Reviewed, UniProtKB/Swiss-Prot A3N1B9 (ENO_ACTP2)

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:	APL_1113

Organism

Actinobacillus pleuropneumoniae serotype 5b (strain L20) [Complete proteome] [HAMAP]

Taxonomic identifier

416269 [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. HAMAP MF_00318
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: 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 – 436	436	Enolase HAMAP MF_00318		PRO_1000019181
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)
	A3N1B9-1 [UniParc]. Last modified April 3, 2007. Version 1. Checksum: 9B9AE27CC5790370	FASTA	436	45,857
	10 20 30 40 50 60 MAKIVKVIGR EIIDSRGNPT VEAEVHLEGG FVGLAAAPSG ASTGSREALE LRDGDKSRFL 70 80 90 100 110 120 GKGVLKAVSA VNNEIAQAIL GKDGSAQAEI 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]	"The complete genome sequence of Actinobacillus pleuropneumoniae L20 (serotype 5b)." Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M., Nash J.H.E. J. Bacteriol. 190:1495-1496(2008) [PubMed: 18065534] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000569 Genomic DNA. Translation: ABN74205.1.
RefSeq	YP_001053810.1.
3D structure databases
SMR	A3N1B9. Positions 2-436.
ModBase	Search...
Protein-protein interaction databases
STRING	A3N1B9.
Genome annotation databases
GeneID	4849738.
GenomeReviews	Gene locus APL_1113 in contig CP000569_GR.
KEGG	apl:APL_1113.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HBG726599.
OMA	DIAVGTN.
PhylomeDB	A3N1B9.
Family and domain databases
HAMAP	MF_00318. Enolase. [Tree]
InterPro	IPR000941. Enolase. IPR020810. Enolase_C. IPR020809. Enolase_CS. IPR020811. Enolase_N. [Graphical view]
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_ACTP2

Accession

Primary (citable) accession number: A3N1B9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	April 3, 2007
Last modified:	February 9, 2010
This is version 28 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)