NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/JB.188.6.2262-2274.2006; PubMed=16513756 [NCBI, ExPASy, EBI, Israel, Japan]
Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., Inatomi K., Furukawa K., Inui M., Yukawa H.;
"Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195.";
J. Bacteriol. 188:2262-2274(2006).

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.
CAUTION: Asp-165 is present instead of the conserved Glu which is expected to be a substrate-binding residue.
CAUTION: Ala-369 is present instead of the conserved His which is expected to be part of the substrate-binding region.

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

AP008230; BAE82778.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_517222.1; -.

3D structure databases

ModBase

Q24YW4.

Enzyme and pathway databases

BioCyc

DHAF138119:DSY0989-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

3953183; -.

GenomeReviews

AP008230_GR; DSY0989.

KEGG

dsy:DSY0989; -.

NMPDR

fig|138119.3.peg.1233; -.

Phylogenomic databases

HOGENOM

Q24YW4; -.

Genome annotation databases

CMR

Q24YW4; DSY0989.

Other

ProtoNet

Q24YW4.

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

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 437`	`437`	`Enolase 1.`	`PRO_0000280844`
`ACT_SITE`	`206 206`		`Proton donor (By similarity).`
`ACT_SITE`	`341 341`		`Proton acceptor (By similarity).`
`METAL`	`244 244`		`Magnesium (By similarity).`
`METAL`	`289 289`		`Magnesium (By similarity).`
`METAL`	`316 316`		`Magnesium (By similarity).`
`BINDING`	`156 156`		`Substrate (By similarity).`
`BINDING`	`289 289`		`Substrate (By similarity).`
`BINDING`	`316 316`		`Substrate (By similarity).`
`BINDING`	`341 341`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`392 392`		`Substrate (By similarity).`
`MOD_RES`	`283 283`		`Phosphotyrosine (By similarity).`

Sequence information

Length: 437 AA [This is the length of the unprocessed precursor]

Molecular weight: 47492 Da [This is the MW of the unprocessed precursor]

CRC64: E8BCC5D462347988 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEGFKIKSVK ARQVFDSRAN PTVEVDITLK DGTVGRGIVP SGASTGLFEA VELRDGEETF 

        70         80         90        100        110        120 
DGKGVSKAIH HVNEQLAPLL LDMDVRDQKA IDSRLIEIDG TPNKSRLGAN AILGCSMAAC 

       130        140        150        160        170        180 
WAGANYYKVP LYRYLGGSAA NKLPVPMVQI IGGGAHADNV IDIQDFLVIP TSAPTFSEGY 

       190        200        210        220        230        240 
EMVVNVYNAA KMIFKGAGKP VSIADEGGLW PTGFQSNEEG LKLLCESIEL AGYTPGQDLG 

       250        260        270        280        290        300 
IALDIASSEF YDPERGTYRL ELEKKTLTKE EMVGMLSDWV DNYPIISIED GMSELDWEGN 

       310        320        330        340        350        360 
LLLTQKLGKK IQLIGDDLFT TNIERIRKGV EMKVDNAVLI KMNQIGTITE TIETIEFTQN 

       370        380        390        400        410        420 
HGYLPVVSAR SGETEDCTIV HLAIATNAGQ LKVGSAARSE RTAKWNEVLR IEEALGSSAR 

       430 
YPSKGVFAAA GIQFNQY

Q24YW4 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