Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00458
Entry Name
UniProt Accession
Theoretical PI
5.38
Molecular Weight
68862.49
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
Protein Synonyms/Alias
2.3.1.12; Dihydrolipoamide S-acetyltransferase component 1 of pyruvate dehydrogenase complex; Pyruvate dehydrogenase complex component E2 1; PDC-E2 1; PDCE2 1;
Gene Name
LTA3
Gene Synonyms/Alias
At3g52200; F4F15.310;
Created Date
14-NOV-2006
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
120
Canonical
VEVGDVLCEIETDKA
[1]
S-Palmitoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Predicted from GPS-Lipid
Functional Description
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Sequence Annotation
Domain: 86 160 Lipoyl-binding 1.
Domain: 213 287 Lipoyl-binding 2.
Region: 332 363 E3-binding site.
Active site: 610 610
Active site: 614 614
Modified residue: 126 126 N6-lipoyllysine.
Modified residue: 253 253 N6-lipoyllysine.
Protein Length
637 AA.
Protein Sequence
(Canonical)
MVLPLFRRAA IARTSSLLRA RLFAPASEFH SRFSNGLYHL DDKISSSNGV RSASIDLITR  60
MDDSSPKPIL RFGVQNFSST GPISQTVLAM PALSPTMSHG NVVKWMKKEG DKVEVGDVLC  120
EIETDKATVE FESQEEGFLA KILVTEGSKD IPVNEPIAIM VEEEDDIKNV PATIEGGRDG  180
KEETSAHQVM KPDESTQQKS SIQPDASDLP PHVVLEMPAL SPTMNQGNIA KWWKKEGDKI  240
EVGDVIGEIE TDKATLEFES LEEGYLAKIL IPEGSKDVAV GKPIALIVED AESIEAIKSS  300
SAGSSEVDTV KEVPDSVVDK PTERKAGFTK ISPAAKLLIL EHGLEASSIE ASGPYGTLLK  360
SDVVAAIASG KASKSSASTK KKQPSKETPS KSSSTSKPSV TQSDNNYEDF PNSQIRKIIA  420
KRLLESKQKI PHLYLQSDVV LDPLLAFRKE LQENHGVKVS VNDIVIKAVA VALRNVRQAN  480
AFWDAEKGDI VMCDSVDISI AVATEKGLMT PIIKNADQKS ISAISLEVKE LAQKARSGKL  540
APHEFQGGTF SISNLGMYPV DNFCAIINPP QAGILAVGRG NKVVEPVIGL DGIEKPSVVT  600
KMNVTLSADH RIFDGQVGAS FMSELRSNFE DVRRLLL                           637
FASTA
(Canonical)
>LipidDB-3702-00458|Q0WQF7
MVLPLFRRAAIARTSSLLRARLFAPASEFHSRFSNGLYHLDDKISSSNGVRSASIDLITR
MDDSSPKPILRFGVQNFSSTGPISQTVLAMPALSPTMSHGNVVKWMKKEGDKVEVGDVLC
EIETDKATVEFESQEEGFLAKILVTEGSKDIPVNEPIAIMVEEEDDIKNVPATIEGGRDG
KEETSAHQVMKPDESTQQKSSIQPDASDLPPHVVLEMPALSPTMNQGNIAKWWKKEGDKI
EVGDVIGEIETDKATLEFESLEEGYLAKILIPEGSKDVAVGKPIALIVEDAESIEAIKSS
SAGSSEVDTVKEVPDSVVDKPTERKAGFTKISPAAKLLILEHGLEASSIEASGPYGTLLK
SDVVAAIASGKASKSSASTKKKQPSKETPSKSSSTSKPSVTQSDNNYEDFPNSQIRKIIA
KRLLESKQKIPHLYLQSDVVLDPLLAFRKELQENHGVKVSVNDIVIKAVAVALRNVRQAN
AFWDAEKGDIVMCDSVDISIAVATEKGLMTPIIKNADQKSISAISLEVKELAQKARSGKL
APHEFQGGTFSISNLGMYPVDNFCAIINPPQAGILAVGRGNKVVEPVIGLDGIEKPSVVT
KMNVTLSADHRIFDGQVGASFMSELRSNFEDVRRLLL
Gene Ontology
GO:0005739; C:mitochondrion; IEA:UniProtKB-KW
GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB
GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC
GO:0006096; P:glycolytic process; IEA:UniProtKB-KW
Interpro
InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS
InterPro; IPR001078; 2-oxoacid_DH_actylTfrase
InterPro; IPR000089; Biotin_lipoyl
InterPro; IPR023213; CAT-like_dom
InterPro; IPR004167; E3-bd
InterPro; IPR011053; Single_hybrid_motif
Pfam
Pfam; PF00198; 2-oxoacid_dh;
Pfam; PF00364; Biotin_lipoyl;
Pfam; PF02817; E3_binding;
SMART
PROSITE
PROSITE; PS50968; BIOTINYL_LIPOYL;
PROSITE; PS00189; LIPOYL;
PRINTS