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P49432 (ODPB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Pdhb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length359 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion Ref.3
Chain31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000020459

Sites

Binding site891Thiamine pyrophosphate By similarity

Amino acid modifications

Modified residue671Phosphotyrosine By similarity
Modified residue3541N6-acetyllysine By similarity

Experimental info

Sequence conflict31A → G Ref.1
Sequence conflict11 – 155PLRQA → LCGRL Ref.1
Sequence conflict221R → L Ref.1
Sequence conflict251R → C Ref.1
Sequence conflict2381T → N Ref.1
Sequence conflict241 – 2422AH → CY Ref.1
Sequence conflict2591E → G Ref.1

Sequences

Sequence LengthMass (Da)Tools
P49432 [UniParc].

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

FASTA35938,982
        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' 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, IDENTIFICATION BY 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.
PIRS15892.
RefSeqNP_001007621.1. NM_001007620.1.
XP_006251816.1. XM_006251754.1.
UniGeneRn.102424.

3D structure databases

ProteinModelPortalP49432.
SMRP49432. Positions 30-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP49432. 2 interactions.
MINTMINT-4592348.
STRING10116.ENSRNOP00000010545.

PTM databases

PhosphoSiteP49432.

2D gel databases

UCD-2DPAGEP49432.
World-2DPAGE0004:P49432.

Proteomic databases

PaxDbP49432.
PRIDEP49432.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010545; ENSRNOP00000010545; ENSRNOG00000007895.
GeneID289950.
KEGGrno:289950.

Organism-specific databases

CTD5162.
RGD1359146. Pdhb.

Phylogenomic databases

eggNOGCOG0022.
GeneTreeENSGT00530000063423.
HOGENOMHOG000281450.
HOVERGENHBG000917.
InParanoidP49432.
KOK00162.
OMANVKVPMV.
OrthoDBEOG7KSX8S.
PhylomeDBP49432.
TreeFamTF105674.

Gene expression databases

GenevestigatorP49432.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Other

NextBio630523.
PROP49432.

Entry information

Entry nameODPB_RAT
AccessionPrimary (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: June 11, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program