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Protein

Acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Escherichia coli (strain B / BL21-DE3)
Status
Unreviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

(R)-lipoateUniRule annotationNote: Binds 3 lipoyl cofactors covalently.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: UniProtKB-KW
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)Imported
Taxonomic identifieri469008 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000009074 Componenti: Chromosome UP000002032 Componenti: Chromosome UP000001509 Componenti: 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.UniRule annotation

Protein-protein interaction databases

STRINGi469008.ECBD_3504.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

LipoylUniRule annotationSAAS annotation

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

        10         20         30         40         50
MAIEIKVPDI GADEVEITEI LVKVGDKVEA EQSLITVEGD KASMEVPSPQ
60 70 80 90 100
AGIVKEIKVS VGDKTQTGAL IMIFDSADGA ADAAPAQAEE KKEAAPAAAP
110 120 130 140 150
AAAAAKDVNV PDIGSDEVEV TEILVKVGDK VEAEQSLITV EGDKASMEVP
160 170 180 190 200
APFAGTVKEI KVNVGDKVST GSLIMVFEVA GEAGAAAPAA KQEAAPAAAP
210 220 230 240 250
APAAGVKEVN VPDIGGDEVE VTEVMVKVGD KVAAEQSLIT VEGDKASMEV
260 270 280 290 300
PAPFAGVVKE LKVNVGDKVK TGSLIMIFEV EGAAPAAAPA KQEAAAPAPA
310 320 330 340 350
AKAEAPAAAP AAKAEGKSEF AENDAYVHAT PLIRRLAREF GVNLAKVKGT
360 370 380 390 400
GRKGRILRED VQAYVKEAIK RAEAAPAATG GGIPGMLPWP KVDFSKFGEI
410 420 430 440 450
EEVELGRIQK ISGANLSRNW VMIPHVTHFD KTDITELEAF RKQQNEEAAK
460 470 480 490 500
RKLDVKITPV VFIMKAVAAA LEQMPRFNSS LSEDGQRLTL KKYINIGVAV
510 520 530 540 550
DTPNGLVVPV FKDVNKKGII ELSRELMTIS KKARDGKLTA GEMQGGCFTI
560 570 580 590 600
SSIGGLGTTH FAPIVNAPEV AILGVSKSAM EPVWNGKEFV PRLMLPISLS
610 620 630
FDHRVIDGAD GARFITIINN TLSDIRRLVM
Length:630
Mass (Da):66,096
Last modified:September 1, 2009 - v1
Checksum:i802A513A1E88F5DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
KEGGiebd:ECBD_3504.
ebe:B21_00113.
ebl:ECD_00114.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi469008.ECBD_3504.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

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]
ProtoNetiSearch...

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]Imported 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]Imported.
  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]Imported.
  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: April 29, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.