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 archaeal 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

BA000002; BAA81473.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A72477; A72477.

RefSeq

NP_148623.1; -.

3D structure databases

HSSP

P00924; 4ENL. [HSSP ENTRY / PDB]

ModBase

Q9Y927.

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: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

1445431; -.

GenomeReviews

BA000002_GR; APE_2458.

KEGG

ape:APE_2458; -.

NMPDR

fig|272557.1.peg.1731; -.

Phylogenomic databases

HOGENOM

Q9Y927; -.

Genome annotation databases

CMR

Q9Y927; APE_2458.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 432`	`432`	`Enolase.`	`PRO_0000134019`
`REGION`	`367 370`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`210 210`		`Proton donor (By similarity).`
`ACT_SITE`	`340 340`		`Proton acceptor (By similarity).`
`METAL`	`247 247`		`Magnesium (By similarity).`
`METAL`	`288 288`		`Magnesium (By similarity).`
`METAL`	`315 315`		`Magnesium (By similarity).`
`BINDING`	`158 158`		`Substrate (By similarity).`
`BINDING`	`167 167`		`Substrate (By similarity).`
`BINDING`	`288 288`		`Substrate (By similarity).`
`BINDING`	`315 315`		`Substrate (By similarity).`
`BINDING`	`340 340`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`391 391`		`Substrate (By similarity).`

Sequence information

Length: 432 AA [This is the length of the unprocessed precursor]

Molecular weight: 46344 Da [This is the MW of the unprocessed precursor]

CRC64: 924E6362F8BDFDDE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGVNDFAIER VWGLQVLDSR GNPTVKAYVK LAGGSLGWGI APSGASRGER EAVELRDGGG 

        70         80         90        100        110        120 
KWRGKGVSRA VSLLNTVVAP RLEGVDARRQ AQIDRLLIEL DGTPNKSRLG GNTTTALSIA 

       130        140        150        160        170        180 
VSRAAAAQAR LELFQYLGGA GARRLPIPLL NVINGGVHAG NELDFQEFMI IPYGFESFTE 

       190        200        210        220        230        240 
AMRAAVETYG ELKSLLKDRY GASAVNVGDE GGFAPPMRSA EEALKTLVDA VEKAGYQPGS 

       250        260        270        280        290        300 
EIALGIDAAA SQLYSNGRYS VEGKSLSREE LLSLYQRLVE QYPIVYLEDP FSEDDYEGFK 

       310        320        330        340        350        360 
AAVDALSTET IIVGDDLLVT NPQRVKEASA LKAVTGLLVK VNQVGTLTEA LEAIQAARDR 

       370        380        390        400        410        420 
GIVHIVSHRS GDTEDTFIAD LAVATEALMI KTGAPARGER TSKYNRLLEI ENILGYSAEY 

       430 
AGPELRGVMG RR

Q9Y927 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