Reviewed, UniProtKB/Swiss-Prot Q030Y9 (ENO2_LACLS)

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:	LACR_0668

Organism

Lactococcus lactis subsp. cremoris (strain SK11) [Complete proteome] [HAMAP]

Taxonomic identifier

272622 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	433 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 – 433	433	Enolase 2 HAMAP MF_00318		PRO_0000280858
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	243	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)
	Q030Y9-1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: DEA9ED13BED764FE	FASTA	433	46,912
	10 20 30 40 50 60 MSIITDIYAR EVLDSRGNPT LEVEVYTEDG AFGRGMVPSG ASTGEHEAVE LRDGDKSRYN 70 80 90 100 110 120 GLGTQKAVDN VNNIIAEAII GYEVTDQQAI DRAMIALDGT ENKGKLGANA ILGVSIAAAR 130 140 150 160 170 180 AAADELGVPL YNYLGGFNAK VLPTPMMNII NGGSHSDAPI AFQEFMIVPV GAPTFKEALR 190 200 210 220 230 240 WGAEIFHALK KILKARGLET AVGDEGGFAP KFDGTEDGVE TILKAIEAAG YKAGEDGVMI 250 260 270 280 290 300 GFDCASSEFY ENGVYDYTKF EGEGGKKLSA SEQVDYLEEL VSKYPIITIE DGMDENDWDG 310 320 330 340 350 360 WKILTERLGK KVQLVGDDFF VTNTKYLERG IRENASNAIL IKVNQIGTLT ETFEAIEMAK 370 380 390 400 410 420 EAGFTAIVSH RSGETEDSTI SDIAVATNAG QIKTGSLSRT DRMAKYNQLL RIEDQLAEVA 430 QYKGLKAFYN LKK

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
EMBLGenBankDDBJ	CP000425 Genomic DNA. Translation: ABJ72233.1.
RefSeq	YP_808655.1.
3D structure databases
SMR	Q030Y9. Positions 1-431.
ModBase	Search...
Protein-protein interaction databases
STRING	Q030Y9.
Genome annotation databases
GeneID	4433058.
GenomeReviews	Gene locus LACR_0668 in contig CP000425_GR.
KEGG	llc:LACR_0668.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	DIAVGTN.
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

ENO2_LACLS

Accession

Primary (citable) accession number: Q030Y9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	November 14, 2006
Last modified:	November 3, 2009
This is version 29 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)