Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial precursor

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Q38799 (ODPB1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 116. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
Short name=PDHE1-B
EC=1.2.4.1

Alternative name(s):
Protein MACCI-BOU

Gene names

Name:	PDH2
Synonyms:	MAB1
Ordered Locus Names:	At5g50850
ORF Names:	K16E14.1

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › 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 CO₂. 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 structure	Tetramer of 2 alpha and 2 beta subunits By similarity.
Subcellular location	Mitochondrion matrix.
Tissue specificity	Expressed in roots, immature rosettes, and mature rosettes. Ref.1

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from electronic annotation. Source: InterPro defense response to bacterium Inferred from expression pattern PubMed 17028151. Source: TAIR glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	apoplast Inferred from direct assay PubMed 21798377. Source: TAIR mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 11743114 PubMed 11743115 Ref.5 PubMed 15276431 PubMed 22923678. Source: TAIR nucleolus Inferred from direct assay PubMed 15496452. Source: TAIR vacuolar membrane Inferred from direct assay PubMed 17151019. Source: TAIR
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

Mitochondrion By similarity

Chain

30 – 363

334

Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial

PRO_0000020462

Sites

Binding site

Thiamine pyrophosphate By similarity

Amino acid modifications

Cross-link

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Cross-link

247

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Cross-link

254

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Experimental info

Sequence conflict

334

M → I in AAA52225. Ref.1

Sequence conflict

337

A → T in AAA52225. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q38799 [UniParc].

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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. 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]	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. Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta.
[6]	"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] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-247 AND LYS-254, MASS SPECTROMETRY. Strain: cv. Landsberg erecta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U09137 mRNA. Translation: AAA52225.1. AB026637 Genomic DNA. Translation: BAA98121.1. CP002688 Genomic DNA. Translation: AED96001.1. AY070728 mRNA. Translation: AAL50070.1. BT000839 mRNA. Translation: AAN38676.1.
IPI	IPI00538502.
RefSeq	NP_199898.1. NM_124463.3.
UniGene	At.24270.
3D structure databases
ProteinModelPortal	Q38799.
SMR	Q38799. Positions 35-357.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q38799. 2 interactions.
2D gel databases
SWISS-2DPAGE	Q38799.
Proteomic databases
PaxDb	Q38799.
PRIDE	Q38799.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G50850.1; AT5G50850.1; AT5G50850.
GeneID	835157.
KEGG	ath:AT5G50850.
Organism-specific databases
GeneFarm	2003.
TAIR	At5g50850.
Phylogenomic databases
eggNOG	COG0022.
HOGENOM	HOG000281450.
InParanoid	Q38799.
KO	K00162.
OMA	QHSQDYS.
PhylomeDB	Q38799.
ProtClustDB	PLN02683.
Gene expression databases
ArrayExpress	Q38799.
Genevestigator	Q38799.
GermOnline	AT5G50850. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
InterPro	IPR027110. PDHB. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view]
PANTHER	PTHR11624:SF11. PTHR11624:SF11. 1 hit.
Pfam	PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view]
SMART	SM00861. Transket_pyr. 1 hit. [Graphical view]
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODPB1_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:	May 1, 2013
This is version 116 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents