B0BQ53 (ENO_ACTPJ) 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:	APJL_1132

Organism

Actinobacillus pleuropneumoniae serotype 3 (strain JL03) [Complete proteome] [HAMAP]

Taxonomic identifier

434271 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	436 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 – 436	436	Enolase HAMAP MF_00318		PRO_1000115822
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
Amino acid modifications
	Modified residue	285	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0BQ53 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: FC4D3E10AB40AD40	FASTA	436	45,887
	10 20 30 40 50 60 MAKIVKVIGR EIIDSRGNPT VEAEVHLEGG FVGLAAAPSG ASTGSREALE LRDGDKSRFL 70 80 90 100 110 120 GKGVLKAVSA VNNEIAQAIL GKDGSAQTEI DQIMIDLDGT DNKSKFGANA ILAVSLATAK 130 140 150 160 170 180 AAAASKGLPL YAYIAELNGT PGVYSMPLPM MNIINGGEHA DNNVDIQEFM IQPVGASTLK 190 200 210 220 230 240 EALRIGAEVF HNLAKVLKSK GLNTAVGDEG GFAPNLASNA DALACIKEAV EKAGYVLGKD 250 260 270 280 290 300 VTLAMDCASS EFYNKENGLY EMKGEGKSFT SQEFTHYLEG LCNEYPIKSI EDGQDESDWE 310 320 330 340 350 360 GFAYQTKVLG GKIQLVGDDL FVTNTKILKE GIEKGIANSI LIKFNQIGSL TETLAAIKMA 370 380 390 400 410 420 KDAGYTAVIS HRSGETEDAT IADLAVGTAA GQIKTGSMSR SDRVAKYNQL IRIEEALAAA 430 GTPAPFNGLK EVKGQA

References

[1]

"Genome biology of Actinobacillus pleuropneumoniae JL03, an isolate of serotype 3 prevalent in China." Xu Z., Zhou Y., Li L., Zhou R., Xiao S., Wan Y., Zhang S., Wang K., Li W., Li L., Jin H., Kang M., Dalai B., Li T., Liu L., Cheng Y., Zhang L., Xu T. , Zheng H., Pu S., Wang B., Gu W., Zhang X.L., Zhu G.-F., Wang S., Zhao G.-P., Chen H. PLoS ONE 3:E1450-E1450(2008) [PubMed: 18197260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JL03.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000687 Genomic DNA. Translation: ABY69688.1.
RefSeq	YP_001652132.1. NC_010278.1.
3D structure databases
ProteinModelPortal	B0BQ53.
SMR	B0BQ53. Positions 2-436.
ModBase	Search...
Protein-protein interaction databases
STRING	B0BQ53.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5852811.
GenomeReviews	Gene locus APJL_1132 in contig CP000687_GR.
KEGG	apj:APJL_1132.
PATRIC	20751500. VBIActPle136345_1126.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG726599.
OMA	QEYMIMP.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	APLE434271:APJL_1132-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_ACTPJ

Accession

Primary (citable) accession number: B0BQ53

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	February 26, 2008
Last modified:	January 25, 2012
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program