Reviewed, UniProtKB/Swiss-Prot Q8GE63 (ENO_AERHY)

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

Organism

Aeromonas hydrophila

Taxonomic identifier

644 [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
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_0000133828
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)
	Q8GE63-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 73A7094B4718F399	FASTA	433	45,818
	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 VTLAMDCAAS EFYDAEKKEY NLKGEGRVFT SNGFSDFLEE LTAKFPIVSI EDGLDESDWE 310 320 330 340 350 360 GFAYQTQKLG KKIQIVGDDL FVTNTKILKR GIDNGIANSI LIKFNQIGSL TETLAAIKMA 370 380 390 400 410 420 KDAGYTAVIS HRSGETEDAT IADLAVGTAA GQIKTGSMSR SDRVAKYNQL IRIEEALGAK 430 APFRGLKEVK NQA

References

[1]

"Identification of a potentially new virulence gene enolase that is differentially expressed under in vitro versus in vivo growth conditions in Aeromonas hydrophila." Sha J., Galindo C.L., Pancholi V., Popov V.L., Chopra A.K. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY141757 Genomic DNA. Translation: AAN28926.1.
3D structure databases
HSSP	HSSP built from PDB template 1E9I based on UniProtKB P08324.
SMR	Q8GE63. Positions 2-433.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.11. 3060.
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_AERHY

Accession

Primary (citable) accession number: Q8GE63

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	March 1, 2003
Last modified:	June 16, 2009
This is version 45 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)