eno:Gene Product(s): Difference between revisions

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|-
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!align=left {{table heading style}} |Standard name
!align=left |Standard name
||
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Eno  
Eno  
|-
|-
!align=left {{table heading style}} |Synonyms
!align=left |Synonyms
||
||
enolase<ref name='LIB:Riley_2006'/>, B2779<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Eno<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
enolase<ref name='LIB:Riley_2006'/>, B2779<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>, Eno<ref name='LIB:EcoCyc10.6'/><ref name='LIB:Riley_2006'/>  
|-
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!align=left {{table heading style}} |Product description
!align=left |Product description
||
||
Eno<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  
Eno<ref name='LIB:EcoCyc10.6'/><ref name='LIB:EcoCyc11.1'/>;  
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Enolase; phosphoprotein; component of RNA degradosome<ref name='LIB:EcoGene'/>
Enolase; phosphoprotein; component of RNA degradosome<ref name='LIB:EcoGene'/>
|-
|-
!align=left {{table heading style}} |EC number (for enzymes)
!align=left |EC number (for enzymes)
||
||
* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11]<ref name='LIB:Riley_2006'/>
* [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11]<ref name='LIB:Riley_2006'/>


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!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
!|Qualifier!!GO ID!!GO term name!!Reference(s)!!Evidence Code!!with/from!!Aspect!!Notes!!Status
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complete  
complete  


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!|Partner Type!!Partner!!Notes!!References!!Evidence
!|Partner Type!!Partner!!Notes!!References!!Evidence
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!|Compartment!!Description!!Evidence!!Source!!Notes
!|Compartment!!Description!!Evidence!!Source!!Notes
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PMID:9298646, PMID:8610017, PMID:9600841, PMID:9740056, PMID:9732527, PMID:12035760
PMID:9298646, PMID:8610017, PMID:9600841, PMID:9740056, PMID:9732527, PMID:12035760
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[http://www.york.ac.uk/res/thomas/Echolocation.cfm?EB_SubLocID=EB0254 EchoLocation:eno]
[http://www.york.ac.uk/res/thomas/Echolocation.cfm?EB_SubLocID=EB0254 EchoLocation:eno]
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|-
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!align=left {{table heading style}} |Sequence
!align=left |Sequence
||
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[http://biocyc.org/ECOLI/sequence-aa?object=ENOLASE-MONOMER at EcoCyc]  
[http://biocyc.org/ECOLI/sequence-aa?object=ENOLASE-MONOMER at EcoCyc]  
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PYNGRKEIKG QA</pre>  
PYNGRKEIKG QA</pre>  
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!align=left {{table heading style}} |Length
!align=left |Length
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432
432
|-
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!align=left {{table heading style}} |Mol. Wt
!align=left |Mol. Wt
||
||
45.656 kDa
45.656 kDa
|-
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!align=left {{table heading style}} |pI
!align=left |pI
||
||
5.3 (calculated)
5.3 (calculated)
|-
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!align=left {{table heading style}} |Extinction coefficient
!align=left |Extinction coefficient
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21,890 - 22,015 (calc based on 11 Y, 1 W, and 1 C residues)
21,890 - 22,015 (calc based on 11 Y, 1 W, and 1 C residues)


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[http://www.uniprot.org/uniprot/P0A6P9#section_features UniProt:P0A6P9]  
[http://www.uniprot.org/uniprot/P0A6P9#section_features UniProt:P0A6P9]  


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<beststructure>
<beststructure>
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</beststructure>
</beststructure>
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!align=left {{table heading style}} |Models
!align=left |Models
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View models at:
View models at:
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* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)
* [http://spock.genes.nig.ac.jp/~genome/search.html Genomes TO Protein] (GTOP)


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Revision as of 00:54, 9 January 2010

{{#css:Suppresslinks.css}}<css>h1 .editsection { display:none;} h2 .editsection { display:none;}</css>

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)
edit table


Notes

Function

[back to top]


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:0046872

metal ion binding

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc [5]

complete

GO:0016829

lyase activity

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0456

F

Seeded from EcoCyc [5]

complete

GO:0006096

glycolysis

GO_REF:0000002
GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR000941
SP_KW:KW-0324
HAMAP:MF_00318

P

Seeded from EcoCyc 12.5 [6]

complete

GO:0005856

cytoskeleton

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0206

C

Seeded from EcoCyc [5]

complete

GO:0005737

cytoplasm

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0963

C

Seeded from EcoCyc 12.5 [6]

complete

GO:0004634

phosphopyruvate hydratase activity

GO_REF:0000002
GO_REF:0000003
GO_REF:0000020

IEA: Inferred from Electronic Annotation

InterPro:IPR000941
EC:4.2.1.11
HAMAP:MF_00318

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0000287

magnesium ion binding

GO_REF:0000004
GO_REF:0000020

IEA: Inferred from Electronic Annotation

SP_KW:KW-0460
HAMAP:MF_00318

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0000015

phosphopyruvate hydratase complex

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000941

C

Seeded from EcoCyc [5]

complete

GO:0004634

phosphopyruvate hydratase activity

PMID:4942326[7]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc 12.5 [6]

complete

GO:0005515

protein binding

PMID:15236960[8]

