NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND SUBUNIT.
DOI=10.1093/jb/mvg104; PubMed=12869539 [NCBI, ExPASy, EBI, Israel, Japan]
Hosaka T., Meguro T., Yamato I., Shirakihara Y.;
"Crystal structure of Enterococcus hirae enolase at 2.8 A resolution.";
J. Biochem. 133:817-823(2003).

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.
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 .
SUBUNIT: Homodimer.
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

AB091345; BAC16223.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

PDB

1IYX; X-ray; 2.80 A; A/B=1-432.

[ExPASy / RCSB / EBI]

PDBsum

1IYX; -.

ModBase

Q8GR70.

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.

Other

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

Keywords

3D-structure; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Secreted.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 432`	`432`	`Enolase.`	`PRO_0000133886`
`REGION`	`367 370`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`205 205`		`Proton donor (By similarity).`
`ACT_SITE`	`340 340`		`Proton acceptor (By similarity).`
`METAL`	`242 242`		`Magnesium.`
`METAL`	`288 288`		`Magnesium.`
`METAL`	`315 315`		`Magnesium.`
`BINDING`	`155 155`		`Substrate (By similarity).`
`BINDING`	`164 164`		`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).`
`MOD_RES`	`282 282`		`Phosphotyrosine (By similarity).`
`STRAND`	`3 13`	`11`
`STRAND`	`19 27`	`9`
`STRAND`	`32 36`	`5`
`STRAND`	`45 47`	`3`
`HELIX`	`59 61`	`3`
`HELIX`	`65 73`	`9`
`HELIX`	`75 79`	`5`
`HELIX`	`87 98`	`12`
`TURN`	`104 106`	`3`
`HELIX`	`108 126`	`19`
`HELIX`	`130 135`	`6`
`STRAND`	`147 151`	`5`
`HELIX`	`153 155`	`3`
`STRAND`	`156 159`	`4`
`STRAND`	`162 168`	`7`
`HELIX`	`175 196`	`22`
`STRAND`	`204 206`	`3`
`STRAND`	`213 215`	`3`
`HELIX`	`216 229`	`14`
`TURN`	`233 236`	`4`
`STRAND`	`238 242`	`5`
`TURN`	`245 248`	`4`
`TURN`	`251 253`	`3`
`STRAND`	`255 257`	`3`
`TURN`	`259 262`	`4`
`HELIX`	`268 281`	`14`
`STRAND`	`284 289`	`6`
`HELIX`	`296 306`	`11`
`TURN`	`307 309`	`3`
`STRAND`	`310 315`	`6`
`TURN`	`316 320`	`5`
`HELIX`	`322 331`	`10`
`STRAND`	`337 339`	`3`
`HELIX`	`341 344`	`4`
`HELIX`	`347 359`	`13`
`STRAND`	`364 367`	`4`
`HELIX`	`377 384`	`8`
`STRAND`	`388 391`	`4`
`STRAND`	`395 397`	`3`
`HELIX`	`398 414`	`17`
`HELIX`	`415 417`	`3`
`HELIX`	`422 425`	`4`

Sequence information

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

Molecular weight: 46411 Da [This is the MW of the unprocessed precursor]

CRC64: 45F203F55685F1C1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSIITDVYAR EILDSRGNPT IEVEVYTESG AFGRGMVPSG ASTGEYEAVE LRDGDKARYG 

        70         80         90        100        110        120 
GKGVTKAVDN VNNIIAEAII GYDVRDQMAI DKAMIALDGT PNKGKLGANA ILGVSIAVAR 

       130        140        150        160        170        180 
AAADYLEVPL YHYLGGFNTK VLPTPMMNII NGGSHADNSI DFQEFMIMPV GAPTFKEALR 

       190        200        210        220        230        240 
MGAEVFHALA AILKSRGLAT SVGDEGGFAP NLGSNEEGFE VIIEAIEKAG YVPGKDVVLA 

       250        260        270        280        290        300 
MDAASSEFYD KEKGVYVLAD SGEGEKTTDE MIKFYEELVS KYPIISIEDG LDENDWDGFK 

       310        320        330        340        350        360 
KLTDVLGDKV QLVGDDLFVT NTQKLSEGIE KGIANSILIK VNQIGTLTET FEAIEMAKEA 

       370        380        390        400        410        420 
GYTAVVSHRS GETEDSTISD IAVATNAGQI KTGSLSRTDR IAKYNQLLRI EDQLGEVAEY 

       430 
KGLKSFYNLK AA

Q8GR70 in FASTA format

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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