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ECOLI:ENO

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) eno (ECO:0000255 with HAMAP-Rule:MF_00318)
Protein Name(s) Enolase (ECO:0000255 with HAMAP-Rule:MF_00318)

2-phospho-D-glycerate hydro-lyase (ECO:0000255 with HAMAP-Rule:MF_00318) 2-phosphoglycerate dehydratase (ECO:0000255 with HAMAP-Rule:MF_00318)

External Links
UniProt P0A6P9
EMBL X82400
U29580
U00096
AP009048
M12843
PIR G65059
RefSeq NP_417259.1
YP_490987.1
PDB 1E9I
2FYM
3H8A
PDBsum 1E9I
2FYM
3H8A
ProteinModelPortal P0A6P9
SMR P0A6P9
DIP DIP-31847N
IntAct P0A6P9
MINT MINT-1230935
STRING 511145.b2779
PhosSite P010423
SWISS-2DPAGE P0A6P9
PaxDb P0A6P9
PRIDE P0A6P9
EnsemblBacteria AAC75821
BAE76853
GeneID 12933303
945032
KEGG ecj:Y75_p2716
eco:b2779
PATRIC 32120974
EchoBASE EB0254
EcoGene EG10258
eggNOG COG0148
HOGENOM HOG000072173
InParanoid P0A6P9
KO K01689
OMA NLPLYRY
OrthoDB EOG65J589
PhylomeDB P0A6P9
BioCyc EcoCyc:ENOLASE-MONOMER
ECOL316407:JW2750-MONOMER
MetaCyc:ENOLASE-MONOMER
BRENDA 4.2.1.11
SABIO-RK P0A6P9
UniPathway UPA00109
EvolutionaryTrace P0A6P9
PRO PR:P0A6P9
Proteomes UP000000318
UP000000625
Genevestigator P0A6P9
GO GO:0009986
GO:0005856
GO:0005829
GO:0005576
GO:0016020
GO:0000015
GO:0042802
GO:0000287
GO:0004634
GO:0006096
Gene3D 3.20.20.120
3.30.390.10
HAMAP MF_00318
InterPro IPR000941
IPR020810
IPR029065
IPR020809
IPR020811
IPR029017
PANTHER PTHR11902
Pfam PF00113
PF03952
PIRSF PIRSF001400
PRINTS PR00148
SUPFAM SSF51604
SSF54826
TIGRFAMs TIGR01060
PROSITE PS00164

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004634

phosphopyruvate hydratase activity

PMID:368027[1]

ECO:0000315

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

enables

GO:0004634

phosphopyruvate hydratase activity

PMID:15236960[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000015

phosphopyruvate hydratase complex

PMID:15236960[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:16858726[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:16858726[3]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6P9

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:15236960[2]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0A6P9

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

PMID:410789[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

PMID:4942326[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

PMID:16516921[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

PMID:17242352[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P05055
UniProtKB:P0A8J8
UniProtKB:P21513

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:18304323[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:17309111[9]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:15911532[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

PMID:11676541[11]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0000015

phosphopyruvate hydratase complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

C

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

F

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000941

P

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.11

F

Seeded From UniProt

complete

enables

GO:0004634

phosphopyruvate hydratase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083263

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083263

C

Seeded From UniProt

complete

part_of

GO:0009986

cell surface

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083263

C

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083263

P

Seeded From UniProt

complete

enables

GO:0000287

magnesium ion binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000083263

F

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206
UniProtKB-SubCell:SL-0090

C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

involved_in

GO:0006096

glycolytic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0324
UniPathway:UPA00109

P

Seeded From UniProt

complete

part_of

GO:0009986

cell surface

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0310

C

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 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. ↑ 2.0 2.1 2.2 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
  3. ↑ 3.0 3.1 3.2 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
  4. ↑ Irani, MH & Maitra, PK (1977) Properties of Escherichia coli mutants deficient in enzymes of glycolysis. J. Bacteriol. 132 398-410 PubMed GONUTS page
  5. ↑ Spring, TG & Wold, F (1971) The purification and characterization of Escherichia coli enolase. J. Biol. Chem. 246 6797-802 PubMed GONUTS page
  6. ↑ Chandran, V & Luisi, BF (2006) Recognition of enolase in the Escherichia coli RNA degradosome. J. Mol. Biol. 358 8-15 PubMed GONUTS page
  7. ↑ Taghbalout, A & Rothfield, L (2007) RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton. Proc. Natl. Acad. Sci. U.S.A. 104 1667-72 PubMed GONUTS page
  8. ↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
  9. ↑ Zhang, N et al. (2007) Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS. Proteomics 7 484-93 PubMed GONUTS page
  10. ↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
  11. ↑ Kühnel, K & Luisi, BF (2001) Crystal structure of the Escherichia coli RNA degradosome component enolase. J. Mol. Biol. 313 583-92 PubMed GONUTS page
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