Reviewed, UniProtKB/Swiss-Prot Q38799 (ODPB_ARATH)

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	363 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 29	29	Mitochondrion By similarity
	Chain	30 – 363	334	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PRO_0000020462
Sites
	Binding site	92	1	Thiamine pyrophosphate By similarity
Amino acid modifications
	Cross-link	34		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	247		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
	Cross-link	254		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Experimental info
	Sequence conflict	334	1	M → I in AAA52225. Ref.1
	Sequence conflict	337	1	A → T in AAA52225. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q38799-1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: D044E3A336D4EC52	FASTA	363	39,176
	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

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. , 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
EMBLGenBankDDBJ	U09137 mRNA. Translation: AAA52225.1. AB026637 Genomic DNA. Translation: BAA98121.1. AY070728 mRNA. Translation: AAL50070.1. BT000839 mRNA. Translation: AAN38676.1.
RefSeq	NP_199898.1.
UniGene	At.24270
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P11177.
ModBase	Search...
2-D gel databases
SWISS-2DPAGE	Q38799.
Genome annotation databases
GeneID	835157.
GenomeReviews	Gene locus AT5G50850 in contig BA000015_GR.
KEGG	ath:AT5G50850.
NMPDR	fig|3702.1.peg.26947.
Organism-specific databases
GeneFarm	2003.
TAIR	At5g50850.
Gene expression databases
ArrayExpress	Q38799.
GermOnline	AT5G50850. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR005476. Transketo_C. IPR005475. Transketo_Cen_R. IPR015941. Transketolase_C-like. [Graphical view]
Gene3D	G3DSA:3.40.50.920. Transketo_C_like. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ODPB_ARATH

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)