Reviewed, UniProtKB/Swiss-Prot A0LW71 (ENO_ACIC1)

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:	Acel_1909

Organism

Acidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]

Taxonomic identifier

351607 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Frankineae › Acidothermaceae › Acidothermus

Protein attributes

Sequence length	429 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 – 429	429	Enolase HAMAP MF_00318		PRO_0000280829
Regions
	Region	361 – 364	4	Substrate binding By similarity
Sites
	Active site	204	1	Proton donor By similarity
	Active site	334	1	Proton acceptor By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	282	1	Magnesium By similarity
	Metal binding	309	1	Magnesium By similarity
	Binding site	154	1	Substrate By similarity
	Binding site	163	1	Substrate By similarity
	Binding site	282	1	Substrate By similarity
	Binding site	309	1	Substrate By similarity
	Binding site	334	1	Substrate (covalent); in inhibited form By similarity
	Binding site	385	1	Substrate By similarity
Amino acid modifications
	Modified residue	276	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LW71-1 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 64B845854D47F90E	FASTA	429	45,415
	10 20 30 40 50 60 MAVIEAIGAR EILDSRGNPT VEVEVLLDDG TVGRAAVPSG ASTGAFEAVE KRDGDDRYGG 70 80 90 100 110 120 KGVRQAVQAV TDQIAPEIIG FDATEQRVLD ARLIELDGTP NKSRLGANAI LGVSMAVARA 130 140 150 160 170 180 AADSADLPLF RYLGGPNAHL LPVPMMNILN GGAHADSNVD IQEFLIAPIG AATFAEALRY 190 200 210 220 230 240 GVETYHALKA VLKGRGLATG LGDEGGFAPN LAHNREALDL ILEAIGKAGF RPGRDIAVAI 250 260 270 280 290 300 DAAATEFYRD GRYILEGQPR TAAELIRYYE ELVASYPLVS LEDPLAEEDW DGWRELTAAL 310 320 330 340 350 360 GGTVQLVGDD IFVTNPERIS RGIQTSVANA VLIKLNQIGT VTETLDAVEL AHRAGYRTMI 370 380 390 400 410 420 SHRSGETEDT TIADVAVATN AGQIKTGAPA RSERVAKYNQ LLRIEEELDD AARYAGVAAF PRFAGGSAG

References

[1]

"Complete sequence of Acidothermus cellulolyticus 11B." 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., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000481 Genomic DNA. Translation: ABK53681.1.
RefSeq	YP_873667.1.
3D structure databases
SMR	A0LW71. Positions 2-420.
ModBase	Search...
Protein-protein interaction databases
STRING	A0LW71.
Genome annotation databases
GeneID	4485556.
GenomeReviews	Gene locus Acel_1909 in contig CP000481_GR.
KEGG	ace:Acel_1909.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0148.
HOGENOM	HBG726599.
OMA	RDAMRIG.
PhylomeDB	A0LW71.
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

ENO_ACIC1

Accession

Primary (citable) accession number: A0LW71

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	December 12, 2006
Last modified:	February 9, 2010
This is version 28 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)