Q9CIT0 (ENO2_LACLA) 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
Synonyms:	enoB
Ordered Locus Names:	LL0276
ORF Names:	L0008

Organism

Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)

Taxonomic identifier

272623 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus

Protein attributes

Sequence length	422 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
PTM	Phosphoprotein
Technical term	Complete proteome Reference 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 – 422	422	Enolase 2 HAMAP MF_00318		PRO_0000133905
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)
	Q9CIT0 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 009091F066C7C8DF	FASTA	422	45,809
	10 20 30 40 50 60 MTVTIENIHA REIFDSRGNP TVEVDVRLTD GTLGRAAVPS GASTGDREAV ELRDGGDRLQ 70 80 90 100 110 120 GKGVSKAVAN VNGEIYEALK GQSPFNQAKL DHLMIELDGT KNKSRLGANA ILGVSMAISR 130 140 150 160 170 180 AAANSEKIPL YRYLGGVDLE LPQPFFNVIN GGVHADSGID VQEFLITPVK RESFRDGLEK 190 200 210 220 230 240 IANIYHTLKK ILADKGLETA VGDEGGFAPK LGSTENAIAT LYQAIESAGY VPGEEIAIAI 250 260 270 280 290 300 DPASSEFYDD KEKVYRFEGQ KLTSKELLTY YENLVEKYPA LISIEDGFSE HDWEGFAAQT 310 320 330 340 350 360 KAQGQKIQLV GDDIFVTNPE IFKEGIKKGV ANAILIKLNQ IGTVTEAIEA ISLARKAGYK 370 380 390 400 410 420 TMISHRSGET VDSYIADFAV AMHAGQIKTG SMARSERVEK YNQFLRIEEE LGKDVALASF PG

References

[1]	"The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis IL1403." Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J., Ehrlich S.D., Sorokin A. Genome Res. 11:731-753(2001) [PubMed: 11337471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: IL1403.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005176 Genomic DNA. Translation: AAK04374.1.
PIR	D86659.
RefSeq	NP_266432.1. NC_002662.1.
3D structure databases
ProteinModelPortal	Q9CIT0.
SMR	Q9CIT0. Positions 4-417.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1113886.
GenomeReviews	Gene locus LL0276 in contig AE005176_GR.
KEGG	lla:L0008.
NMPDR	fig|272623.1.peg.284.
PATRIC	22292736. VBILacLac136773_0302.
Phylogenomic databases
HOGENOM	HBG726599.
OMA	NVNTEIN.
ProtClustDB	PRK00077.
Enzyme and pathway databases
BioCyc	LLAC272623:L0008-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_LACLA

Accession

Primary (citable) accession number: Q9CIT0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	June 1, 2001
Last modified:	January 25, 2012
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program