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

CP000075; AAY36532.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_234570.1; -.

3D structure databases

ModBase

Q4ZWE0.

Enzyme and pathway databases

BioCyc

PSYR205918:PSYR_1482-MON; -.

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.

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

3366981; -.

GenomeReviews

CP000075_GR; Psyr_1482.

KEGG

psb:Psyr_1482; -.

NMPDR

fig|205918.4.peg.1966; -.

Phylogenomic databases

HOGENOM

Q4ZWE0; -.

Genome annotation databases

CMR

Q4ZWE0; Psyr_1482.

Other

ProtoNet

Q4ZWE0.

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`	`1 427`	`427`	`Enolase 2.`	`PRO_0000267080`
`REGION`	`366 369`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`207 207`		`Proton donor (By similarity).`
`ACT_SITE`	`339 339`		`Proton acceptor (By similarity).`
`METAL`	`244 244`		`Magnesium (By similarity).`
`METAL`	`287 287`		`Magnesium (By similarity).`
`METAL`	`314 314`		`Magnesium (By similarity).`
`BINDING`	`156 156`		`Substrate (By similarity).`
`BINDING`	`166 166`		`Substrate (By similarity).`
`BINDING`	`287 287`		`Substrate (By similarity).`
`BINDING`	`314 314`		`Substrate (By similarity).`
`BINDING`	`339 339`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`390 390`		`Substrate (By similarity).`
`MOD_RES`	`281 281`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 427 AA [This is the length of the unprocessed precursor]

Molecular weight: 46037 Da [This is the MW of the unprocessed precursor]

CRC64: FAE71E15B6043CB4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKTQIQAIHA REILDSRGNP TVEVDVTLEC GAMGRASVPS GASTGAHEAV ELRDKDTQRY 

        70         80         90        100        110        120 
SGKGVLKAVS NVNTEILESL RGMNAIDQEQ IDHLMIKLDG TSDKSRLGGN AILGVSLAVA 

       130        140        150        160        170        180 
RAAASALNLP LFQYLGGEQA ARMPVPMFNI LNGGVHANWQ GPDFQEFMIA PTGAGSFKEA 

       190        200        210        220        230        240 
LRWGSEVYHE LKAVLKDAGY STAVGDEGGF APALKKNSDA IELIIKAIER AGYTPGSQIE 

       250        260        270        280        290        300 
IAIDPASSGF YENGLYHLRS EGRKVDAQEL INLYSSWVDK YPIAVLEDGL AEDDWSGWKL 

       310        320        330        340        350        360 
LNAALGDRIE LVGDDLFVTN VERIQRGITE NVANAVLIKP NQIGTLTETK AAIEMAYGAN 

       370        380        390        400        410        420 
WGAMVSHRSG ETVDSSIADL TVAMGTGHLK TGAPCRGERV EKYNQFLRIE EDLGSRAFYA 


GHDAFVR

Q4ZWE0 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