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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

Pdhb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891Thiamine pyrophosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_275973. Pyruvate metabolism.
REACT_312589. Signaling by Retinoic Acid.
REACT_321551. Regulation of pyruvate dehydrogenase (PDH) complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-B
Gene namesi
Name:Pdhb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi1359146. Pdhb.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: RGD
  • nucleoplasm Source: Ensembl
  • pyruvate dehydrogenase complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
BLAST
Chaini31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020459Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei354 – 3541N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP49432.
PRIDEiP49432.

2D gel databases

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

PTM databases

PhosphoSiteiP49432.

Expressioni

Gene expression databases

GenevestigatoriP49432.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi253064. 1 interaction.
IntActiP49432. 2 interactions.
MINTiMINT-4592348.
STRINGi10116.ENSRNOP00000010545.

Structurei

3D structure databases

ProteinModelPortaliP49432.
SMRiP49432. Positions 30-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0022.
GeneTreeiENSGT00530000063423.
HOGENOMiHOG000281450.
HOVERGENiHBG000917.
InParanoidiP49432.
KOiK00162.
OMAiDIPTPYN.
OrthoDBiEOG7KSX8S.
PhylomeDBiP49432.
TreeFamiTF105674.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD
60 70 80 90 100
EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA
110 120 130 140 150
MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSAGLQPV PIVFRGPNGA
160 170 180 190 200
SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDDNPVVML
210 220 230 240 250
ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV AHSRPVGHCL
260 270 280 290 300
EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG
310 320 330 340 350
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII

FAIKKTLNI
Length:359
Mass (Da):38,982
Last modified:January 9, 2007 - v2
Checksum:i1B942D0A68C86D51
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31A → G (PubMed:2025639).Curated
Sequence conflicti11 – 155PLRQA → LCGRL (PubMed:2025639).Curated
Sequence conflicti22 – 221R → L (PubMed:2025639).Curated
Sequence conflicti25 – 251R → C (PubMed:2025639).Curated
Sequence conflicti238 – 2381T → N (PubMed:2025639).Curated
Sequence conflicti241 – 2422AH → CY (PubMed:2025639).Curated
Sequence conflicti259 – 2591E → G (PubMed:2025639).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079137 mRNA. Translation: AAH79137.1.
PIRiS15892.
RefSeqiNP_001007621.1. NM_001007620.1.
XP_006251816.1. XM_006251754.1.
UniGeneiRn.102424.

Genome annotation databases

EnsembliENSRNOT00000010545; ENSRNOP00000010545; ENSRNOG00000007895.
GeneIDi289950.
KEGGirno:289950.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC079137 mRNA. Translation: AAH79137.1.
PIRiS15892.
RefSeqiNP_001007621.1. NM_001007620.1.
XP_006251816.1. XM_006251754.1.
UniGeneiRn.102424.

3D structure databases

ProteinModelPortaliP49432.
SMRiP49432. Positions 30-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi253064. 1 interaction.
IntActiP49432. 2 interactions.
MINTiMINT-4592348.
STRINGi10116.ENSRNOP00000010545.

PTM databases

PhosphoSiteiP49432.

2D gel databases

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

Proteomic databases

PaxDbiP49432.
PRIDEiP49432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010545; ENSRNOP00000010545; ENSRNOG00000007895.
GeneIDi289950.
KEGGirno:289950.

Organism-specific databases

CTDi5162.
RGDi1359146. Pdhb.

Phylogenomic databases

eggNOGiCOG0022.
GeneTreeiENSGT00530000063423.
HOGENOMiHOG000281450.
HOVERGENiHBG000917.
InParanoidiP49432.
KOiK00162.
OMAiDIPTPYN.
OrthoDBiEOG7KSX8S.
PhylomeDBiP49432.
TreeFamiTF105674.

Enzyme and pathway databases

ReactomeiREACT_275973. Pyruvate metabolism.
REACT_312589. Signaling by Retinoic Acid.
REACT_321551. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

NextBioi630523.
PROiP49432.

Gene expression databases

GenevestigatoriP49432.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiODPB_RAT
AccessioniPrimary (citable) accession number: P49432
Secondary accession number(s): Q6AY95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 9, 2007
Last modified: May 27, 2015
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.