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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).By similarity

Catalytic activityi

Acetyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-acetyldihydrolipoyl)lysine.

Cofactori

(R)-lipoateBy similarityNote: Binds 1 lipoyl cofactor covalently.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei375Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

Enzyme and pathway databases

BioCyciBAPH198804:G1FZU-214-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
E2
Gene namesi
Name:aceF
Ordered Locus Names:BUsg_200
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera
Proteomesi
  • UP000000416 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622761 – 402Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei35N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

PRIDEiQ8K9T8

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi198804.BUsg200

Structurei

3D structure databases

ProteinModelPortaliQ8K9T8
SMRiQ8K9T8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 69Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST69
Domaini109 – 146Peripheral subunit-binding (PSBD)PROSITE-ProRule annotationAdd BLAST38

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated

Keywords - Domaini

Lipoyl

Phylogenomic databases

eggNOGiENOG4107QSN Bacteria
COG0508 LUCA
KOiK00627
OMAiFTPIFME
OrthoDBiPOG091H05OF

Family and domain databases

Gene3Di3.30.559.10, 1 hit
4.10.320.10, 1 hit
InterProiView protein in InterPro
IPR003016 2-oxoA_DH_lipoyl-BS
IPR001078 2-oxoacid_DH_actylTfrase
IPR006256 AcTrfase_Pyrv_DH_cplx
IPR000089 Biotin_lipoyl
IPR023213 CAT-like_dom_sf
IPR036625 E3-bd_dom_sf
IPR004167 PSBD
IPR011053 Single_hybrid_motif
PANTHERiPTHR43178:SF2 PTHR43178:SF2, 2 hits
PfamiView protein in Pfam
PF00198 2-oxoacid_dh, 1 hit
PF00364 Biotin_lipoyl, 1 hit
PF02817 E3_binding, 1 hit
SUPFAMiSSF47005 SSF47005, 1 hit
SSF51230 SSF51230, 1 hit
PROSITEiView protein in PROSITE
PS50968 BIOTINYL_LIPOYL, 1 hit
PS00189 LIPOYL, 1 hit
PS51826 PSBD, 1 hit

Sequencei

Sequence statusi: Complete.

Q8K9T8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDIGLEEVE VTEILVKIGE EIKLDQGLIT VEGDKASMEI PSPISGIVKD
60 70 80 90 100
ITIKIGEKVK TSSIIMIFKV NNLNSIKNEK DLNYIKTEKK LNENFLEEKK
110 120 130 140 150
DIKKIVLVHA TPVVRRLARH LNVDLKNITP SGPKNRILKE DIELYIRNNT
160 170 180 190 200
SNKSSFNIEK NNTTNFHKDL FNEIPITNIQ QIIGKNLHQN WVNIPHVTQF
210 220 230 240 250
DEVNITLLEE FRHKYNTEKK QKNNMCSKIT ILPFIIKSVA YGLLEFPIFN
260 270 280 290 300
SSLSVNKKTI FLKKYVNVGI AVDVQNALFV PVLKNVDKKN IANLSSELIF
310 320 330 340 350
LSKKAHENKL DASDMKDGCF TISNLGGIGG SWFSPIINSP EVAILGVSKA
360 370 380 390 400
LIKPLWNGKE FIPSLMLPLS LSYDHRVING ADAARFLTFI GKMLSDIRFL

IM
Length:402
Mass (Da):45,421
Last modified:November 8, 2002 - v2
Checksum:i1F784349E26E5643
GO

Sequence cautioni

The sequence AAM67764 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013218 Genomic DNA Translation: AAM67764.1 Different initiation.
RefSeqiWP_044006086.1, NC_004061.1

Genome annotation databases

EnsemblBacteriaiAAM67764; AAM67764; BUsg_200
KEGGibas:BUsg_200

Similar proteinsi

Entry informationi

Entry nameiODP2_BUCAP
AccessioniPrimary (citable) accession number: Q8K9T8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: November 8, 2002
Last modified: May 23, 2018
This is version 103 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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