Pyruvate dehydrogenase E1 component subunit beta, mitochondrial precursor

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P49432 (ODPB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 103. History...

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

Third-party data

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

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:

Pdhb

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	359 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, and thereby links the glycolytic pathway to the tricarboxylic cycle By similarity.
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.
Cofactor	Thiamine pyrophosphate By similarity.
Subunit structure	Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules By similarity.
Subcellular location	Mitochondrion matrix By similarity.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay PubMed 7487891. Source: RGD glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay PubMed 7487891. Source: RGD pyruvate dehydrogenase complex Inferred from direct assay PubMed 7487891. Source: RGD
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from direct assay PubMed 7487891. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

Mitochondrion Ref.3

Chain

31 – 359

329

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

PRO_0000020459

Sites

Binding site

Thiamine pyrophosphate By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Experimental info

Sequence conflict

A → G Ref.1

Sequence conflict

11 – 15

PLRQA → LCGRL Ref.1

Sequence conflict

R → L Ref.1

Sequence conflict

R → C Ref.1

Sequence conflict

238

T → N Ref.1

Sequence conflict

241 – 242

AH → CY Ref.1

Sequence conflict

259

E → G Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P49432 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: 1B942D0A68C86D51
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FASTA

359

38,982

        10         20         30         40         50         60 
MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD EKVFLLGEEV 

        70         80         90        100        110        120 
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 

       130        140        150        160        170        180 
DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS 

       190        200        210        220        230        240 
EDAKGLIKSA IRDDNPVVML ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV 

       250        260        270        280        290        300 
AHSRPVGHCL EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG 

       310        320        330        340        350 
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase." Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T. Biochim. Biophys. Acta 1089:1-7(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[3]	Dunn M.J. Submitted (MAR-1996) to UniProtKB Cited for: PROTEIN SEQUENCE OF 31-38. Tissue: Heart.
[4]	Lubec G., Afjehi-Sadat L., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 286-324, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC079137 mRNA. Translation: AAH79137.1.
IPI	IPI00194324.
PIR	S15892.
RefSeq	NP_001007621.1. NM_001007620.1.
UniGene	Rn.102424.
3D structure databases
ProteinModelPortal	P49432.
SMR	P49432. Positions 30-359.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49432. 1 interaction.
MINT	MINT-4592348.
STRING	10116.ENSRNOP00000010545.
PTM databases
PhosphoSite	P49432.
2D gel databases
UCD-2DPAGE	P49432.
World-2DPAGE	0004:P49432.
Proteomic databases
PaxDb	P49432.
PRIDE	P49432.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010545; ENSRNOP00000010545; ENSRNOG00000007895.
GeneID	289950.
KEGG	rno:289950.
Organism-specific databases
CTD	5162.
RGD	1359146. Pdhb.
Phylogenomic databases
eggNOG	COG0022.
GeneTree	ENSGT00530000063423.
HOGENOM	HOG000281450.
HOVERGEN	HBG000917.
InParanoid	P49432.
KO	K00162.
OMA	QHSQDYS.
OrthoDB	EOG4CJVHD.
Gene expression databases
Genevestigator	P49432.
GermOnline	ENSRNOG00000007895. Rattus norvegicus.
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...
Other
NextBio	630523.

Entry information

Entry name

ODPB_RAT

Accession

Primary (citable) accession number: P49432
Secondary accession number(s): Q6AY95

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 9, 2007
Last modified:	April 3, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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

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

PTM 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

Other

Entry information