IPI: Inferred from Physical Interaction

UniProtKB:P21513

F

Seeded from EcoCyc [5]

complete

GO:0005624

membrane fraction

PMID:16858726[9]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [5]

complete

GO:0042802

identical protein binding

PMID:15236960[8]

IPI: Inferred from Physical Interaction

UniProtKB:P0A6P9

F

Seeded from EcoCyc [5]

complete

GO:0005576

extracellular region

GO_REF:0000004
GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_KW:KW-0964
SP_SL:SL-0243

C

Seeded from EcoCyc [5]

complete

NOT

GO:0005739

mitochondrion

PMID:16858726[9]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [5]

complete

GO:0005829

cytosol

PMID:16858726[9]

IDA: Inferred from Direct Assay

C

Seeded from EcoCyc [5]

complete

GO:0009986

cell surface

GO_REF:0000020
GO_REF:0000023

IEA: Inferred from Electronic Annotation

HAMAP:MF_00318
SP_SL:SL-0310

C

Seeded from EcoCyc [5]

complete

GO:0009061

anaerobic respiration

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0006094

gluconeogenesis

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0004634

phosphopyruvate hydratase activity

PMID:4942326[7]

IDA: Inferred from Direct Assay

F

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

complete

GO:0005515

protein binding

PMID:16516921[10]

IPI: Inferred from Physical Interaction

EcoliWiki:eno


F

Enolase is homodimeric (Figure 1).

complete

GO:0005515

protein binding

PMID:16516921[10]

IPI: Inferred from Physical Interaction

EcoliWiki:rne


F

complete

GO:0000287

magnesium ion binding

PMID:16516921[10]

IDA: Inferred from Direct Assay

F

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

complete

GO:0006096

glycolysis

PMID:410789[11]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0004634

phosphopyruvate hydratase activity

PMID:12054465[12]

IMP: Inferred from Mutant Phenotype

F

complete

edit table

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[13]

Experiment(s):EBI-1143906

Protein

rplI

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

yfeX

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

rplW

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

nadE

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

rdgC

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

ybdN

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

yqjK

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

racR

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

nanE

PMID:16606699[13]

Experiment(s):EBI-1143906

Protein

dnaK

PMID:15690043[14]

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

Protein

fabZ

PMID:15690043[14]

Experiment(s):EBI-880413

Protein

gltX

PMID:15690043[14]

Experiment(s):EBI-880413

Protein

pnp

PMID:15690043[14]

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

Protein

yniC

PMID:15690043[14]

Experiment(s):EBI-880413

Protein

pinR

PMID:15690043[14]

Experiment(s):EBI-885840

Protein

rpsE

PMID:15690043[14]

Experiment(s):EBI-885840

Protein

Subunits of degradosome

could be indirect


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Notes

IMP for enolase activity probably in [15] (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[16], PMID:8610017[17], PMID:9600841[18], PMID:9740056[19], PMID:9732527[20], PMID:12035760[21]

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

Initiator Methionine

1

Removed

UniProt:P0A6P9

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<motif_map/>

Structure
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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 3.4 3.5 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. ↑ 5.00 5.01 5.02 5.03 5.04 5.05 5.06 5.07 5.08 5.09 5.10 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
  6. ↑ 6.0 6.1 6.2 6.3 6.4 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  7. ↑ 7.0 7.1 Spring, TG & Wold, F (1971) The purification and characterization of Escherichia coli enolase. J. Biol. Chem. 246 6797-802 PubMed
  8. ↑ 8.0 8.1 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
  9. ↑ 9.0 9.1 9.2 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
  10. ↑ 10.0 10.1 10.2 Chandran, V & Luisi, BF (2006) Recognition of enolase in the Escherichia coli RNA degradosome. J. Mol. Biol. 358 8-15 PubMed
  11. ↑ Irani, MH & Maitra, PK (1977) Properties of Escherichia coli mutants deficient in enzymes of glycolysis. J. Bacteriol. 132 398-410 PubMed
  12. ↑ 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
  13. ↑ 13.00 13.01 13.02 13.03 13.04 13.05 13.06 13.07 13.08 13.09 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  14. ↑ 14.0 14.1 14.2 14.3 14.4 14.5 14.6 Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  15. ↑ 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
  16. ↑ 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
  17. ↑ Py, B et al. (1996) A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381 169-72 PubMed
  18. ↑ Wilkins, MR et al. (1998) Protein identification with N and C-terminal sequence tags in proteome projects. J. Mol. Biol. 278 599-608 PubMed
  19. ↑ Tonella, L et al. (1998) '98 Escherichia coli SWISS-2DPAGE database update. Electrophoresis 19 1960-71 PubMed
  20. ↑ Rompf, A et al. (1998) Changes in protein synthesis as a consequence of heme depletion in Escherichia coli. Curr. Microbiol. 37 226-30 PubMed
  21. ↑ Carpousis, AJ (2002) The Escherichia coli RNA degradosome: structure, function and relationship in other ribonucleolytic multienzyme complexes. Biochem. Soc. Trans. 30 150-5 PubMed

Categories

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