Reviewed, UniProtKB/Swiss-Prot Q88YH3 (ENO1_LACPL)

Names and origin

Protein names

Recommended name:
    Enolase 1
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase 1
    2-phospho-D-glycerate hydro-lyase 1

Gene names

Name:	eno1
Synonyms:	enoA, enoA1
Ordered Locus Names:	lp_0792

Organism

Lactobacillus plantarum [Complete proteome] [HAMAP]

Taxonomic identifier

1590 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	442 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 – 442	442	Enolase 1 HAMAP MF_00318		PRO_0000133906
Regions
	Region	369 – 372	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	342	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	290	1	Magnesium By similarity
	Metal binding	317	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	290	1	Substrate By similarity
	Binding site	317	1	Substrate By similarity
	Binding site	342	1	Substrate (covalent); in inhibited form By similarity
	Binding site	393	1	Substrate By similarity
Amino acid modifications
	Modified residue	284	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q88YH3-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: B4FD3E75AA7359D4	FASTA	442	48,030
	10 20 30 40 50 60 MSIITDIYAR EVLDSRGNPT VEVELYTESG AFGRGIVPSG ASTGEHEAVE LRDGDKSRFM 70 80 90 100 110 120 GKGVTKAVDN VNKLIAKEIV GYDVTDQRAI DQAMIKLDGT PNKAKLGANA ILGVSIAAAR 130 140 150 160 170 180 AAADELEMPL YNYLGGFNAH VLPTPMMNVI NGGAHANNDV DFQEFMIMPV GASSVKEAIR 190 200 210 220 230 240 MGSETFHNLK AILNERGYST AVGDEGGFAP DLKNNEEPFE ILVEAIERAG YKPGKDIAIA 250 260 270 280 290 300 FDCAASEFYN EETGKYDLKG EGENGQSFTA EEFVDLLDSI VDKYPIVSIE DPLDENNWED 310 320 330 340 350 360 WQMATAKLGK KVQIVGDDLF VTNTDYLAKG IKMGVANSIL IKVNQIGTLT ETVEAIEMAK 370 380 390 400 410 420 EAGYTAIVSH RSGETEDTTI ADLVVAMNAG QIKTGSMSRT ERIAKYNQLM RIEDQLESTS 430 440 EYKGIHGFYN LDEAARNTIT SK

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	AL935254 Genomic DNA. Translation: CAD63380.1.
RefSeq	NP_784537.1.
3D structure databases
SMR	Q88YH3. Positions 2-434.
ModBase	Search...
Genome annotation databases
GeneID	1063808.
KEGG	lpl:lp_0792.
NMPDR	fig|220668.1.peg.671.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG726599.
OMA	DIAVGTN.
Enzyme and pathway databases
BioCyc	LPLA220668:LP_0792-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

ENO1_LACPL

Accession

Primary (citable) accession number: Q88YH3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2003
Last sequence update:	June 1, 2003
Last modified:	February 9, 2010
This is version 56 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)