Reviewed, UniProtKB/Swiss-Prot A6TU30 (ENO_ALKMQ)

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:	Amet_3576

Organism

Alkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]

Taxonomic identifier

293826 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Alkaliphilus

Protein attributes

Sequence length	430 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 – 430	430	Enolase		PRO_1000059453
Regions
	Region	366 – 369	4	Substrate binding By similarity
Sites
	Active site	205	1	Proton donor By similarity
	Active site	339	1	Proton acceptor By similarity
	Metal binding	242	1	Magnesium By similarity
	Metal binding	287	1	Magnesium By similarity
	Metal binding	314	1	Magnesium By similarity
	Binding site	155	1	Substrate By similarity
	Binding site	164	1	Substrate By similarity
	Binding site	287	1	Substrate By similarity
	Binding site	314	1	Substrate By similarity
	Binding site	339	1	Substrate (covalent); in inhibited form By similarity
	Binding site	390	1	Substrate By similarity
Amino acid modifications
	Modified residue	281	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6TU30-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: C48F6090BBD05164	FASTA	430	46,416
	10 20 30 40 50 60 MTIISDVYAR EVLDSRGNPT IEVEVYLESG VLGRAIVPSG ASTGAFEAVE LRDGDKGRYL 70 80 90 100 110 120 GKGVLKAVEN VNDIIAPEIT GLDALDQVAI DKIMLDLDGT PNKAKLGANA ILGVSMAVAK 130 140 150 160 170 180 AAAEALDIPL FQYLGGVNAK QLPVPMMNIL NGGSHADNNV DIQEFMVMPV GAKTFKEALR 190 200 210 220 230 240 MGTEIYHNLK DVLKSKGLAT GVGDEGGFAP NLSSNEEALQ IIMEAIEAAG YKPGVDIKLA 250 260 270 280 290 300 LDVAATEFYD EDEKLYKLTG EGVTKTAEEM VDFYEALVKK YPIVSIEDGL SEDDWEGWRV 310 320 330 340 350 360 MTERLGDNIQ IVGDDLFVTN TERLKKGIQT KTANSILVKL NQIGTITETL DAIEMAKRAG 370 380 390 400 410 420 YTTVISHRSG ETEDATIADI AVAVNAGQIK TGAPARTDRV AKYNQLLRIE DMLGFTGQYI 430 GNEVFYNIKK

References

[1]

"Complete sequence of Alkaliphilus metalliredigens QYMF." 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., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000724 Genomic DNA. Translation: ABR49698.1.
RefSeq	YP_001321357.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5313657.
GenomeReviews	Gene locus Amet_3576 in contig CP000724_GR.
KEGG	amt:Amet_3576.
Organism-specific databases
CMR	Search...
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_ALKMQ

Accession

Primary (citable) accession number: A6TU30

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	August 21, 2007
Last modified:	November 25, 2008
This is version 16 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)