Reviewed, UniProtKB/Swiss-Prot Q042F4 (ENO2_LACGA)

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
Ordered Locus Names:	LGAS_1305

Organism

Lactobacillus gasseri (strain ATCC 33323 / DSM 20243) [Complete proteome] [HAMAP]

Taxonomic identifier

324831 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length	432 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 – 432	432	Enolase 2 HAMAP MF_00318		PRO_0000280856
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)
	Q042F4-1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 8567FD11E2EC934C	FASTA	432	46,911
	10 20 30 40 50 60 MSVITDIHAR EVLDSRGNPT VEAEVYTELG GFGRAIVPSG ASTGEHEAVE LRDGDKSRFG 70 80 90 100 110 120 GQGVLTAVEN VNGEIAKAVI GLDVTDQRLI DQTMIDLDGT PNKGRLGANA ILSVSLASAR 130 140 150 160 170 180 AAADELGLPL YEYLGGPNAH VLPTPMMNVI NGGKHADNNV DIQEFMIMPV GAKSLHEAVR 190 200 210 220 230 240 MGAETFHTLK GLLQERGEST AVGDEGGFAP NLKNNEEPFE ILVEAIQRAG YKPGQDIAIA 250 260 270 280 290 300 FDCAASEFYN KDTKKYVTVA DGREYTAEEW TSLIEDLVDK YPVISVEDPL DENDWEGWKT 310 320 330 340 350 360 FTERLGDKVQ IVGDDLFVTN TSYLEKGIKM GVANSILIKL NQIGTLTETF EAIEMAKEAG 370 380 390 400 410 420 YTAVVSHRSG ETEDTTIADL VVATNAGQIK TGSMSRTDRI AKYNQLMRIE EALGSTAQYK 430 GIHSFYNLHK QF

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000413 Genomic DNA. Translation: ABJ60668.1.
RefSeq	YP_815106.1.
3D structure databases
SMR	Q042F4. Positions 2-428.
ModBase	Search...
Protein-protein interaction databases
STRING	Q042F4.
Genome annotation databases
GeneID	4439494.
GenomeReviews	Gene locus LGAS_1305 in contig CP000413_GR.
KEGG	lga:LGAS_1305.
NMPDR	fig|1596.1.peg.1573.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HBG726599.
OMA	DIAVGTN.
PhylomeDB	Q042F4.
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_LACGA

Accession

Primary (citable) accession number: Q042F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	November 14, 2006
Last modified:	February 9, 2010
This is version 32 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)