Reviewed, UniProtKB/Swiss-Prot Q1ISS7 (ENO_ACIBL)

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:	Acid345_1070

Organism

Acidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]

Taxonomic identifier

204669 [NCBI]

Taxonomic lineage

Bacteria › Acidobacteria › Acidobacteriales › Acidobacteriaceae

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 + H(2)O.
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.
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: HAMAP extracellular region Inferred from electronic annotation. Source: UniProtKB-KW 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		PRO_0000266991
Regions
	Region	365 – 368	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	338	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	286	1	Magnesium By similarity
	Metal binding	313	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	286	1	Substrate By similarity
	Binding site	313	1	Substrate By similarity
	Binding site	338	1	Substrate (covalent); in inhibited form By similarity
	Binding site	389	1	Substrate By similarity
Amino acid modifications
	Modified residue	280	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q1ISS7-1 [UniParc]. Last modified June 13, 2006. Version 1. Checksum: 6B268DB6EFA38EC4	FASTA	433	46,524
	10 20 30 40 50 60 MFDITLVHAR EILDSRGNPT VEAEVTLSGG AVGRAAVPSG ASTGEHEAVE LRDGDNARYL 70 80 90 100 110 120 GKGVLKAVEN VEGEIAQALG GMDASQQRDI DMRMLDLDGT ENKGRLGANA ILAVSMASAR 130 140 150 160 170 180 AVANQLDIPL YRYLGGVNGN ILPVPMMNIL NGGAHADNNV DFQEFMAMPV GAESFSEALR 190 200 210 220 230 240 WGAEVFHTLK GVLKKRGYNT AVGDEGGFAP SLKSNVEAIE VILEAIQQAG YTPGEQIAIA 250 260 270 280 290 300 LDPAASEFFK DGKYIFKKSD KSEKTSEQMV RWWSDWANKY PIVSIEDGLA EDDWEGWKLL 310 320 330 340 350 360 TDELGDKIQL VGDDLFVTNP ERLARGIDNG VANSILIKVN QIGTLSETLD AIEMARRNGY 370 380 390 400 410 420 TAVISHRSGE TEDTFIADLA VATGAGQIKT GSASRTDRVA KYNQLLRIEE QLGAGARFLG 430 IGALNYDGDL SAE

References

[1]

"Complete sequence of Acidobacteria bacterium Ellin345." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Kiss H., Gilna P., Schmutz J. , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Kuske C., Janssen P.H., Richardson P. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000360 Genomic DNA. Translation: ABF40073.1.
RefSeq	YP_590147.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4070030.
GenomeReviews	Gene locus Acid345_1070 in contig CP000360_GR.
KEGG	aba:Acid345_1070.
NMPDR	fig|204669.6.peg.1057.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q1ISS7.
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_ACIBL

Accession

Primary (citable) accession number: Q1ISS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	June 13, 2006
Last modified:	November 25, 2008
This is version 24 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)