NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Reith M.E., Singh R.K., Curtis B., Boyd J., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J., Johnson S., Brown L.;
"The genome sequence of Aeromonas salmonicida subsp. salmonicida A449.";
Submitted (MAR-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

CP000644; ABO91443.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001143191.1; -.

3D structure databases

ModBase

A4SRC1.

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

4996844; -.

GenomeReviews

CP000644_GR; ASA_3475.

KEGG

asa:ASA_3475; -.

CMR

A4SRC1; ASA_3475.

Other

ProtoNet

A4SRC1.

UniRef

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

Keywords

Complete proteome; Cytoplasm; Glycolysis; Lyase; Magnesium; Metal-binding; Secreted.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 433`	`433`	`Enolase.`	`PRO_1000019182`
`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).`

Sequence information

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

Molecular weight: 45736 Da [This is the MW of the unprocessed precursor]

CRC64: 03F29464410F376E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKIVKVIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRFL 

        70         80         90        100        110        120 
GKGVLKALEA VNGPIAQALL GKDAKDQAAI DQIMIDLDGT ENKSKFGANA ILAVSLANAK 

       130        140        150        160        170        180 
AAAAAKGMPL YAHIAELNGT AGVYSMPLPM MNIINGGEHA DNNVDIQEFM IQPVGAKTLK 

       190        200        210        220        230        240 
EAVRMGAEVF HNLAKVLKSK GYNTAVGDEG GFAPNLKSNA EALEVIAEAV AAAGYVLGKD 

       250        260        270        280        290        300 
ITLAMDCAAS EFYDAEKKEY NLKGEGRIFT SNEFSDYLAD LTTKFPIVSI EDGLDESDWD 

       310        320        330        340        350        360 
GFAYQTKELG KKIQIVGDDL FVTNTKILKR GIDNGIANSI LIKFNQIGSL TETLAAIKMA 

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

       430 
APFNGLKEVK GQA

A4SRC1 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