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Q5M729 (ODP23_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Ordered Locus Names:At1g54220
ORF Names:F20D21.4
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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). Ref.7

Catalytic activity

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

Cofactor

Binds 1 lipoyl cofactor covalently.

Subcellular location

Mitochondrion matrix Ref.6.

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family.

Contains 1 lipoyl-binding domain.

Sequence caution

The sequence AAD25602.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion
Chain? – 539Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrialPRO_0000260027

Regions

Domain112 – 18675Lipoyl-binding
Region250 – 28132E3-binding site By similarity

Sites

Active site5121 Potential
Active site5161 Potential

Amino acid modifications

Modified residue1521N6-lipoyllysine By similarity

Experimental info

Sequence conflict451T → I in AAK53067. Ref.1
Sequence conflict2671I → T in AAK53067. Ref.1
Sequence conflict4421N → S in AAM97076. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q5M729 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: 0C4E141079A2698F

FASTA53958,467
        10         20         30         40         50         60 
MAYASRIINH SKKLKDVSTL LRRENAATIR YYSNTNRAPL NREDTFNSRL GYPPLERISI 

        70         80         90        100        110        120 
CSTSTLPVSI IFSTTRSNLS SAMGRPIFGK EFSCLMQSAR GFSSGSDLPP HQEIGMPSLS 

       130        140        150        160        170        180 
PTMTEGNIAR WLKKEGDKVA PGEVLCEVET DKATVEMECM EEGYLAKIVK AEGSKEIQVG 

       190        200        210        220        230        240 
EVIAITVEDE EDIGKFKDYT PSSTADAAPT KAEPTPAPPK EEKVKQPSSP PEPKASKPST 

       250        260        270        280        290        300 
PPTGDRVFAS PLARKLAEDN NVPLSDIEGT GPEGRIVKAD IDEYLASSGK GATAKPSKST 

       310        320        330        340        350        360 
DSKAPALDYV DIPHSQIRKV TASRLAFSKQ TIPHYYLTVD TCVDKLMALR SQLNSFKEAS 

       370        380        390        400        410        420 
GGKRISVNDL VVKAAALALR KVPQCNSSWT DDYIRQFKNV NINVAVQTEN GLYVPVVKDA 

       430        440        450        460        470        480 
DRKGLSTIGE EVRLLAQKAK ENSLKPEDYE GGTFTVSNLG GPFGIKQFCA VVNPPQAAIL 

       490        500        510        520        530 
AVGSAEKRVV PGNGPDQFNF ASYMPVTLSC DHRVVDGAIG AEWLKAFKGY IENPKSMLL 

« Hide

References

« Hide 'large scale' references
[1]"Mono-lipoyl E2 from pyruvate dehydrogenase complex from Arabidopsis."
Broz A.K., Randall D.D., Miernyk J.A., Mooney B.P.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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. expand/collapse author list , 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.
[5]"Arabidopsis ORF clones."
Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[6]"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.
[7]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRE96583.
RefSeqNP_001031186.1. NM_001036109.1.
NP_564654.1. NM_104300.3.
UniGeneAt.19093.
At.21338.

3D structure databases

ProteinModelPortalQ5M729.
SMRQ5M729. Positions 113-192, 246-286, 305-539.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ5M729.
PRIDEQ5M729.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G54220.1; AT1G54220.1; AT1G54220.
AT1G54220.2; AT1G54220.2; AT1G54220.
GeneID841863.
KEGGath:AT1G54220.

Organism-specific databases

TAIRAT1G54220.

Phylogenomic databases

eggNOGCOG0508.
HOGENOMHOG000281566.
InParanoidQ5M729.
KOK00627.
OMASSAMGRP.
PhylomeDBQ5M729.
ProtClustDBPLN02744.

Enzyme and pathway databases

BioCycARA:AT1G54220-MONOMER.
ARA:GQT-1082-MONOMER.

Gene expression databases

GenevestigatorQ5M729.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 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]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 1 hit.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 1 hit.
TIGRFAMsTIGR01349. PDHac_trf_mito. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODP23_ARATH
AccessionPrimary (citable) accession number: Q5M729
Secondary accession number(s): Q8L787, Q94IP5, Q9SLL0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2006
Last sequence update: February 1, 2005
Last modified: March 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names