Reviewed, UniProtKB/Swiss-Prot B7H227 (ENO_ACIB3)

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:	ABBFA_001557

Organism

Acinetobacter baumannii (strain AB307-0294) [Complete proteome] [HAMAP]

Taxonomic identifier

557600 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	429 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 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
PTM	Phosphoprotein
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 – 429	429	Enolase HAMAP MF_00318		PRO_1000119561
Regions
	Region	368 – 371	4	Substrate binding By similarity
Sites
	Active site	208	1	Proton donor By similarity
	Active site	341	1	Proton acceptor By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	289	1	Magnesium By similarity
	Metal binding	316	1	Magnesium By similarity
	Binding site	158	1	Substrate By similarity
	Binding site	167	1	Substrate By similarity
	Binding site	289	1	Substrate By similarity
	Binding site	316	1	Substrate By similarity
	Binding site	341	1	Substrate (covalent); in inhibited form By similarity
	Binding site	392	1	Substrate By similarity
Amino acid modifications
	Modified residue	283	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B7H227-1 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: 0B30CADF8D47066B	FASTA	429	46,216
	10 20 30 40 50 60 MSQIVDIRAR EILDSRGNPT IEADVILESG VVGRACAPSG ASTGSREALE LRDGDKSRYL 70 80 90 100 110 120 GKGVRTAVQN VNSSIHELLV GQSVFEQKAL DEKMIAFDGT ENKSKLGANA TLAVSLAAAH 130 140 150 160 170 180 AAAAEQKLPL FQYIANLRGQ TTLTMPVPMM NILNGGAHAD NTVDIQEFMI EPVGFTSFAE 190 200 210 220 230 240 ALRAGAEVFH SLKSVLKKQG LNTAVGDEGG FAPNLRSNEE AITVILQAIE QTGYKAGSDI 250 260 270 280 290 300 MLALDCASSE FYKNGQYILE GEGNKSFTSN QFADYLAGLV KQYPIISIED GLDESDWEGW 310 320 330 340 350 360 SYLTSILGDK IQLVGDDLFV TNPKILQRGI DEKVGNSILI KYNQIGTLTE TLDAIYLAKA 370 380 390 400 410 420 NGYTTVISHR SGETEDSTIA DLAVGTAAGQ IKTGSLCRSD RVSKYNQLLR IEELTKAVYR GKAEFKGLN

References

[1]

"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii." Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R. J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP001172 Genomic DNA. Translation: ACJ58651.1.
RefSeq	YP_002325460.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7059105.
GenomeReviews	Gene locus ABBFA_001557 in contig CP001172_GR.
KEGG	abb:ABBFA_001557.
Organism-specific databases
CMR	Search...
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.
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO_ACIB3

Accession

Primary (citable) accession number: B7H227

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	June 16, 2009
This is version 6 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)