genome annotation databases

CMR

Q0A7K4; Mlg_1839.

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`	`1 429`	`429`	`Enolase.`	`PRO_0000266993`
`REGION`	`364 367`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`205 205`		`Proton donor (By similarity).`
`ACT_SITE`	`337 337`		`Proton acceptor (By similarity).`
`METAL`	`242 242`		`Magnesium (By similarity).`
`METAL`	`285 285`		`Magnesium (By similarity).`
`METAL`	`312 312`		`Magnesium (By similarity).`
`BINDING`	`155 155`		`Substrate (By similarity).`
`BINDING`	`164 164`		`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: 429 AA [This is the length of the unprocessed precursor]

Molecular weight: 46083 Da [This is the MW of the unprocessed precursor]

CRC64: 65E5BA96EBF84536 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGTIKQIKAR EILDSRGNPT VEADVILDSG VMGRAAVPSG ASTGTREAVE LRDGDAGRYL 

        70         80         90        100        110        120 
GKGVRKAVEN VNTVIADALC GMDASGQRAL DDRMRELDGT DNKGKLGANA LLAVSLAAAR 

       130        140        150        160        170        180 
ATAAERGQSL FRYLNPEGPW SLPVPMMNIL NGGEHADNSV DIQEFMVMPT GFDRFSEALR 

       190        200        210        220        230        240 
CGTEIFHALK KVLQDRGLNT GVGDEGGFAP DLPSNEAALE VILEAIDRAG YKAGENVWLA 

       250        260        270        280        290        300 
LDAASSEFYQ DGVYRLASEG REFSAEAFAD YLADLCARYP ILSIEDGMDE SDWVGWKALT 

       310        320        330        340        350        360 
DKLGDRVQLV GDDLFVTNTR ILKRGIDEGV GNSILIKFNQ IGTLSETLDA IAMAHEAGFT 

       370        380        390        400        410        420 
SVVSHRSGET EDTTIADLAV ATTATQIKTG SLSRSDRVAK YNQLLRIEEE LGEQADYPGL 


AAFPQLRRG

Q0A7K4 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