Q74J64 (ENO2_LACJO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Enolase 2
EC=4.2.1.11

Alternative name(s):
2-phospho-D-glycerate hydro-lyase 2
2-phosphoglycerate dehydratase 2

Gene names

Name:	eno2
Ordered Locus Names:	LJ_1246

Organism

Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) [Complete proteome] [HAMAP]

Taxonomic identifier

257314 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	428 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 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: 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 – 428	428	Enolase 2 HAMAP MF_00318		PRO_0000133902
Regions
	Region	364 – 367	4	Substrate binding By similarity
Sites
	Active site	204	1	Proton donor By similarity
	Active site	337	1	Proton acceptor By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	285	1	Magnesium By similarity
	Metal binding	312	1	Magnesium By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	285	1	Substrate By similarity
	Binding site	312	1	Substrate By similarity
	Binding site	337	1	Substrate (covalent); in inhibited form By similarity
	Binding site	388	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q74J64 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 7521EB6D22E689D8	FASTA	428	47,269
	10 20 30 40 50 60 MTVYVEKVRA LEIFDSRGNP TVEVHAYLSD GTVAKAEVPS GASTGEKEAV ELRDGGNRLQ 70 80 90 100 110 120 GKGVTQAVTN VNGPINDALK GLSPYNQAEI DRTMIKLDGT LNKAKLGANA ILGTSMAIAR 130 140 150 160 170 180 AAARSKDEPL YRYLGGCELE MPQTFHNVIN GGKHADNGID IQEFMITPVA KNSFRDGFEK 190 200 210 220 230 240 IVNTYHALKA VIEEAGFETG LGDEGGFAPN LNSSEEALKM LRKAIIKAGY KPRKDIAIAF 250 260 270 280 290 300 DAAASSFYNT EDGKYHFEGH IWNGEEMLQY YDKLLKEFPE IISCEDPFDE NDWENFEKFT 310 320 330 340 350 360 AKFGSTHQVV ADDNVCTNPK LVRKAIKDKL CNSILIKLNQ IGTITETLET IRLARKNNMT 370 380 390 400 410 420 TMVSHRSGET GDTFIADFTV ATNAGQLKSG APARSERVEK YNRLLEIENQ IGVENERLNH FPNNVDFD

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: CNCM I-1225 / La1 / NCC 533.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017198 Genomic DNA. Translation: AAS09067.1.
RefSeq	NP_965101.1. NC_005362.1.
3D structure databases
ProteinModelPortal	Q74J64.
SMR	Q74J64. Positions 5-423.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2742995.
GenomeReviews	Gene locus LJ_1246 in contig AE017198_GR.
KEGG	ljo:LJ1246.
NMPDR	fig|257314.1.peg.1087.
PATRIC	22238869. VBILacJoh1832_1112.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG726599.
OMA	DENDWEN.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	LJOH257314:LJ_1246-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

ENO2_LACJO

Accession

Primary (citable) accession number: Q74J64

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program