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Reviewed, UniProtKB/Swiss-Prot Q38799 (ODPB_ARATH)

Last modified November 4, 2008. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
      Short name=PDHE1-B
    EC=1.2.4.1
Gene names
Name: PDH2
Ordered Locus Names: At5g50850
ORF Names: K16E14.1
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length363 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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).

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).

Cofactor

Thiamine pyrophosphate.

Subunit structure

Tetramer of 2 alpha and 2 beta subunits By similarity.

Subcellular location

Mitochondrion matrix.

Ontologies

Keywords

   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMUbl conjugation
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion By similarity
Chain30 – 363334Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000020462

Sites

Binding site921Thiamine pyrophosphate By similarity

Amino acid modifications

Cross-link34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link247Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Experimental info

Sequence conflict3341M → I in AAA52225. Ref.1
Sequence conflict3371A → T in AAA52225. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q38799-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: D044E3A336D4EC52

FASTA36339,176
        10         20         30         40         50         60 
MLGILRQRAI DGASTLRRTR FALVSARSYA AGAKEMTVRD ALNSAIDEEM SADPKVFVMG 

        70         80         90        100        110        120 
EEVGQYQGAY KITKGLLEKY GPERVYDTPI TEAGFTGIGV GAAYAGLKPV VEFMTFNFSM 

       130        140        150        160        170        180 
QAIDHIINSA AKSNYMSAGQ INVPIVFRGP NGAAAGVGAQ HSQCYAAWYA SVPGLKVLAP 

       190        200        210        220        230        240 
YSAEDARGLL KAAIRDPDPV VFLENELLYG ESFPISEEAL DSSFCLPIGK AKIEREGKDV 

       250        260        270        280        290        300 
TIVTFSKMVG FALKAAEKLA EEGISAEVIN LRSIRPLDRA TINASVRKTS RLVTVEEGFP 

       310        320        330        340        350        360 
QHGVCAEICA SVVEESFSYL DAPVERIAGA DVPMPYAANL ERLALPQIED IVRASKRACY 


RSK 

« Hide

References

[1]"The nucleotide and deduced amino acid sequences of a cDNA encoding the E1 beta-subunit of the Arabidopsis thaliana mitochondrial pyruvate dehydrogenase complex."
Luethy M.H., Miernyk J.A., Randall D.D.
Biochim. Biophys. Acta 1187:95-98(1994) [PubMed: 8061040] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. XI."
Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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. 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: 14593172] [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: 14671022] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[5]"Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants."
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.
Mol. Cell. Proteomics 6:601-610(2007) [PubMed: 17272265] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-247 AND LYS-254, MASS SPECTROMETRY.

Cross-references

Sequence databases

U09137 mRNA. Translation: AAA52225.1.
AB026637 Genomic DNA. Translation: BAA98121.1.
AY070728 mRNA. Translation: AAL50070.1.
BT000839 mRNA. Translation: AAN38676.1.
RefSeqNP_199898.1.
UniGeneAt.24270

3D structure databases

HSSPHSSP built from PDB template 1NI4 based on UniProtKB P11177.
ModBaseSearch...

2-D gel databases

SWISS-2DPAGEQ38799.

Genome annotation databases

GeneID835157.
GenomeReviewsGene locus AT5G50850 in contig BA000015_GR.
KEGGath:AT5G50850.
NMPDRfig|3702.1.peg.26947.

Organism-specific databases

GeneFarm2003.
TAIRAt5g50850.

Gene expression databases

ArrayExpressQ38799.
GermOnlineAT5G50850. Arabidopsis thaliana.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR005475. Transketo_Cen_R.
IPR015941. Transketolase_C-like.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODPB_ARATH
AccessionPrimary (citable) accession number: Q38799
Secondary accession number(s): Q9LSM8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 6, 2002
Last modified: November 4, 2008
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents