Reviewed, UniProtKB/Swiss-Prot Q0VQD6 (ENO_ALCBS)

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:	ABO_1164

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

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_0000266992
Regions
	Region	368 – 371	4	Substrate binding By similarity
Sites
	Active site	209	1	Proton donor By similarity
	Active site	341	1	Proton acceptor By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	289	1	Magnesium By similarity
	Metal binding	316	1	Magnesium By similarity
	Binding site	159	1	Substrate By similarity
	Binding site	168	1	Substrate By similarity
	Binding site	289	1	Substrate By similarity
	Binding site	316	1	Substrate By similarity
	Binding site	341	1	Substrate (covalent); in inhibited form By similarity
	Binding site	392	1	Substrate By similarity
Amino acid modifications
	Modified residue	283	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VQD6-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: FE68747AD14300CE	FASTA	430	46,032
	10 20 30 40 50 60 MSKIVDIKAR EILDSRGNPT IEADVILESG ASGSACAPSG ASTGSREALE LRDGDKSRYL 70 80 90 100 110 120 GKGVTKAVGN VNSAIRELLV GMEVSDQKAL DQAMLDADGT ENKGNLGANA ILAVSLAAAK 130 140 150 160 170 180 AAAVDQGKPL YEYISDLQDD DNEYSLPVPM MNIINGGEHA DNNVDIQEFM IQPVGAPTVA 190 200 210 220 230 240 EAIRYGAEIF HALKGVLKKR GLNTAVGDEG GFAPNLPSNE AALEAIMEAI EIAGYKAGDD 250 260 270 280 290 300 VTLALDCAAS EFYKDGKYVL AGEDRSMNSE EFADYLAELC DRYPIISIED GMDESDWDGW 310 320 330 340 350 360 KILTEKLGKK VQLVGDDLFV TNTRILQRGI DEKVANSILI KFNQIGSLTE TLDAIKMAKD 370 380 390 400 410 420 AGYTAVISHR SGETADTTIA DLAVATAAGQ IKTGSLCRSD RVAKYNRLIR IEQELGRAAY 430 HGRKEFKLLG

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL16612.1.
RefSeq	YP_692884.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4213348.
GenomeReviews	Gene locus ABO_1164 in contig AM286690_GR.
KEGG	abo:ABO_1164.
NMPDR	fig|393595.12.peg.1175.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VQD6.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1164-MON.
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_ALCBS

Accession

Primary (citable) accession number: Q0VQD6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	September 5, 2006
Last modified:	November 25, 2008
This is version 27 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)