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Protein

Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex

Gene

aceF

Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
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 sitei369Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processGlycolysis

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:BU206
OrganismiBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium)
Taxonomic identifieri107806 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera
Proteomesi
  • UP000001806 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001622751 – 396Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complexAdd BLAST396

Amino acid modifications

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

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi107806.BU206

Structurei

3D structure databases

ProteinModelPortaliP57302
SMRiP57302
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 69Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST69
Domaini104 – 141Peripheral 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
HOGENOMiHOG000281562
KOiK00627
OMAiFTPIFME

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.

P57302-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDIGLEEVE IIEILVSINE KIAPEQGLIT VEGDKTSMEI PSPISGIVKH
60 70 80 90 100
IFIKIGEKIK TDALIMRCEV ENIDFHVKKK EEICLDNNVL NKVEKNFKKD
110 120 130 140 150
IFFHATPLIR RLARNLNINL YDVVGTGPKN RILKEDLDLY QSNIKENLIE
160 170 180 190 200
EKNKINFGDS KKSKTKELEL SDIQKNIGNN LHRNWMNIPH VTQFDEVDIT
210 220 230 240 250
ILEKFRQKYN NEKRNQKKTN ENITILVFII KVVAYALEKF PIFNSSLNIN
260 270 280 290 300
NKKIILKKYI NIGFAIDVNN DLFVPVLKDV NKKNIKQLSS ELILLSEKAR
310 320 330 340 350
TRKLNIEDMT GGCFTISNLG GIGGSWFSPI INSPEVAILG ISKSQIKPSW
360 370 380 390
NGKEFIPSLM LPLSLSYDHR VINGAYAARF ITFISRVLSD MHFLIM
Length:396
Mass (Da):45,278
Last modified:December 1, 2000 - v1
Checksum:i1D5B49322AE963BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000003 Genomic DNA Translation: BAB12923.1
RefSeqiNP_240037.2, NC_002528.1

Genome annotation databases

EnsemblBacteriaiBAB12923; BAB12923; BAB12923
GeneIDi1109649
KEGGibuc:BU206
PATRICifig|107806.10.peg.217

Similar proteinsi

Entry informationi

Entry nameiODP2_BUCAI
AccessioniPrimary (citable) accession number: P57302
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: March 28, 2018
This is version 98 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health