eno:Gene Product(s): Difference between revisions

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[[Category:RefGenome_Annotated_Gene]]
[[Category:RefGenome_Annotated_Gene]]
[[Category:Pfam:PF00113_!_Enolase, C-terminal TIM barrel domain]]
[[Category:Pfam:PF00113_!_Enolase, C-terminal TIM barrel domain]]
[[Category:Pfam:PF03952_!_Enolase, N-terminal domain]]

Revision as of 21:28, 24 June 2010

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Quickview   Gene   Gene Product(s)   Expression   Evolution   On One Page    
Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

Eno

Synonyms

enolase[1], B2779[2][1], Eno[2][1]

Product description

Eno[2][3];

Component of enolase[2][3]; degradosome[3]

Enolase; phosphoprotein; component of RNA degradosome[4]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0004634

phosphopyruvate hydratase activity

PMID:4942326[5]

IDA: Inferred from Direct Assay

F

purification, assay according to ref 5, which is not in Pubmed

complete

GO:0000015

phosphopyruvate hydratase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000941

C

Seeded from EcoCyc (v14.0)

complete

GO:0000015

phosphopyruvate hydratase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020809

C

Seeded from EcoCyc (v14.0)

complete

GO:0000015

phosphopyruvate hydratase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020810

C

Seeded from EcoCyc (v14.0)

complete

GO:0000015

phosphopyruvate hydratase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020811

C

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00318

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000941

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020809

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020810

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020811

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

PMID:16516921[6]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0004634

phosphopyruvate hydratase activity

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00318

F

Seeded from EcoCyc (v14.0)

complete

GO:0004634

phosphopyruvate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000941

F

Seeded from EcoCyc (v14.0)

complete

GO:0004634

phosphopyruvate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020809

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:16516921[6]

IPI: Inferred from Physical Interaction

EcoliWiki:eno


F

Enolase is homodimeric (Figure 1).

complete

GO:0004634

phosphopyruvate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020810

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

PMID:16516921[6]

IPI: Inferred from Physical Interaction

EcoliWiki:rne


F

complete

GO:0004634

phosphopyruvate hydratase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020811

F

Seeded from EcoCyc (v14.0)

complete

GO:0000287

magnesium ion binding

PMID:16516921[6]

IDA: Inferred from Direct Assay

F

Each monomer binds and coordinates 1 MG2+ cation (Figure 3).

complete

GO:0004634

phosphopyruvate hydratase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:4.2.1.11

F

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

PMID:410789[7]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0005515

protein binding

PMID:16516921[6]

IPI: Inferred from Physical Interaction

F

Seeded from EcoCyc (v14.0)

Missing: with/from

GO:0004634

phosphopyruvate hydratase activity

PMID:12054465[8]

IMP: Inferred from Mutant Phenotype

F

complete

GO:0005515

protein binding

PMID:16516921[6]

IPI: Inferred from Physical Interaction

EcoliWiki:eno

F

Seeded from EcoCyc (v14.0)

complete

GO:0005576

extracellular region

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0964

C

Seeded from EcoCyc (v14.0)

complete

GO:0005576

extracellular region

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0243

C

Seeded from EcoCyc (v14.0)

complete

GO:0005829

cytosol

PMID:16858726[9]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

GO:0005856

cytoskeleton

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0206

C

Seeded from EcoCyc (v14.0)

complete

GO:0005856

cytoskeleton

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0090

C

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00318

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000941

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020809

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020810

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR020811

P

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0324

P

Seeded from EcoCyc (v14.0)

complete

GO:0009986

cell surface

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_00318

C

Seeded from EcoCyc (v14.0)

complete

GO:0009986

cell surface

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-0310

C

Seeded from EcoCyc (v14.0)

complete

GO:0016020

membrane

PMID:16858726[9]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc (v14.0)

complete

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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of enolase

could be indirect

Protein

aroF

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

rplI

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

yfeX

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

rplW

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

nadE

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

rdgC

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

ybdN

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

yqjK

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

racR

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

nanE

PMID:16606699[10]

Experiment(s):EBI-1143906

Protein

dnaK

PMID:15690043[11]

Experiment(s):EBI-880413, EBI-885840

Protein

fabZ

PMID:15690043[11]

Experiment(s):EBI-880413

Protein

gltX

PMID:15690043[11]

Experiment(s):EBI-880413

Protein

pnp

PMID:15690043[11]

Experiment(s):EBI-880413, EBI-883913, EBI-891089, EBI-885840

Protein

yniC

PMID:15690043[11]

Experiment(s):EBI-880413

Protein

pinR

PMID:15690043[11]

Experiment(s):EBI-885840

Protein

rpsE

PMID:15690043[11]

Experiment(s):EBI-885840

Protein

Subunits of degradosome

could be indirect


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Notes

IMP for enolase activity probably in [12] (based on abstract. need to get paper and read).

