Reviewed, UniProtKB/Swiss-Prot P48285 (ENO_HELPY)

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:	HP_0154

Organism

Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP]

Taxonomic identifier

210 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	426 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 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: 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 – 426	426	Enolase HAMAP MF_00318		PRO_0000133897
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
Experimental info
	Sequence conflict	26	1	V → I Ref.2
	Sequence conflict	26	1	V → I Ref.3
	Sequence conflict	85	1	I → T in AAC43380. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P48285-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 7B7A0B87A5DFB398	FASTA	426	46,534
	10 20 30 40 50 60 MLTIKDIHAL EVMDSRGNPT IQASVVLSDN TKASAIVPSG ASTGKREALE LRDNDKTRFL 70 80 90 100 110 120 GKGVLRACEN VNSVIKHHLI GLEAINQAFV DERLRALDGT PNYANLGANA VLGVSMALAR 130 140 150 160 170 180 ASAKALNLPL YRYLGGANAL TLPVPMLNII NGGTHANNSI DFQEYMIMPL GFESFKEALR 190 200 210 220 230 240 ASAEVYHTLK KLLDGKNQLT SVGDEGGFAP NFSNNVEPLE VISQAIEKAG YKLGEEIALA 250 260 270 280 290 300 LDVASSELVD ENFNYHLKGE NKILDSHELV AYYKELVAKY PIVSIEDGLS EDDWEGWAFL 310 320 330 340 350 360 SKELGRQIQL VGDDLFVTNA SLLQKGIEKN IANAVLIKPN QIGTISETLE TIRLAKHHAY 370 380 390 400 410 420 QCVMSHRSGE SEDSFIADFA VALNTGEIKT GSTARSERIA KYNRLLEIEH ELKGGIYIGK ELFKHG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.
[2]	"Isolation of the Helicobacter pylori recA gene and involvement of the recA region in resistance to low pH." Thompson S.A., Blaser M.J. Infect. Immun. 63:2185-2193(1995) [PubMed: 7768597] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-178. Strain: ATCC 53726 / 84-183.
[3]	"Cloning of the Helicobacter pylori recA gene and functional characterization of its product." Schmitt W., Odenbreit S., Heuermann D., Haas R. Mol. Gen. Genet. 248:563-572(1995) [PubMed: 7476856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68. Strain: 69A.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000511 Genomic DNA. Translation: AAD07219.1. U13756 Genomic DNA. Translation: AAC43380.1. Z35478 Genomic DNA. No translation available.
PIR	S58684. B64539.
RefSeq	NP_206953.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3344N.
Genome annotation databases
GeneID	898806.
GenomeReviews	Gene locus HP_0154 in contig AE000511_GR.
KEGG	hpy:HP0154.
NMPDR	fig|85962.1.peg.151.
TIGR	HP_0154.
Phylogenomic databases
HOGENOM	P48285.
OMA	DIAVGTN
Enzyme and pathway databases
BRENDA	4.2.1.11. 1131.
Family and domain databases
HAMAP	MF_00318. [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_HELPY

Accession

Primary (citable) accession number: P48285

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	November 1, 1997
Last modified:	November 24, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)