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aceF:Gene Product(s)
From EcoliWiki
| 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] |
| 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 |
Notes
Function
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:0004742 |
dihydrolipoyllysine-residue acetyltransferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0045254 |
pyruvate dehydrogenase complex |
IEA: Inferred from Electronic Annotation |
C |
Seeded from EcoCyc [5] |
complete | |||
| GO:0031405 |
lipoic acid binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0005515 |
protein binding |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0006096 |
glycolysis |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [5] |
complete | |||
| GO:0008152 |
metabolic process |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc [5] |
complete | |||
| GO:0008415 |
acyltransferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0016740 |
transferase activity |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc [5] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005515 |
protein binding |
IPI: Inferred from Physical Interaction |
F |
Seeded from EcoCyc 12.5 [6] |
complete | |||
| GO:0005737 |
cytoplasm |
IDA: Inferred from Direct Assay |
C |
Seeded from EcoCyc [5] |
complete | |||
| GO:0016052 |
carbohydrate catabolic process |
P |
Seeded from EcoCyc 11.1[3]. |
required fields missing | ||||
| GO:0006086 |
acetyl-CoA biosynthetic process from pyruvate |
P |
Seeded from EcoCyc 11.1[3]. |
required fields missing | ||||
| GO:0009436 |
glyoxylate catabolic process |
P |
Seeded from EcoCyc 11.1[3]. |
required fields missing | ||||
| GO:0009061 |
anaerobic respiration |
P |
Seeded from EcoCyc 11.1[3]. |
required fields missing | ||||
| GO:0045254 |
pyruvate dehydrogenase complex |
IDA: Inferred from Direct Assay |
C |
complete | ||||
| GO:0045254 |
pyruvate dehydrogenase complex |
IGI: Inferred from Genetic Interaction |
C |
EcoliWiki:aceE|EcoliWiki:lpd |
Missing: with/from | |||
| GO:0004742 |
dihydrolipoyllysine-residue acetyltransferase activity |
IDA: Inferred from Direct Assay |
F |
complete | ||||
| GO:0031405 |
lipoic acid binding |
IDA: Inferred from Direct Assay |
F |
Lysine at aa 425 is lipoylated |
complete | |||
|
Contributes to | GO:0004738 |
pyruvate dehydrogenase activity |
IDA: Inferred from Direct Assay |
F |
complete | |||
| GO:0006090 |
pyruvate metabolic process |
IMP: Inferred from Mutant Phenotype |
P |
complete | ||||
| GO:0006086 |
acetyl-CoA biosynthetic process from pyruvate |
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 |
Experiment(s):EBI-889144, EBI-894157 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
|
Protein |
Experiment(s):EBI-1135600 | |||
| edit table |
Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
| Compartment | Description | Evidence | Source | Notes |
|---|---|---|---|---|
|
Cytoplasm |
| |||
| edit table |
Notes
Structure and Physical Properties
Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
| Sequence |
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 |
|
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures
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| Resource type | Source | Notes/Reference |
|---|---|---|
| edit table |
Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
| Database | Accession | Notes |
|---|---|---|
|
| ||
| edit table |
Notes
Links
| Name | URL | Comments |
|---|---|---|
| edit table |
References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 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
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
- ↑ 6.0 6.1 6.2 6.3 6.4 6.5 6.6 6.7 6.8 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 7.0 7.1 7.2 7.3 7.4 7.5 7.6 7.7 7.8 Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
- ↑ 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 EcoliWiki page
- ↑ 9.0 9.1 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 EcoliWiki page
- ↑ 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 EcoliWiki page
- ↑ 11.0 11.1 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 EcoliWiki page
- ↑ 12.0 12.1 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 EcoliWiki page
- ↑ 13.0 13.1 13.2 13.3 13.4 13.5 13.6 13.7 13.8 Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
- ↑ 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 EcoliWiki page
