Reviewed, UniProtKB/Swiss-Prot Q032H8 (ENO1_LACLS)

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:	LACR_0283

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	418 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 – 418	418	Enolase 1 HAMAP MF_00318		PRO_0000280857
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
Amino acid modifications
	Modified residue	278	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q032H8-1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 7C84D587CC74144D	FASTA	418	45,336
	10 20 30 40 50 60 MTVTIENIHA REIFDSRGNP TVEVDVRLTD GTLGRAAVPS GASTGDREAV ELRDGGARLQ 70 80 90 100 110 120 GKDVSKAVAN VNGEIYEALK GQSPFNQAKL DHLMIELDGT KNKSRLGANA ILGVSMAIAR 130 140 150 160 170 180 AAANSEKIPL YRYLGGVDLE LPQPFFNVIN GGVHADSGID VQEFLITPVK RASFRDGLEK 190 200 210 220 230 240 IANIYHTLKK ILADKGLETA VGDEGGFAPK LGSTENAIAT LYQAIERAGY VPGEEIAIAI 250 260 270 280 290 300 DPASSEFYDD KEKVYHFEGQ KLTSAELLTY YEGLVEKYPA LISIEDGFSE HDWAGFAAQT 310 320 330 340 350 360 KVQGQKIQLV GDDIFVTNPE IFKEGIQKGV ANAILIKLNQ IGTVTEAIEA ISLARKAGYK 370 380 390 400 410 TMISHRSGET VDSFIADFAV AMHAGQIKTG SMARSERVEK YNQFLRIEEE LLGLEVTK

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	CP000425 Genomic DNA. Translation: ABJ71894.1.
RefSeq	YP_808316.1.
3D structure databases
SMR	Q032H8. Positions 4-412.
ModBase	Search...
Protein-protein interaction databases
STRING	Q032H8.
Genome annotation databases
GeneID	4434437.
GenomeReviews	Gene locus LACR_0283 in contig CP000425_GR.
KEGG	llc:LACR_0283.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HBG726599.
OMA	NVNTEIN.
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_LACLS

Accession

Primary (citable) accession number: Q032H8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	November 14, 2006
Last modified:	February 9, 2010
This is version 33 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)