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C6EAU2

- C6EAU2_ECOBD

UniProt

C6EAU2 - C6EAU2_ECOBD

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Protein
Acetyltransferase component of pyruvate dehydrogenase complex
Gene
aceF, B21_00113, ECBD_3504, ECD_00114
Organism
Escherichia coli (strain B / BL21-DE3)
Status
Unreviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity.UniRule annotation

Catalytic activityi

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.UniRule annotation

Cofactori

Binds 1 lipoyl cofactor covalently By similarity.UniRule annotation
Binds 2 lipoyl cofactors covalently By similarity.UniRule annotation
Binds 3 lipoyl cofactors covalently By similarity.UniRule annotation

GO - Molecular functioni

  1. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC
  2. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. glycolytic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

AcyltransferaseUniRule annotationImported, OxidoreductaseImported, Transferase

Keywords - Biological processi

GlycolysisUniRule annotation

Keywords - Ligandi

PyruvateImported

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyltransferase component of pyruvate dehydrogenase complexUniRule annotation (EC:2.3.1.12UniRule annotation)
Gene namesi
Name:aceFImported
Ordered Locus Names:B21_00113Imported, ECBD_3504Imported, ECD_00114Imported
OrganismiEscherichia coli (strain B / BL21-DE3)
Taxonomic identifieri469008 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001509: Chromosome, UP000002032: Chromosome, UP000009074: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Interactioni

Subunit structurei

Forms a 24-polypeptide structural core with octahedral symmetry By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi469008.ECBD_3504.

Structurei

3D structure databases

ProteinModelPortaliC6EAU2.
SMRiC6EAU2. Positions 1-183, 206-284, 328-365, 388-630.

Family & Domainsi

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.UniRule annotation
Contains 3 lipoyl-binding domains.UniRule annotation

Keywords - Domaini

LipoylUniRule annotationSAAS annotations

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281562.
KOiK00627.
OMAiTEIMVAV.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsiTIGR01348. PDHac_trf_long. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C6EAU2-1 [UniParc]FASTAAdd to Basket

« Hide

MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ    50
AGIVKEIKVS VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP 100
AAAAAKDVNV PDIGSDEVEV TEILVKVGDK VEAEQSLITV EGDKASMEVP 150
APFAGTVKEI KVNVGDKVST GSLIMVFEVA GEAGAAAPAA KQEAAPAAAP 200
APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT VEGDKASMEV 250
PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA 300
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT 350
GRKGRILRED VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI 400
EEVELGRIQK ISGANLSRNW VMIPHVTHFD KTDITELEAF RKQQNEEAAK 450
RKLDVKITPV VFIMKAVAAA LEQMPRFNSS LSEDGQRLTL KKYINIGVAV 500
DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA GEMQGGCFTI 550
SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS 600
FDHRVIDGAD GARFITIINN TLSDIRRLVM 630
Length:630
Mass (Da):66,096
Last modified:September 1, 2009 - v1
Checksum:i802A513A1E88F5DA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001665 Genomic DNA. Translation: ACT30503.1.
CP001509 Genomic DNA. Translation: ACT42015.1.
AM946981 Genomic DNA. Translation: CAQ30630.1.
RefSeqiYP_002997980.1. NC_012892.2.
YP_003037688.1. NC_012947.1.
YP_003052786.1. NC_012971.2.

Genome annotation databases

EnsemblBacteriaiACT30503; ACT30503; ECBD_3504.
ACT42015; ACT42015; ECD_00114.
CAQ30630; CAQ30630; B21_00113.
GeneIDi8115316.
8157821.
8181520.
KEGGiebd:ECBD_3504.
ebe:B21_00113.
ebl:ECD_00114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001665 Genomic DNA. Translation: ACT30503.1 .
CP001509 Genomic DNA. Translation: ACT42015.1 .
AM946981 Genomic DNA. Translation: CAQ30630.1 .
RefSeqi YP_002997980.1. NC_012892.2.
YP_003037688.1. NC_012947.1.
YP_003052786.1. NC_012971.2.

3D structure databases

ProteinModelPortali C6EAU2.
SMRi C6EAU2. Positions 1-183, 206-284, 328-365, 388-630.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 469008.ECBD_3504.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACT30503 ; ACT30503 ; ECBD_3504 .
ACT42015 ; ACT42015 ; ECD_00114 .
CAQ30630 ; CAQ30630 ; B21_00113 .
GeneIDi 8115316.
8157821.
8181520.
KEGGi ebd:ECBD_3504.
ebe:B21_00113.
ebl:ECD_00114.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281562.
KOi K00627.
OMAi TEIMVAV.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 3 hits.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 3 hits.
TIGRFAMsi TIGR01348. PDHac_trf_long. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 3 hits.
PS00189. LIPOYL. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and gene expression analysis of Escherichia coli BL21(DE3)."
    Krempl P.M., Mairhofer J., Eisenkolb M., Specht T., Leparc G.G., Kreil D.P., Bayer K., Striedner G.
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21Imported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Korea] and BL21Imported.
  3. "Sequencing and gene expression analysis of Escherichia coli BL21."
    Leparc G., Striedner G., Bayer K., Kreil D., Krempl P.M.
    Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [Austria].
  4. "Complete sequence of Escherichia coli 'BL21-Gold(DE3)pLysS AG'."
    US DOE Joint Genome Institute
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21-GoldImported.
  5. "Complete sequence of Escherichia coli BL21(DE3)."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Sorek R., Rubin E.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B / BL21-DE3 [JGI].
  6. Jeong H., Shim J.-H., Studier F.W., Oh T.K., Kim J.F.
    Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BL21.

Entry informationi

Entry nameiC6EAU2_ECOBD
AccessioniPrimary (citable) accession number: C6EAU2
Secondary accession number(s): C5W122
Entry historyi
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: September 3, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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