ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q38799


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name ODPB_ARATH
Primary accession number Q38799
Secondary accession number Q9LSM8
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on June 6, 2002 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 77)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit beta, mitochondrial [Precursor]
Synonyms PDHE1-B
EC 1.2.4.1
Gene name
Name: PDH2
OrderedLocusNames: At5g50850
ORFNames: K16E14.1
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
DOI=10.1016/0005-2728(94)90171-6; PubMed=8061040 [NCBI, ExPASy, EBI, Israel, Japan]
Luethy M.H., Miernyk J.A., Randall D.D.;
"The nucleotide and deduced amino acid sequences of a cDNA encoding the E1 beta-subunit of the Arabidopsis thaliana mitochondrial pyruvate dehydrogenase complex.";
Biochim. Biophys. Acta 1187:95-98(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1105/tpc.016055; PubMed=14671022 [NCBI, ExPASy, EBI, Israel, Japan]
Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H.;
"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins.";
Plant Cell 16:241-256(2004).
[5]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-247 AND LYS-254, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M600408-MCP200; PubMed=17272265 [NCBI, ExPASy, EBI, Israel, Japan]
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
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 + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • SUBUNIT: Tetramer of 2 alpha and 2 beta subunits (By similarity).
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U09137; AAA52225.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB026637; BAA98121.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY070728; AAL50070.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT000839; AAN38676.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_199898.1; -.
UniGene At.24270
3D structure databases
HSSP P11177; 1NI4. [HSSP ENTRY / PDB]
ModBase Q38799.
2D gel databases
SWISS-2DPAGE Q38799; -.
Organism-specific databases
GeneFarm 2003; -.
TAIR At5g50850; -.
Gene expression databases
ArrayExpress Q38799; -.
GermOnline AT5G50850; Arabidopsis thaliana.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.
Family and domain databases
InterPro IPR005476; Transketo_C.
IPR005475; Transketo_Cen_R.
IPR015941; Transketolase_C-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.920; Transketo_C_like; 1.
Pfam PF02779; Transket_pyr; 1.
PF02780; Transketolase_C; 1.
Pfam graphical view of domain structure.
BLOCKS Q38799.
Genome annotation databases
GeneID 835157; -.
GenomeReviews BA000015_GR; AT5G50850.
KEGG ath:AT5G50850; -.
NMPDR fig|3702.1.peg.26947; -.
Other
ProtoNet Q38799.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Thiamine pyrophosphate; Transit peptide; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    29  29     Mitochondrion (By similarity). 
CHAIN   30   363  334     Pyruvate dehydrogenase E1 component subunit beta, mitochondrial. PRO_0000020462
BINDING   92    92        Thiamine pyrophosphate (By similarity). 
CROSSLNK   34    34        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   247   247        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   254   254        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CONFLICT   334   334        M -> I (in Ref. 1; AAA52225). 
CONFLICT   337   337        A -> T (in Ref. 1; AAA52225). 
Sequence information
Length: 363 AA [This is the length of the unprocessed precursor] Molecular weight: 39176 Da [This is the MW of the unprocessed precursor] CRC64: D044E3A336D4EC52 [This is a checksum on the sequence]
        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 

Q38799 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!