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Source Notes

cytoplasm

From EcoCyc[3]

Cytoplasm

PMID:9298646[13], PMID:8610017[14], PMID:9600841[15], PMID:9740056[16], PMID:9732527[17], PMID:12035760[18]

EchoLocation:eno


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Notes

Structure and Physical Properties

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Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Sequence

at EcoCyc 

MSKIVKIIGR EIIDSRGNPT VEAEVHLEGG FVGMAAAPSG ASTGSREALE LRDGDKSRFL
GKGVTKAVAA VNGPIAQALI GKDAKDQAGI DKIMIDLDGT ENKSKFGANA ILAVSLANAK
AAAAAKGMPL YEHIAELNGT PGKYSMPVPM MNIINGGEHA DNNVDIQEFM IQPVGAKTVK
EAIRMGSEVF HHLAKVLKAK GMNTAVGDEG GYAPNLGSNA EALAVIAEAV KAAGYELGKD
ITLAMDCAAS EFYKDGKYVL AGEGNKAFTS EEFTHFLEEL TKQYPIVSIE DGLDESDWDG
FAYQTKVLGD KIQLVGDDLF VTNTKILKEG IEKGIANSIL IKFNQIGSLT ETLAAIKMAK
DAGYTAVISH RSGETEDATI ADLAVGTAAG QIKTGSMSRS DRVAKYNQLI RIEEALGEKA
PYNGRKEIKG QA
Length

432

Mol. Wt

45.656 kDa

pI

5.3 (calculated)

Extinction coefficient

21,890 - 22,015 (calc based on 11 Y, 1 W, and 1 C residues)

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Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Initiator Methionine

1

Removed

UniProt:P0A6P9

Modification Site

375

phosphorylation site at T375

probability less than 75%

PMID:17938405[19]

Modification Site

379

phosphorylation site at T379

probability less than 75%

PMID:17938405[19]

Modification Site

372

phosphorylation site at S372

probability less than 75%

PMID:17938405[19]

Domain

143..431

PF00113 Enolase, C-terminal TIM barrel domain

Pfam:P0A6P9

Domain

3..134

PF03952 Enolase, N-terminal domain

Pfam:P0A6P9


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<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=eno taxon=562,83333 </beststructure>

Models

View models at:

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Structure figures

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:ENOLASE-MONOMER

UniProt (EcoliWiki Page)

UniProt:P0A6P9

PFAM (EcoliWiki Page)

PFAM:PF03952

RefSeq (EcoliWiki Page)

RefSeq:NP_417259


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Notes

Links

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References

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

  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 3.3 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. ↑ Spring, TG & Wold, F (1971) The purification and characterization of Escherichia coli enolase. J. Biol. Chem. 246 6797-802 PubMed
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 Chandran, V & Luisi, BF (2006) Recognition of enolase in the Escherichia coli RNA degradosome. J. Mol. Biol. 358 8-15 PubMed
  7. ↑ Irani, MH & Maitra, PK (1977) Properties of Escherichia coli mutants deficient in enzymes of glycolysis. J. Bacteriol. 132 398-410 PubMed
  8. ↑ 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
  9. ↑ 9.0 9.1 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
  10. ↑ 10.00 10.01 10.02 10.03 10.04 10.05 10.06 10.07 10.08 10.09 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 11.4 11.5 11.6 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  12. ↑ Irani, MH & Maitra, PK (1976) Glyceraldehyde 3-p dehydrogenase, glycerate 3-P kinase and enolase mutants of Escherichia coli: genetic studies. Mol. Gen. Genet. 145 65-71 PubMed
  13. ↑ Link, AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 1259-313 PubMed
  14. ↑ Py, B et al. (1996) A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381 169-72 PubMed
  15. ↑ Wilkins, MR et al. (1998) Protein identification with N and C-terminal sequence tags in proteome projects. J. Mol. Biol. 278 599-608 PubMed
  16. ↑ Tonella, L et al. (1998) '98 Escherichia coli SWISS-2DPAGE database update. Electrophoresis 19 1960-71 PubMed
  17. ↑ Rompf, A et al. (1998) Changes in protein synthesis as a consequence of heme depletion in Escherichia coli. Curr. Microbiol. 37 226-30 PubMed
  18. ↑ Carpousis, AJ (2002) The Escherichia coli RNA degradosome: structure, function and relationship in other ribonucleolytic multienzyme complexes. Biochem. Soc. Trans. 30 150-5 PubMed
  19. ↑ 19.0 19.1 19.2 Macek, B et al. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell Proteomics 7 299-307 PubMed

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