ECOLI:ENO

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Species (Taxon ID)	Escherichia coli (strain K12). (taxon:83333)
Gene Name(s)	eno
Protein Name(s)	Enolase 2-phospho-D-glycerate hydro-lyase 2-phosphoglycerate dehydratase
External Links
UniProt Identifier	ENO_ECOLI
UniProt Accessions	P0A6P9, P08324, Q2MA53,
EMBL	X82400, U29580, U00096, AP009048, M12843,
PIR	G65059,
RefSeq	AP_003345.1, NP_417259.1,
PDB	1E9I, 2FYM, 3H8A,
IntAct	P0A6P9,
Pfam	PF00113, PF03952,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0009986	cell surface		IEA: Inferred from Electronic Annotation		C	Source: UniProtKB-SubCell
	GO:0005856	cytoskeleton		IEA: Inferred from Electronic Annotation		C	Source: UniProtKB-SubCell
	GO:0005576	extracellular region		IEA: Inferred from Electronic Annotation		C	Source: UniProtKB-SubCell
	GO:0016020	membrane		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0000015	phosphopyruvate hydratase complex		IEA: Inferred from Electronic Annotation		C	Source: InterPro
	GO:0042802	identical protein binding		IPI: Inferred from Physical Interaction		F	Source: IntAct
	GO:0000287	magnesium ion binding		IDA: Inferred from Direct Assay		F	Source: EcoliWiki
	GO:0004634	phosphopyruvate hydratase activity		IDA: Inferred from Direct Assay		F	Source: EcoliWiki
	GO:0006096	glycolysis		IMP: Inferred from Mutant Phenotype		P	Source: EcoliWiki
	GO:0004634	phosphopyruvate hydratase activity	PMID:368027^[1]	IMP: Inferred from Mutant Phenotype		F	Table 4. A mutant strain that does not contain eno has a significantly lower level of phosphopyruvate hydratase activity than the wild type.	complete
	GO:0000015	phosphopyruvate hydratase complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000941	C
	GO:0000015	phosphopyruvate hydratase complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020809	C
	GO:0000015	phosphopyruvate hydratase complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020810	C
	GO:0000015	phosphopyruvate hydratase complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020811	C
	GO:0000287	magnesium ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000941	F
	GO:0000287	magnesium ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020809	F
	GO:0000287	magnesium ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020810	F
	GO:0000287	magnesium ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020811	F
	GO:0000287	magnesium ion binding	PMID:16516921^[2]	IDA: Inferred from Direct Assay		F
	GO:0004634	phosphopyruvate hydratase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000941	F
	GO:0004634	phosphopyruvate hydratase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020809	F
	GO:0004634	phosphopyruvate hydratase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020810	F
	GO:0004634	phosphopyruvate hydratase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020811	F
	GO:0004634	phosphopyruvate hydratase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:4.2.1.11	F
	GO:0004634	phosphopyruvate hydratase activity	PMID:12054465^[3]	IMP: Inferred from Mutant Phenotype		F
	GO:0004634	phosphopyruvate hydratase activity	PMID:4942326^[4]	IDA: Inferred from Direct Assay		F
	GO:0005515	protein binding	PMID:15236960^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P21513	F
	GO:0005515	protein binding	PMID:16516921^[2]	IPI: Inferred from Physical Interaction	EcoliWiki:eno	F
	GO:0005515	protein binding	PMID:16516921^[2]	IPI: Inferred from Physical Interaction	EcoliWiki:rne	F
	GO:0005576	extracellular region	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0964	C
	GO:0005576	extracellular region	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0243	C
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005829	cytosol	PMID:16858726^[6]	IDA: Inferred from Direct Assay		C
	GO:0005856	cytoskeleton	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0206	C
	GO:0005856	cytoskeleton	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0090	C
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000941	P
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020809	P
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020810	P
	GO:0006096	glycolysis	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020811	P
	GO:0006096	glycolysis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0324	P
	GO:0006096	glycolysis	PMID:410789^[7]	IMP: Inferred from Mutant Phenotype		P
	GO:0009986	cell surface	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0310	C
	GO:0016020	membrane	PMID:16858726^[6]	IDA: Inferred from Direct Assay		C
	GO:0016829	lyase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0456	F
	GO:0042802	identical protein binding	PMID:15236960^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P0A6P9	F
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Thomson J et al. (1979) ColE1 hybrid plasmids for Escherichia coli genes of glycolysis and the hexose monophosphate shunt. J Bacteriol 137: 502-6 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Chandran V & Luisi BF (2006) Recognition of enolase in the Escherichia coli RNA degradosome. J Mol Biol 358: 8-15 PubMed GONUTS page
↑ Poyner RR et al. (2002) Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase. Arch Biochem Biophys 401: 155-63 PubMed GONUTS page
↑ Spring TG & Wold F (1971) The purification and characterization of Escherichia coli enolase. J Biol Chem 246: 6797-802 PubMed GONUTS page
↑ ^5.0 ^5.1 Callaghan AJ et al. (2004) Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J Mol Biol 340: 965-79 PubMed GONUTS page
↑ ^6.0 ^6.1 Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed GONUTS page
↑ Irani MH & Maitra PK (1977) Properties of Escherichia coli mutants deficient in enzymes of glycolysis. J Bacteriol 132: 398-410 PubMed GONUTS page

[PMID:368027-0] Thomson J et al. (1979) ColE1 hybrid plasmids for Escherichia coli genes of glycolysis and the hexose monophosphate shunt. J Bacteriol 137: 502-6 PubMed GONUTS page

[PMID:16516921-1] 2.0 ^2.1 ^2.2 Chandran V & Luisi BF (2006) Recognition of enolase in the Escherichia coli RNA degradosome. J Mol Biol 358: 8-15 PubMed GONUTS page

[PMID:12054465-2] Poyner RR et al. (2002) Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase. Arch Biochem Biophys 401: 155-63 PubMed GONUTS page

[PMID:4942326-3] Spring TG & Wold F (1971) The purification and characterization of Escherichia coli enolase. J Biol Chem 246: 6797-802 PubMed GONUTS page

[PMID:15236960-4] 5.0 ^5.1 Callaghan AJ et al. (2004) Studies of the RNA degradosome-organizing domain of the Escherichia coli ribonuclease RNase E. J Mol Biol 340: 965-79 PubMed GONUTS page

[PMID:16858726-5] 6.0 ^6.1 Lasserre JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27: 3306-21 PubMed GONUTS page

[PMID:410789-6] Irani MH & Maitra PK (1977) Properties of Escherichia coli mutants deficient in enzymes of glycolysis. J Bacteriol 132: 398-410 PubMed GONUTS page

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ECOLI:ENO

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