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=Enolase is secreted and attached to the bacterial cell surface. The export of enolase possibly depends on the covalent binding to the substrate (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

CP000325; ABL06574.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_908045.1; -.

3D structure databases

ModBase

A0PW55.

Organism-specific databases

BuruList

MUL_4631; -.

Ontologies

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.

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

4550802; -.

GenomeReviews

CP000325_GR; MUL_4631.

KEGG

mul:MUL_4631; -.

CMR

A0PW55; MUL_4631.

Other

ProtoNet

A0PW55.

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`	`1 428`	`428`	`Enolase.`	`PRO_0000280866`
`REGION`	`361 364`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`204 204`		`Proton donor (By similarity).`
`ACT_SITE`	`334 334`		`Proton acceptor (By similarity).`
`METAL`	`241 241`		`Magnesium (By similarity).`
`METAL`	`282 282`		`Magnesium (By similarity).`
`METAL`	`309 309`		`Magnesium (By similarity).`
`BINDING`	`154 154`		`Substrate (By similarity).`
`BINDING`	`163 163`		`Substrate (By similarity).`
`BINDING`	`282 282`		`Substrate (By similarity).`
`BINDING`	`309 309`		`Substrate (By similarity).`
`BINDING`	`334 334`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`385 385`		`Substrate (By similarity).`
`MOD_RES`	`276 276`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 44736 Da [This is the MW of the unprocessed precursor]

CRC64: 58A29D49E5EBF57F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPIIEQVGAR EILDSRGNPT VEVEVALIDG TFARAAVPSG ASTGEHEAVE LRDGGDRYGG 

        70         80         90        100        110        120 
KGVKKAVEAV LDEIGPAVIG LNADDQRLVD QALVDLDGTP DKSRLGGNSI LGVSLAVAKA 

       130        140        150        160        170        180 
ASESAELPLF RYIGGPNAHI LPVPMMNILN GGAHADTGVD IQEFMVAPIG APSFSEALRW 

       190        200        210        220        230        240 
GAEVYHALKA VLKKAGLSTG LGDEGGFAPD VASTTAALDL ISQAIEAAGF KPGVDVALAL 

       250        260        270        280        290        300 
DAAANEFHAD GSYTFEGTPR TAAQMTEFYA GLLGSYPVVS IEDPLYENDW DGWAALTAEI 

       310        320        330        340        350        360 
GDRVQIVGDD VFVTNPERLE EGIDRGVANA LLVKVNQIGT LTETLDAVAL AHHSGYRTMI 

       370        380        390        400        410        420 
SHRSGETEDT IIADLAVAVG SGQIKTGAPA RSERVAKYNQ LLRIEEALGD AARYAGDLAF 


PRFVADPK

A0PW55 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