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Q8RWN9

- ODP22_ARATH

UniProt

Q8RWN9 - ODP22_ARATH

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Protein

Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial

Gene
At3g13930, MDC16.5
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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

Binds 1 lipoyl cofactor covalently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei512 – 5121 Reviewed prediction
Active sitei516 – 5161 Reviewed prediction

GO - Molecular functioni

  1. copper ion binding Source: TAIR
  2. dihydrolipoyllysine-residue acetyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
  2. pyruvate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciARA:AT3G13930-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial (EC:2.3.1.12)
Alternative name(s):
Dihydrolipoamide S-acetyltransferase component 2 of pyruvate dehydrogenase complex
Pyruvate dehydrogenase complex component E2 2
Short name:
PDC-E2 2
Short name:
PDCE2 2
Gene namesi
Ordered Locus Names:At3g13930
ORF Names:MDC16.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G13930.

Subcellular locationi

Mitochondrion matrix 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast envelope Source: TAIR
  3. mitochondrial matrix Source: UniProtKB-SubCell
  4. mitochondrion Source: TAIR
  5. pyruvate dehydrogenase complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 539Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260026
Transit peptidei1 – ?Mitochondrion

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei152 – 1521N6-lipoyllysine By similarity

Proteomic databases

PaxDbiQ8RWN9.
PRIDEiQ8RWN9.

Expressioni

Gene expression databases

GenevestigatoriQ8RWN9.

Structurei

3D structure databases

ProteinModelPortaliQ8RWN9.
SMRiQ8RWN9. Positions 113-192, 302-539.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 18675Lipoyl-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni250 – 28132E3-binding site By similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Lipoyl, Transit peptide

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000281566.
InParanoidiQ8RWN9.
KOiK00627.
OMAiMSMKEGT.
PhylomeDBiQ8RWN9.

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.

Q8RWN9-1 [UniParc]FASTAAdd to Basket

« Hide

MASRIINHSK KLKHVSALLR RDHAVAVRCF SNSTHPSLVG REDIFKARLN    50
YSSVERISKC GTGNVTMLSG ISTTSTKLSS PMAGPKLFKE FISSQMRSVR 100
GFSSSSDLPP HQEIGMPSLS PTMTEGNIAR WLKKEGDKVA PGEVLCEVET 150
DKATVEMECM EEGFLAKIVK EEGAKEIQVG EVIAITVEDE DDIQKFKDYT 200
PSSDTGPAAP EAKPAPSLPK EEKVEKPASA PEAKISKPSS APSEDRIFAS 250
PLARKLAEDN NVPLSSIKGT GPEGRIVKAD VEDFLASGSK ETTAKPSKQV 300
DSKVPALDYV DIPHTQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKMMGLR 350
SQLNSFQEAS GGKRISVNDL VIKAAALALR KVPQCNSSWT DEYIRQFKNV 400
NINVAVQTEN GLYVPVVKDA DKKGLSTIGE EVRFLAQKAK ENSLKPEDYE 450
GGTFTVSNLG GPFGIKQFCA VINPPQAAIL AIGSAEKRVV PGTGPDQYNV 500
ASYMSVTLSC DHRVIDGAIG AEWLKAFKGY IETPESMLL 539
Length:539
Mass (Da):58,468
Last modified:November 28, 2006 - v2
Checksum:i219B4BE0E7ACD05A
GO

Sequence cautioni

The sequence BAB02323.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241T → A in AAM12967. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019229 Genomic DNA. Translation: BAB02323.1. Sequence problems.
CP002686 Genomic DNA. Translation: AEE75442.1.
AF367302 mRNA. Translation: AAK32889.1.
AY091691 mRNA. Translation: AAM10290.1.
AY092968 mRNA. Translation: AAM12967.1.
BT000444 mRNA. Translation: AAN17421.1.
BT000702 mRNA. Translation: AAN31846.1.
BT001223 mRNA. Translation: AAN65110.1.
RefSeqiNP_566470.1. NM_112247.2.
UniGeneiAt.21338.

Genome annotation databases

EnsemblPlantsiAT3G13930.1; AT3G13930.1; AT3G13930.
GeneIDi820606.
KEGGiath:AT3G13930.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019229 Genomic DNA. Translation: BAB02323.1 . Sequence problems.
CP002686 Genomic DNA. Translation: AEE75442.1 .
AF367302 mRNA. Translation: AAK32889.1 .
AY091691 mRNA. Translation: AAM10290.1 .
AY092968 mRNA. Translation: AAM12967.1 .
BT000444 mRNA. Translation: AAN17421.1 .
BT000702 mRNA. Translation: AAN31846.1 .
BT001223 mRNA. Translation: AAN65110.1 .
RefSeqi NP_566470.1. NM_112247.2.
UniGenei At.21338.

3D structure databases

ProteinModelPortali Q8RWN9.
SMRi Q8RWN9. Positions 113-192, 302-539.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q8RWN9.
PRIDEi Q8RWN9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G13930.1 ; AT3G13930.1 ; AT3G13930 .
GeneIDi 820606.
KEGGi ath:AT3G13930.

Organism-specific databases

TAIRi AT3G13930.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000281566.
InParanoidi Q8RWN9.
KOi K00627.
OMAi MSMKEGT.
PhylomeDBi Q8RWN9.

Enzyme and pathway databases

BioCyci ARA:AT3G13930-MONOMER.

Gene expression databases

Genevestigatori Q8RWN9.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProi IPR003016. 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 ]
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsi TIGR01349. PDHac_trf_mito. 1 hit.
PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins."
    Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.
    Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: cv. Landsberg erecta.
  5. "Lipoic acid-dependent oxidative catabolism of alpha-keto acids in mitochondria provides evidence for branched-chain amino acid catabolism in Arabidopsis."
    Taylor N.L., Heazlewood J.L., Day D.A., Millar A.H.
    Plant Physiol. 134:838-848(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiODP22_ARATH
AccessioniPrimary (citable) accession number: Q8RWN9
Secondary accession number(s): Q9ASS8, Q9LVK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: June 11, 2014
This is version 90 of the entry and version 2 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

External Data

Dasty 3

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