A1W4R1 (ENO_ACISJ) 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:	Ajs_0997

Organism

Acidovorax sp. (strain JS42) [Complete proteome] [HAMAP]

Taxonomic identifier

232721 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Acidovorax

Protein attributes

Sequence length	428 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 bacterial 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 – 428	428	Enolase HAMAP MF_00318		PRO_0000280831
Regions
	Region	365 – 368	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	338	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	286	1	Magnesium By similarity
	Metal binding	313	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	286	1	Substrate By similarity
	Binding site	313	1	Substrate By similarity
	Binding site	338	1	Substrate (covalent); in inhibited form By similarity
	Binding site	389	1	Substrate By similarity
Amino acid modifications
	Modified residue	280	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A1W4R1 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: BA71544D5339A583	FASTA	428	45,837
	10 20 30 40 50 60 MSAIVDIVGR EVLDSRGNPT VECDVLLESG VMGRAAVPSG ASTGSREAIE LRDGDKSRYL 70 80 90 100 110 120 GKGVLKAVEH INTEISEAVL GLDASEQGFL DKTLIDLDGT DNKSRLGANA MLAVSMAVAR 130 140 150 160 170 180 AAAEESGLPL YRYLGGMGSV QLPVPMMNVI NGGAHANNSL DLQEFMIIPV GAPSFREAVR 190 200 210 220 230 240 WGAEVFHALK KIIHDKGMST AVGDEGGFAP SVENHEAAIQ LILQAIEAAG YTAGEQIALG 250 260 270 280 290 300 LDCAASEFYK DGMYVLEGEG GLQLTAQQWT DMLASWCDKY PIISIEDGMH EGDWDGWKIL 310 320 330 340 350 360 TERLGHNVQL VGDDLFVTNT KILKEGIDKG IANSILIKIN QIGTLTETFA AIEMAKRAGY 370 380 390 400 410 420 TAVISHRSGE TEDSTIADIA VGTNAGQIKT GSLSRSDRIA KYNQLLRIEE DLGDIAFYPG RAAFYNLR

References

[1]

"Complete sequence of chromosome 1 of Acidovorax sp. JS42." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JS42.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000539 Genomic DNA. Translation: ABM41236.1.
RefSeq	YP_985312.1. NC_008782.1.
3D structure databases
ProteinModelPortal	A1W4R1.
SMR	A1W4R1. Positions 1-427.
ModBase	Search...
Protein-protein interaction databases
STRING	A1W4R1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4674385.
GenomeReviews	Gene locus Ajs_0997 in contig CP000539_GR.
KEGG	ajs:Ajs_0997.
PATRIC	20687272. VBIAciSp27161_1188.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HBG726599.
OMA	QEYMIMP.
PhylomeDB	A1W4R1.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	ASP232721:AJS_0997-MONOMER.
Family and domain databases
HAMAP	MF_00318. Enolase. [Tree]
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
KO	K01689.
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_ACISJ

Accession

Primary (citable) accession number: A1W4R1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	February 6, 2007
Last modified:	December 14, 2011
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program