Reviewed, UniProtKB/Swiss-Prot Q88VW2 (ENO2_LACPL)

Names and origin

Protein names

Recommended name:
    Enolase 2
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 2
    2-phospho-D-glycerate hydro-lyase 2

Gene names

Name:	eno2
Synonyms:	enoA2, enoB
Ordered Locus Names:	lp_1920

Organism

Lactobacillus plantarum [Complete proteome] [HAMAP]

Taxonomic identifier

1590 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	429 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
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 2 HAMAP MF_00318		PRO_0000133907
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

Sequences

	Sequence		Length	Mass (Da)
	Q88VW2-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: A4548B6533D0AA05	FASTA	429	46,621
	10 20 30 40 50 60 MEKQVIETVK AREIFDSRGN PTVEADVILS DGTLGRAEVP SGASTGEKEA VELRDGGDRL 70 80 90 100 110 120 AGKGVLKAVN NVNTVINHAL HGADPFNQAH IDQIMIDLDG TPNKARLGAN AILGVSMATA 130 140 150 160 170 180 RAAANALQQP LYRYLGGTDL ELPQTFHNVI NGGEHADNGI DIQEFMITPV ERTSFRDGFE 190 200 210 220 230 240 KIVNTYHTLK KVIEDAGYTS GLGDEGGFAP DLKNSEEALQ MLHDAIIKAG YTPGKEIAIA 250 260 270 280 290 300 FDAAASYFYN RTTHNYDFEG KTYTPAALGD YYLQLLAKFP EIVSIEDPYG EEDWDNFASF 310 320 330 340 350 360 TAAHGDQLQI VADDPVCTNP QLIRQAIQRG MANNILIKLN QIGTVTETLA AIRLARKNGY 370 380 390 400 410 420 ATMMSHRSGE TGDTFVADFT VATNAAQLKA GAPARSERVE KYNQLLRIEE ELGADGARLA HFPNNVMFD

References

[1]

"Complete genome sequence of Lactobacillus plantarum WCFS1." Kleerebezem M., Boekhorst J., van Kranenburg R., Molenaar D., Kuipers O.P., Leer R., Tarchini R., Peters S.A., Sandbrink H.M., Fiers M.W.E.J., Stiekema W., Klein Lankhorst R.M., Bron P.A., Hoffer S.M., Nierop Groot M.N., Kerkhoven R., De Vries M., Ursing B., De Vos W.M., Siezen R.J. Proc. Natl. Acad. Sci. U.S.A. 100:1990-1995(2003) [PubMed: 12566566] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-793 / NCIMB 8826 / WCFS1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL935257 Genomic DNA. Translation: CAD64309.1.
RefSeq	NP_785460.1.
3D structure databases
SMR	Q88VW2. Positions 5-414.
ModBase	Search...
Genome annotation databases
GeneID	1061655.
KEGG	lpl:lp_1920.
NMPDR	fig|220668.1.peg.1594.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG726599.
OMA	NVNTEIN.
Enzyme and pathway databases
BioCyc	LPLA220668:LP_1920-MONOMER.
BRENDA	4.2.1.11. 593.
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

ENO2_LACPL

Accession

Primary (citable) accession number: Q88VW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 54 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)