Reviewed, UniProtKB/Swiss-Prot Q9CHS7 (ENO1_LACLA)

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
Synonyms:	enoA
Ordered Locus Names:	LL0644
ORF Names:	L0007

Organism

Lactococcus lactis subsp. lactis (Streptococcus lactis) [Complete proteome] [HAMAP]

Taxonomic identifier

1360 [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 1 HAMAP MF_00318		PRO_0000133904
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)
	Q9CHS7-1 [UniParc]. Last modified June 1, 2001. 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]

"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE006297 Genomic DNA. Translation: AAK04742.1.
PIR	D86705.
RefSeq	NP_266800.1.
3D structure databases
HSSP	HSSP built from PDB template 1OEP based on UniProtKB Q9NDH8.
SMR	Q9CHS7. Positions 1-431.
ModBase	Search...
Genome annotation databases
GeneID	1114264.
GenomeReviews	Gene locus LL0644 in contig AE005176_GR.
KEGG	lla:L0007.
NMPDR	fig|272623.1.peg.659.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q9CHS7.
OMA	Q9CHS7. DIAVGTN.
Enzyme and pathway databases
BioCyc	LLAC272623:L0007-MON.
BRENDA	4.2.1.11. 278870.
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

ENO1_LACLA

Accession

Primary (citable) accession number: Q9CHS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 27, 2002
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 57 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)