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Protein

Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial

Gene

At1g54220

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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).1 Publication

Catalytic activityi

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

Cofactori

(R)-lipoateNote: Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei512Sequence analysis1
Active sitei516Sequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciARA:AT1G54220-MONOMER.
ReactomeiR-ATH-70268. Pyruvate metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide S-acetyltransferase component 3 of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2 3
Short name:
PDC-E2 3
Short name:
PDCE2 3
Gene namesi
Ordered Locus Names:At1g54220
ORF Names:F20D21.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G54220.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000260027? – 539Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei152N6-lipoyllysinePROSITE-ProRule annotationBy similarity1

Proteomic databases

PaxDbiQ5M729.
PRIDEiQ5M729.

Expressioni

Gene expression databases

GenevisibleiQ5M729. AT.

Interactioni

Protein-protein interaction databases

BioGridi27088. 1 interactor.
STRINGi3702.AT1G54220.1.

Structurei

3D structure databases

ProteinModelPortaliQ5M729.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini111 – 187Lipoyl-bindingPROSITE-ProRule annotationAdd BLAST77

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni250 – 281E3-binding siteBy similarityAdd BLAST32

Sequence similaritiesi

Belongs to the 2-oxoacid dehydrogenase family.Curated
Contains 1 lipoyl-binding domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiKOG0557. Eukaryota.
COG0508. LUCA.
HOGENOMiHOG000281566.
InParanoidiQ5M729.
KOiK00627.
OMAiVHIGMAT.
OrthoDBiEOG093607WT.
PhylomeDBiQ5M729.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5M729-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAYASRIINH SKKLKDVSTL LRRENAATIR YYSNTNRAPL NREDTFNSRL
60 70 80 90 100
GYPPLERISI CSTSTLPVSI IFSTTRSNLS SAMGRPIFGK EFSCLMQSAR
110 120 130 140 150
GFSSGSDLPP HQEIGMPSLS PTMTEGNIAR WLKKEGDKVA PGEVLCEVET
160 170 180 190 200
DKATVEMECM EEGYLAKIVK AEGSKEIQVG EVIAITVEDE EDIGKFKDYT
210 220 230 240 250
PSSTADAAPT KAEPTPAPPK EEKVKQPSSP PEPKASKPST PPTGDRVFAS
260 270 280 290 300
PLARKLAEDN NVPLSDIEGT GPEGRIVKAD IDEYLASSGK GATAKPSKST
310 320 330 340 350
DSKAPALDYV DIPHSQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKLMALR
360 370 380 390 400
SQLNSFKEAS GGKRISVNDL VVKAAALALR KVPQCNSSWT DDYIRQFKNV
410 420 430 440 450
NINVAVQTEN GLYVPVVKDA DRKGLSTIGE EVRLLAQKAK ENSLKPEDYE
460 470 480 490 500
GGTFTVSNLG GPFGIKQFCA VVNPPQAAIL AVGSAEKRVV PGNGPDQFNF
510 520 530
ASYMPVTLSC DHRVVDGAIG AEWLKAFKGY IENPKSMLL
Length:539
Mass (Da):58,467
Last modified:February 1, 2005 - v1
Checksum:i0C4E141079A2698F
GO

Sequence cautioni

The sequence AAD25602 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45T → I in AAK53067 (Ref. 1) Curated1
Sequence conflicti267I → T in AAK53067 (Ref. 1) Curated1
Sequence conflicti442N → S in AAM97076 (PubMed:14593172).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033001 mRNA. Translation: AAK53067.1.
AC005287 Genomic DNA. Translation: AAD25602.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33067.1.
CP002684 Genomic DNA. Translation: AEE33068.1.
AY136410 mRNA. Translation: AAM97076.1.
BT020419 mRNA. Translation: AAV97810.1.
PIRiE96583.
RefSeqiNP_001031186.1. NM_001036109.1.
NP_564654.1. NM_104300.4.
UniGeneiAt.19093.
At.21338.

Genome annotation databases

EnsemblPlantsiAT1G54220.1; AT1G54220.1; AT1G54220.
AT1G54220.2; AT1G54220.2; AT1G54220.
GeneIDi841863.
GrameneiAT1G54220.1; AT1G54220.1; AT1G54220.
AT1G54220.2; AT1G54220.2; AT1G54220.
KEGGiath:AT1G54220.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY033001 mRNA. Translation: AAK53067.1.
AC005287 Genomic DNA. Translation: AAD25602.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE33067.1.
CP002684 Genomic DNA. Translation: AEE33068.1.
AY136410 mRNA. Translation: AAM97076.1.
BT020419 mRNA. Translation: AAV97810.1.
PIRiE96583.
RefSeqiNP_001031186.1. NM_001036109.1.
NP_564654.1. NM_104300.4.
UniGeneiAt.19093.
At.21338.

3D structure databases

ProteinModelPortaliQ5M729.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi27088. 1 interactor.
STRINGi3702.AT1G54220.1.

Proteomic databases

PaxDbiQ5M729.
PRIDEiQ5M729.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G54220.1; AT1G54220.1; AT1G54220.
AT1G54220.2; AT1G54220.2; AT1G54220.
GeneIDi841863.
GrameneiAT1G54220.1; AT1G54220.1; AT1G54220.
AT1G54220.2; AT1G54220.2; AT1G54220.
KEGGiath:AT1G54220.

Organism-specific databases

TAIRiAT1G54220.

Phylogenomic databases

eggNOGiKOG0557. Eukaryota.
COG0508. LUCA.
HOGENOMiHOG000281566.
InParanoidiQ5M729.
KOiK00627.
OMAiVHIGMAT.
OrthoDBiEOG093607WT.
PhylomeDBiQ5M729.

Enzyme and pathway databases

BioCyciARA:AT1G54220-MONOMER.
ReactomeiR-ATH-70268. Pyruvate metabolism.

Miscellaneous databases

PROiQ5M729.

Gene expression databases

GenevisibleiQ5M729. AT.

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.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR006257. LAT1.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMiSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsiTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiODP23_ARATH
AccessioniPrimary (citable) accession number: Q5M729
Secondary accession number(s): Q8L787, Q94IP5, Q9SLL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: February 1, 2005
Last modified: November 30, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.