Reviewed, UniProtKB/Swiss-Prot A9NF93 (ENO_ACHLI)

Names and origin

Protein names

Recommended name:
    Enolase
    EC=4.2.1.11
Alternative name(s):
    2-phosphoglycerate dehydratase
    2-phospho-D-glycerate hydro-lyase

Gene names

Name:	eno
Ordered Locus Names:	ACL_0402

Organism

Acholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]

Taxonomic identifier

441768 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	431 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 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 – 431	431	Enolase HAMAP MF_00318		PRO_1000079120
Regions
	Region	367 – 370	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	340	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	288	1	Magnesium By similarity
	Metal binding	315	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	288	1	Substrate By similarity
	Binding site	315	1	Substrate By similarity
	Binding site	340	1	Substrate (covalent); in inhibited form By similarity
	Binding site	391	1	Substrate By similarity
Amino acid modifications
	Modified residue	282	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9NF93-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: ED267A606B57B74B	FASTA	431	46,517
	10 20 30 40 50 60 MPFITSVYAR EVLDSRGNPT VEVEIVTDSG AFGRTLVPSG ASTGEHEAVE LRDGDKSRYL 70 80 90 100 110 120 GKGVLKAVEN VNDIIGPAIL GDSVLDQVAL DRKLIALDGT KNKGKLGANA ILGVSIAAAK 130 140 150 160 170 180 AAADLLNLEL YQYLGGFNAK QLPVPMMNII NGGAHSDAPI DFQEFMIFPV GAPSFKEAIR 190 200 210 220 230 240 WGAEIFHALK AILKKKGLST AVGDEGGFAP NLASNEDTID NILEAIKNAG YKAGEEVFIG 250 260 270 280 290 300 FDVAASEFFD KAKGKYVFKK STKEEFTSAE LVEYYAGLVQ KYPIISIEDG MDENDWDGWK 310 320 330 340 350 360 LLTDKLGSKI QLVGDDLFVT NTEYLARGIK TNTANSILVK VNQIGTLTET FDAIEMAKRA 370 380 390 400 410 420 GYTAVISHRS GETEDTTIAD IAVAANTGQI KTGSASRTDR VAKYNQLMRI EDQLGEDAVY 430 LGKDSFYNLK K

References

[1]

"Acholeplasma laidlawii complete genome." Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.A., Kostrjukova E.S., Selezneva O.V., Vtyurin N.N., Rogov S.I., Alekseev D.G., Ladygina V.G. , Titova G.A., Karpov V.A., Govorun V.M. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000896 Genomic DNA. Translation: ABX81023.1.
RefSeq	YP_001620399.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5803119.
GenomeReviews	Gene locus ACL_0402 in contig CP000896_GR.
KEGG	acl:ACL_0402.
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

ENO_ACHLI

Accession

Primary (citable) accession number: A9NF93

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 5, 2008
Last modified:	November 3, 2009
This is version 15 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)