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P49432

- ODPB_RAT

UniProt

P49432 - ODPB_RAT

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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene
Pdhb
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Thiamine pyrophosphate By similarity.

Sites

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

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: RGD
  2. pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: RGD
  2. glucose metabolic process Source: UniProtKB-KW
  3. tricarboxylic acid cycle Source: UniProtKB
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_203088. Pyruvate metabolism.

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: Chromosome 15

Organism-specific databases

RGDi1359146. Pdhb.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. mitochondrion Source: RGD
  3. 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 – 671Phosphotyrosine By similarity
Modified residuei354 – 3541N6-acetyllysine By 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.

Protein-protein interaction databases

IntActiP49432. 2 interactions.
MINTiMINT-4592348.
STRINGi10116.ENSRNOP00000010545.

Structurei

3D structure databases

ProteinModelPortaliP49432.
SMRiP49432. Positions 30-359.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0022.
GeneTreeiENSGT00530000063423.
HOGENOMiHOG000281450.
HOVERGENiHBG000917.
InParanoidiP49432.
KOiK00162.
OMAiNVKVPMV.
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

MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD    50
EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA 100
MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSAGLQPV PIVFRGPNGA 150
SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDDNPVVML 200
ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV AHSRPVGHCL 250
EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG 300
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII 350
FAIKKTLNI 359
Length:359
Mass (Da):38,982
Last modified:January 9, 2007 - v2
Checksum:i1B942D0A68C86D51
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31A → G1 Publication
Sequence conflicti11 – 155PLRQA → LCGRL1 Publication
Sequence conflicti22 – 221R → L1 Publication
Sequence conflicti25 – 251R → C1 Publication
Sequence conflicti238 – 2381T → N1 Publication
Sequence conflicti241 – 2422AH → CY1 Publication
Sequence conflicti259 – 2591E → G1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
BC079137 mRNA. Translation: AAH79137.1 .
PIRi S15892.
RefSeqi NP_001007621.1. NM_001007620.1.
XP_006251816.1. XM_006251754.1.
UniGenei Rn.102424.

3D structure databases

ProteinModelPortali P49432.
SMRi P49432. Positions 30-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P49432. 2 interactions.
MINTi MINT-4592348.
STRINGi 10116.ENSRNOP00000010545.

PTM databases

PhosphoSitei P49432.

2D gel databases

UCD-2DPAGE P49432.
World-2DPAGE 0004:P49432.

Proteomic databases

PaxDbi P49432.
PRIDEi P49432.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000010545 ; ENSRNOP00000010545 ; ENSRNOG00000007895 .
GeneIDi 289950.
KEGGi rno:289950.

Organism-specific databases

CTDi 5162.
RGDi 1359146. Pdhb.

Phylogenomic databases

eggNOGi COG0022.
GeneTreei ENSGT00530000063423.
HOGENOMi HOG000281450.
HOVERGENi HBG000917.
InParanoidi P49432.
KOi K00162.
OMAi NVKVPMV.
OrthoDBi EOG7KSX8S.
PhylomeDBi P49432.
TreeFami TF105674.

Enzyme and pathway databases

Reactomei REACT_203088. Pyruvate metabolism.

Miscellaneous databases

NextBioi 630523.
PROi P49432.

Gene expression databases

Genevestigatori P49432.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
PANTHERi PTHR11624:SF56. PTHR11624:SF56. 1 hit.
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 113 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

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