Reviewed, UniProtKB/Swiss-Prot Q74K78 (ENO1_LACJO)

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
Ordered Locus Names:	LJ_0875

Organism

Lactobacillus johnsonii [Complete proteome] [HAMAP]

Taxonomic identifier

33959 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
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.
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.
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 – 432	432	Enolase 1 HAMAP MF_00318		PRO_0000133901
Regions
	Region	366 – 369	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	339	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	287	1	Magnesium By similarity
	Metal binding	314	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	287	1	Substrate By similarity
	Binding site	314	1	Substrate By similarity
	Binding site	339	1	Substrate (covalent); in inhibited form By similarity
	Binding site	390	1	Substrate By similarity
Amino acid modifications
	Modified residue	281	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q74K78-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 48F322BE095258C2	FASTA	432	47,072
	10 20 30 40 50 60 MSVITDIHAR EVLDSRGNPT VEAEVYTELG GFGRAIVPSG ASTGEHEAVE LRDGDKSRFL 70 80 90 100 110 120 GQGVLTAVEN VNGEIAKAVI GLDVTDQRLI DQTMIDLDGT PNKGRLGANA MLAVSLASAR 130 140 150 160 170 180 AAADELGLPL YEYLGGPNAH VLPTPMMNVI NGGKHADNNV DIQEFMIMPV GAKSLHEAVR 190 200 210 220 230 240 MGAETFHTLK SLLQERGEST AVGDEGGFAP NLKNNEEPFE ILVEAIQRAG YKPGQDISIA 250 260 270 280 290 300 FDCAASEFYN KDTKKYVTVA DGREYTAEEW TSLMEDIVDK YPVISIEDPL DENDWEGWKV 310 320 330 340 350 360 FTERLGDKVQ IVGDDLFVTN TNYLEKGIKM GVANSILIKL NQIGTLTETF EAIEMAKEAG 370 380 390 400 410 420 YTAVVSHRSG ETEDTTIADL VVATNAGQIK TGSMSRTDRI AKYNQLMRIE EALGSTAQYK 430 GIHSFYNLHK QF

References

[1]

"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533." Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A. Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed: 14983040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 533.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE017198 Genomic DNA. Translation: AAS08696.1.
RefSeq	NP_964730.1.
3D structure databases
SMR	Q74K78. Positions 2-428.
ModBase	Search...
Genome annotation databases
GeneID	2742817.
GenomeReviews	Gene locus LJ_0875 in contig AE017198_GR.
KEGG	ljo:LJ0875.
NMPDR	fig|257314.1.peg.716.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q74K78.
OMA	DIAVGTN.
Enzyme and pathway databases
BioCyc	LJOH257314:LJ_0875-MON.
BRENDA	4.2.1.11. 141476.
Family and domain databases
HAMAP	MF_00318. [Tree]
InterPro	IPR000941. Enolase. [Graphical view]
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.
ProDom	PD000902. Enolase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01060. eno. 1 hit.
PROSITE	PS00164. ENOLASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ENO1_LACJO

Accession

Primary (citable) accession number: Q74K78

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 46 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)