NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P.;
"Complete sequence of Actinobacillus succinogenes 130Z.";
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.

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

CP000746; ABR75397.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001345332.1; -.

3D structure databases

ModBase

A6VR00.

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

5348039; -.

GenomeReviews

CP000746_GR; Asuc_2051.

KEGG

asu:Asuc_2051; -.

CMR

A6VR00; Asuc_2051.

Other

ProtoNet

A6VR00.

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.`	`PRO_1000072004`
`REGION`	`370 373`	`4`	`Substrate binding (By similarity).`
`ACT_SITE`	`209 209`		`Proton donor (By similarity).`
`ACT_SITE`	`343 343`		`Proton acceptor (By similarity).`
`METAL`	`246 246`		`Magnesium (By similarity).`
`METAL`	`291 291`		`Magnesium (By similarity).`
`METAL`	`318 318`		`Magnesium (By similarity).`
`BINDING`	`159 159`		`Substrate (By similarity).`
`BINDING`	`168 168`		`Substrate (By similarity).`
`BINDING`	`291 291`		`Substrate (By similarity).`
`BINDING`	`318 318`		`Substrate (By similarity).`
`BINDING`	`343 343`		`Substrate (covalent); in inhibited form (By similarity).`
`BINDING`	`394 394`		`Substrate (By similarity).`
`MOD_RES`	`285 285`		`Phosphotyrosine (By similarity).`

Sequence information

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

Molecular weight: 45910 Da [This is the MW of the unprocessed precursor]

CRC64: 455BF1BF1FC4DF9A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAKIVKVIGR EIIDSRGNPT VEAEVHLEGG FVGLAAAPSG ASTGSREALE LRDGDKSRFL 

        70         80         90        100        110        120 
GKGVLKAVSA VNNEIAQAVV GKDASNQAEI DQIMIDLDGT DNKSKFGANA ILAVSLANAK 

       130        140        150        160        170        180 
AAAASKGLPL YAYIAELNGT PGQYSMPLPM MNIINGGEHA DNNVDIQEFM IQPVGAKTLR 

       190        200        210        220        230        240 
EAVRIGSEVF HNLAKVLKAK GYNTAVGDEG GFAPNLGSNA EALACIKEAV EKAGYTLGKD 

       250        260        270        280        290        300 
VTLAMDCASS EFYNKETGKY EMKGEGRSFT SQEFTHYLEE LCKQYPIVSI EDGQDESDWD 

       310        320        330        340        350        360 
GFAYQTKVLG DNVQLVGDDL FVTNTKILKE GIEKGIANSI LIKFNQIGSL TETLAAIKMA 

       370        380        390        400        410        420 
KDAGYTAVIS HRSGETEDAT IADLAVGTAA GQIKTGSMSR SDRVAKYNQL IRIEEALGDK 

       430 
APFLGLKAVK GQA

A6VR00 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