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O44451 (ODPB_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize 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-1
ORF Names:C04C3.3
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length352 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. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. UniProtKB P11177

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. UniProtKB P11177

Cofactor

Thiamine pyrophosphate By similarity. UniProtKB P11177

Subunit structure

Tetramer of 2 alpha and 2 beta subunits By similarity.

Subcellular location

Mitochondrion matrix By similarity UniProtKB P11177.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 20188671. Source: WormBase

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion Potential
Chain22 – 352331Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000042638

Sites

Binding site811Thiamine pyrophosphate By similarity UniProtKB P11177

Sequences

Sequence LengthMass (Da)Tools
O44451 [UniParc].

Last modified October 1, 2001. Version 2.
Checksum: 37F4A4A28C8ADECA

FASTA35238,141
        10         20         30         40         50         60 
MALRKCGNLF VARLAGTSTR AASTMTVRDA LNQAMDEEIK RDDRVFLMGE EVAQYDGAYK 

        70         80         90        100        110        120 
ISKGLWKKHG DKRVVDTPIT EMGFAGIAVG AAFAGLRPIC EFMTFNFSMQ AIDQIINSAA 

       130        140        150        160        170        180 
KTYYMSAGRV PVPIVFRGPN GAAAGVAAQH SQDFSAWYAH CPGLKVVCPY SAEDAKGLLK 

       190        200        210        220        230        240 
AAIRDDNPVV FLENEILYGQ SFPVGDEVLS DDFVVPIGKA KIERAGDHVT IVSYSRGVEF 

       250        260        270        280        290        300 
SLEAAKQLEA IGVSAEVINL RSLRPFDFES IRQSVHKTHH LVSVETGWPF AGIGSEIAAQ 

       310        320        330        340        350 
VMESDVFDQL DAPLLRVTGV DVPMPYTQTL EAAALPTAEH VVKAVKKSLN IA 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]Bienvenut W.V.
Submitted (SEP-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 130-137; 237-246 AND 262-272, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO080230 Genomic DNA. Translation: CCD62196.1.
PIRT32598.
RefSeqNP_500340.1. NM_067939.5.
UniGeneCel.7275.

3D structure databases

ProteinModelPortalO44451.
SMRO44451. Positions 25-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid42248. 6 interactions.
DIPDIP-24348N.
IntActO44451. 5 interactions.
MINTMINT-1052850.
STRING6239.C04C3.3.2.

Proteomic databases

PaxDbO44451.
PRIDEO44451.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaC04C3.3.1; C04C3.3.1; C04C3.3.
C04C3.3.2; C04C3.3.2; C04C3.3.
GeneID177108.
KEGGcel:CELE_C04C3.3.
UCSCC04C3.3.1. c. elegans.

Organism-specific databases

CTD177108.
WormBaseC04C3.3; CE27647; WBGene00015413; pdhb-1.

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHOG000281450.
InParanoidO44451.
KOK00162.
OMADIPTPYN.
PhylomeDBO44451.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Other

NextBio895372.
PROO44451.

Entry information

Entry nameODPB_CAEEL
AccessionPrimary (citable) accession number: O44451
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 1, 2001
Last modified: April 16, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase