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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

PDHB

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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

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

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  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

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595 Componenti: Chromosome 3

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrial matrix Source: UniProtKB-SubCell
  3. nucleus Source: Ensembl
  4. pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000271409Add
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

PRIDEiQ5RE79.

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

Structurei

3D structure databases

ProteinModelPortaliQ5RE79.
SMRiQ5RE79. Positions 30-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063423.
HOVERGENiHBG000917.
InParanoidiQ5RE79.
KOiK00162.
OMAiDIPTPYN.
OrthoDBiEOG7KSX8S.
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.

Q5RE79-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVSGLVRR PLREVSRLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD
60 70 80 90 100
EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA
110 120 130 140 150
MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSGGLQPV PIVFRGPNGA
160 170 180 190 200
SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDNNPVVVL
210 220 230 240 250
ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV SHSRPVGHCL
260 270 280 290 300
EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG
310 320 330 340 350
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII

FAIKKTLNI
Length:359
Mass (Da):39,333
Last modified:December 20, 2004 - v1
Checksum:i8575D7E8740D431B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857655 mRNA. Translation: CAH89928.1.
RefSeqiNP_001124905.1. NM_001131433.2.
UniGeneiPab.11853.

Genome annotation databases

EnsembliENSPPYT00000016006; ENSPPYP00000015393; ENSPPYG00000013760.
GeneIDi100171772.
KEGGipon:100171772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857655 mRNA. Translation: CAH89928.1.
RefSeqiNP_001124905.1. NM_001131433.2.
UniGeneiPab.11853.

3D structure databases

ProteinModelPortaliQ5RE79.
SMRiQ5RE79. Positions 30-359.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ5RE79.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSPPYT00000016006; ENSPPYP00000015393; ENSPPYG00000013760.
GeneIDi100171772.
KEGGipon:100171772.

Organism-specific databases

CTDi5162.

Phylogenomic databases

GeneTreeiENSGT00530000063423.
HOVERGENiHBG000917.
InParanoidiQ5RE79.
KOiK00162.
OMAiDIPTPYN.
OrthoDBiEOG7KSX8S.
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.
ProtoNetiSearch...

Publicationsi

  1. The German cDNA consortium
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Heart.

Entry informationi

Entry nameiODPB_PONAB
AccessioniPrimary (citable) accession number: Q5RE79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 8, 2007
Last sequence update: December 20, 2004
Last modified: March 3, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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.