Reviewed, UniProtKB/Swiss-Prot A0KGH3 (ENO_AERHH)

Names and origin

Protein names

Recommended name:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase

Gene names

Name:	eno
Ordered Locus Names:	AHA_0821

Organism

Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240) [Complete proteome] [HAMAP]

Taxonomic identifier

380703 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. HAMAP MF_00318
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. HAMAP MF_00318
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.
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: HAMAP
Cellular component	cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell phosphopyruvate hydratase complex Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphopyruvate hydratase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 433	433	Enolase HAMAP MF_00318		PRO_0000280832
Regions
	Region	370 – 373	4	Substrate binding By similarity
Sites
	Active site	209	1	Proton donor By similarity
	Active site	343	1	Proton acceptor By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	291	1	Magnesium By similarity
	Metal binding	318	1	Magnesium By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	291	1	Substrate By similarity
	Binding site	318	1	Substrate By similarity
	Binding site	343	1	Substrate (covalent); in inhibited form By similarity
	Binding site	394	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0KGH3-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: C311B54F0EFFB3D5	FASTA	433	45,720
	10 20 30 40 50 60 MSKIVKVIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRFL 70 80 90 100 110 120 GKGVLKALEA VNGPIAQALL GKDAKDQATV DQIMIDLDGT ENKSKFGANA ILAVSLANAK 130 140 150 160 170 180 AAAAAKGMPL YAHIAELNGT PGVYSMPLPM MNIINGGEHA DNNVDIQEFM IQPVGAKTLK 190 200 210 220 230 240 EAVRMGAEVF HNLAKVLKSK GYNTAVGDEG GFAPNLKSNA EALEVIAEAV AAAGYKLGTD 250 260 270 280 290 300 ITLAMDCAAS EFYDAEKKEY NLKGEGRVFT SNGFSDFLAD LTTKFPIVSI EDGLDESDWD 310 320 330 340 350 360 GFAYQTAELG KKIQIVGDDL FVTNTKILKR GIDNGIANSI LIKFNQIGSL TETLAAIKMA 370 380 390 400 410 420 KDAGYTAVIS HRSGETEDAT IADLAVGTAA GQIKTGSMSR SDRVAKYNQL IRIEEALGAK 430 APFRGLKEVK NQA

References

[1]

"Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades." Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F. J. Bacteriol. 188:8272-8282(2006) [PubMed: 16980456] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000462 Genomic DNA. Translation: ABK35864.1.
RefSeq	YP_855364.1.
3D structure databases
SMR	A0KGH3. Positions 2-433.
ModBase	Search...
Protein-protein interaction databases
STRING	A0KGH3.
Genome annotation databases
GeneID	4489301.
GenomeReviews	Gene locus AHA_0821 in contig CP000462_GR.
KEGG	aha:AHA_0821.
TIGR	AHA_0821.
Phylogenomic databases
OMA	DIAVGTN.
Family and domain databases
HAMAP	MF_00318. [Tree]
InterPro	IPR000941. Enolase. [Graphical view]
PANTHER	PTHR11902. Enolase. 1 hit.
Pfam	PF00113. Enolase_C. 1 hit. PF03952. Enolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF001400. Enolase. 1 hit.
PRINTS	PR00148. ENOLASE.
ProDom	PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO_AERHH

Accession

Primary (citable) accession number: A0KGH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	December 12, 2006
Last modified:	November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)