aceF:Gene Product(s)

From EcoliWiki
Jump to: navigation, search

{{#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

AceF

Synonyms

pyruvate dehydrogenase, dihydrolipoyltransacetylase component E2[1], B0115[2][1] , ECK0114, JW0111, b0115

Product description

AceF-lipoate[2][3], AceF-S-acetyldihydrolipoate[2][3]

Pyruvate dehydrogenase, dihydrolipoamide acetyltransferase E2; acetate requirement[4]

EC number (for enzymes)
edit table

<protect></protect>

Notes

Function

[back to top]


<protect> 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 Evidence Code with/from Aspect Notes Status
GO:0004742

dihydrolipoyllysine-residue acetyltransferase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006256

F

Seeded from EcoCyc (v14.0)

complete

GO:0004742

dihydrolipoyllysine-residue acetyltransferase activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:2.3.1.12

F

Seeded from EcoCyc (v14.0)

complete

GO:0005515

protein binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR004167

F

Seeded from EcoCyc (v14.0)

complete

GO:0006096

glycolysis

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006256

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:0031405

lipoic acid binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0450

F

Seeded from EcoCyc (v14.0)

complete

GO:0031405

lipoic acid binding

PMID:12651118[5]

IDA: Inferred from Direct Assay

F

Seeded from EcoCyc (v14.0)

complete

GO:0045254

pyruvate dehydrogenase complex

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR006256

C

Seeded from EcoCyc (v14.0)

complete

GO:0005737

cytoplasm

PMID:16858726[6]

IDA: Inferred from Direct Assay

C

complete

GO:0045254

pyruvate dehydrogenase complex

PMID:3903169[7]

IDA: Inferred from Direct Assay

C

complete

GO:0045254

pyruvate dehydrogenase complex

PMID:327021[8]

IGI: Inferred from Genetic Interaction

EcoliWiki:lpd EcoliWiki:acE


C

complete

GO:0004742

dihydrolipoyllysine-residue acetyltransferase activity

PMID:12651118[5]

IDA: Inferred from Direct Assay

F

complete

GO:0031405

lipoic acid binding

PMID:12651118[5]

IDA: Inferred from Direct Assay

F

Lysine at aa 425 is lipoylated

complete

Contributes to

GO:0004738

pyruvate dehydrogenase activity

PMID:3903169[7]

IDA: Inferred from Direct Assay

F

complete

GO:0006090

pyruvate metabolic process

PMID:349114[9]

IMP: Inferred from Mutant Phenotype

P

complete

GO:0006086

acetyl-CoA biosynthetic process from pyruvate

PMID:349114[9]

IMP: Inferred from Mutant Phenotype

P

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

dcm

PMID:15690043[10]

Experiment(s):EBI-889144, EBI-894157

Protein

rpmF

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

sdhA

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

lpdA

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

rplV

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

acnB

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

aceE

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

rplY

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

rpmH

PMID:16606699[11]

Experiment(s):EBI-1135600

Protein

mukB

PMID:16606699[11]

Experiment(s):EBI-1135600
edit table

</protect>

Notes

Localization

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

Compartment Description Evidence Reference/Source Notes

Cytoplasm

PMID:9298646[12]

EchoLocation:aceF


edit table

<protect></protect>

Notes

Structure and Physical Properties

[back to top]


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

Name
Sequence

at EcoCyc 

MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ AGIVKEIKVS
VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP AAAAAKDVNV PDIGSDEVEV
TEILVKVGDK VEAEQSLITV EGDKASMEVP APFAGTVKEI KVNVGDKVST GSLIMVFEVA
GEAGAAAPAA KQEAAPAAAP APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT
VEGDKASMEV PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT GRKGRILRED
VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI EEVELGRIQK ISGANLSRNW
VMIPHVTHFD KTDITELEAF RKQQNEEAAK RKLDVKITPV VFIMKAVAAA LEQMPRFNSS
LSEDGQRLTL KKYINIGVAV DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA
GEMQGGCFTI SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
FDHRVIDGAD GARFITIINN TLSDIRRLVM
Length

630

Mol. Wt

66.095 kDa

pI

5.0 (calculated)

Extinction coefficient

20,970 - 21,095 (calc based on 3 Y, 3 W, and 1 C residues)

edit table


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:P06959

Domain

397..630

PF00198 2-oxoacid dehydrogenases acyltransferase (catalytic domain)

PMID:19920124[13]

Domain

3..74

PF00364 Biotin-requiring enzyme

PMID:19920124[13]

Domain

106..177

PF00364 Biotin-requiring enzyme

PMID:19920124[13]

Domain

207..278

PF00364 Biotin-requiring enzyme

PMID:19920124[13]

Domain

325..363

PF02817 e3 binding domain

PMID:19920124[13]

edit table

<motif_map/>

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

Structures

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

Models

View models at:

edit table
</protect>

Structure figures

<protect>

</protect>

Notes

Gene Product Resources

[back to top]


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

Resource type Source Notes/Reference
edit table

<protect></protect>

Notes

Accessions in Other Databases

[back to top]


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

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16128108

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:944794

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0000400

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P06959

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG10025

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG10025

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:944794

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120000022

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB0024

Escherichia coli str. K-12 substr. MG1655

edit table

<protect></protect>

Notes

Links

[back to top]




References

[back to top]


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

  1. ↑ 1.0 1.1 1.2 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 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. ↑ 5.0 5.1 5.2 Wei, W et al. (2003) Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase. Protein Expr. Purif. 28 140-50 PubMed
  6. ↑ 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
  7. ↑ 7.0 7.1 Guest, JR et al. (1985) Genetic reconstruction and functional analysis of the repeating lipoyl domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol. 185 743-54 PubMed
  8. ↑ Langley, D & Guest, JR (1977) Biochemical genetics of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: isolation and biochemical properties of deletion mutants. J. Gen. Microbiol. 99 263-76 PubMed
  9. ↑ 9.0 9.1 Langley, D & Guest, JR (1978) Biochemical genetics of the alpha-keto acid dehydrogenase complexes of Escherichia coli K12: genetic characterization and regulatory properties of deletion mutants. J. Gen. Microbiol. 106 103-17 PubMed
  10. ↑ Butland, G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433 531-7 PubMed
  11. ↑ 11.0 11.1 11.2 11.3 11.4 11.5 11.6 11.7 11.8 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  12. ↑ 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
  13. ↑ 13.0 13.1 13.2 13.3 13.4 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

[back to top]


Retrieved from "https://ecoliwiki.org/colipedia/index.php?title=aceF:Gene_Product(s)&oldid=1492160"