NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IL1403;
DOI=10.1101/gr.GR-1697R; PubMed=11337471 [NCBI, ExPASy, EBI, Israel, Japan]
Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A.;
"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403.";
Genome Res. 11:731-753(2001).

Comments

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

AE006297; AAK04742.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

D86705; D86705.

RefSeq

NP_266800.1; -.

3D structure databases

HSSP

Q9NDH8; 1OEP. [HSSP ENTRY / PDB]

SMR

Q9CHS7; 1-431.

ModBase

Q9CHS7.

Enzyme and pathway databases

BioCyc

LLAC272623:L0007-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

1114264; -.

AE005176_GR; LL0644.

lla:L0007; -.

fig|272623.1.peg.659; -.

Phylogenomic databases

HOGENOM

Q9CHS7; -.

Genome annotation databases

CMR

Q9CHS7; LL0644.

Other

ProtoNet

Q9CHS7.

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`	`1 433`	`433`	`Enolase 1.`	`PRO_0000133904`
`REGION`	`369 372`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`205 205`		`Proton donor (By similarity).`
`ACT_SITE`	`342 342`		`Proton acceptor (By similarity).`
`METAL`	`243 243`		`Magnesium (By similarity).`
`METAL`	`290 290`		`Magnesium (By similarity).`
`METAL`	`317 317`		`Magnesium (By similarity).`
`BINDING`	`155 155`		`Substrate (By similarity).`
`BINDING`	`164 164`		`Substrate (By similarity).`
`BINDING`	`290 290`		`Substrate (By similarity).`
`BINDING`	`317 317`		`Substrate (By similarity).`
`BINDING`	`342 342`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`393 393`		`Substrate (By similarity).`
`MOD_RES`	`284 284`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 433 AA [This is the length of the unprocessed precursor]

Molecular weight: 46912 Da [This is the MW of the unprocessed precursor]

CRC64: DEA9ED13BED764FE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIITDIYAR EVLDSRGNPT LEVEVYTEDG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYN 

        70         80         90        100        110        120 
GLGTQKAVDN VNNIIAEAII GYEVTDQQAI DRAMIALDGT ENKGKLGANA ILGVSIAAAR 

       130        140        150        160        170        180 
AAADELGVPL YNYLGGFNAK VLPTPMMNII NGGSHSDAPI AFQEFMIVPV GAPTFKEALR 

       190        200        210        220        230        240 
WGAEIFHALK KILKARGLET AVGDEGGFAP KFDGTEDGVE TILKAIEAAG YKAGEDGVMI 

       250        260        270        280        290        300 
GFDCASSEFY ENGVYDYTKF EGEGGKKLSA SEQVDYLEEL VSKYPIITIE DGMDENDWDG 

       310        320        330        340        350        360 
WKILTERLGK KVQLVGDDFF VTNTKYLERG IRENASNAIL IKVNQIGTLT ETFEAIEMAK 

       370        380        390        400        410        420 
EAGFTAIVSH RSGETEDSTI SDIAVATNAG QIKTGSLSRT DRMAKYNQLL RIEDQLAEVA 

       430 
QYKGLKAFYN LKK

Q9CHS7 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