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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

PDHB

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

Cofactori

thiamine diphosphateBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei194Important for interaction with DLATBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processCarbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle
LigandPyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrialBy similarity (EC:1.2.4.1)
Short name:
PDHE1-BBy similarity
Gene namesi
Name:PDHBBy similarity
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaCricetidaeCricetinaeMesocricetus
Proteomesi
  • UP000189706 Componenti: Genome assembly

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000394306‹1 – ›211Pyruvate dehydrogenase E1 component subunit beta, mitochondrialAdd BLAST›211

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP86222.

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. Interacts with DLAT.By similarity

Structurei

3D structure databases

ProteinModelPortaliP86222.
SMRiP86222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
InterProiView protein in InterPro
IPR029061. THDP-binding.
IPR009014. Transketo_C/PFOR_II.
IPR005475. Transketolase-like_Pyr-bd.
IPR033248. Transketolase_C.
PfamiView protein in Pfam
PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
SMARTiView protein in SMART
SM00861. Transket_pyr. 1 hit.
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Fragments.

P86222-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
EAINQGMDEE LERDEKVFLL GEEVAQYDGA YKVSRTYYMS AGLQPVPIVF
60 70 80 90 100
RGPNGASAGV AAQHSQCFAA WYGHCPGLKV VSPWNSEDAK GLIKSAIRDD
110 120 130 140 150
NPVVMLENEL MYGVAFELPT EAQSKDFLIP IGKEGIECEV INLRTIRPMD
160 170 180 190 200
IEAIEASVMK TNHLVTVEGG WPQFGVGAEI CARIMEGPAF NFLDAPAVRV
210
TGADVPMPYA K
Length:211
Mass (Da):23,010
Last modified:May 18, 2010 - v1
Checksum:i0F24DCE9BB09B3E7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11
Non-adjacent residuesi35 – 36Curated2
Non-adjacent residuesi133 – 134Curated2
Non-terminal residuei2111

Similar proteinsi

Entry informationi

Entry nameiODPB_MESAU
AccessioniPrimary (citable) accession number: P86222
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: May 18, 2010
Last modified: October 25, 2017
This is version 29 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome