B0V677 (ENO_ACIBY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase
2-phosphoglycerate dehydratase

Gene names

Name:	eno
Ordered Locus Names:	ABAYE1669

Organism

Acinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]

Taxonomic identifier

509173 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
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. HAMAP MF_00318
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. HAMAP MF_00318
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 cell surface By similarity. HAMAP MF_00318
Sequence similarities	Belongs to the enolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm Secreted
Ligand	Magnesium Metal-binding
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro phosphopyruvate hydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Enolase HAMAP MF_00318		PRO_1000115819
Regions
	Region	370 – 373	4	Substrate binding By similarity
Sites
	Active site	210	1	Proton donor By similarity
	Active site	343	1	Proton acceptor By similarity
	Metal binding	247	1	Magnesium By similarity
	Metal binding	291	1	Magnesium By similarity
	Metal binding	318	1	Magnesium By similarity
	Binding site	160	1	Substrate By similarity
	Binding site	169	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
Amino acid modifications
	Modified residue	285	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0V677 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: A4044ADB0E18CE2B	FASTA	431	46,495
	10 20 30 40 50 60 MFMSQIVDIR AREILDSRGN PTIEADVILE SGVVGRACAP SGASTGSREA LELRDGDKSR 70 80 90 100 110 120 YLGKGVRTAV QNVNSSIHEL LVGQSVFEQK ALDEKMIAFD GTENKSKLGA NATLAVSLAA 130 140 150 160 170 180 AHAAAAEQKL PLFQYIANLR GQTTLTMPVP MMNILNGGAH ADNTVDIQEF MIEPVGFTSF 190 200 210 220 230 240 AEALRAGAEV FHSLKSVLKK QGLNTAVGDE GGFAPNLRSN EEAITVILQA IEQTGYKAGS 250 260 270 280 290 300 DIMLALDCAS SEFYKNGQYI LEGEGNKSFT SNQFADYLAG LVKQYPIISI EDGLDESDWE 310 320 330 340 350 360 GWSYLTSILG DKIQLVGDDL FVTNPKILQR GIDEKVGNSI LIKYNQIGTL TETLDAIYLA 370 380 390 400 410 420 KANGYTTVIS HRSGETEDST IADLAVGTAA GQIKTGSLCR SDRVSKYNQL LRIEELTKAV 430 YRGKAEFKGL N

References

[1]

"Comparative analysis of Acinetobacters: three genomes for three lifestyles." Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S. PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AYE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU459141 Genomic DNA. Translation: CAM86561.1.
RefSeq	YP_001713561.1. NC_010410.1.
3D structure databases
ProteinModelPortal	B0V677.
SMR	B0V677. Positions 4-429.
ModBase	Search...
Protein-protein interaction databases
STRING	B0V677.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6003411.
GenomeReviews	Gene locus ABAYE1669 in contig CU459141_GR.
PATRIC	20726682. VBIAciBau69881_1659.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG726599.
OMA	QEYMIMP.
ProtClustDB	PRK00077.
Family and domain databases
HAMAP	MF_00318. Enolase. [Tree]
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [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.
TIGRFAMs	TIGR01060. Eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO_ACIBY

Accession

Primary (citable) accession number: B0V677

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 8, 2008
Last modified:	January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program