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P52904 (ODPB_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Short name=PDHE1-B
EC=1.2.4.1
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length359 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).

Catalytic activity

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

Cofactor

Thiamine pyrophosphate.

Subunit structure

Tetramer of 2 alpha and 2 beta subunits By similarity.

Subcellular location

Mitochondrion matrix.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process from pyruvate

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 1919Mitochondrion By similarity
Chain20 – 359340Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000020463

Sites

Binding site821Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P52904 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 5AFE49F165C13C83

FASTA35938,793
        10         20         30         40         50         60 
MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG EEVGEYQGAY 

        70         80         90        100        110        120 
KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV VEFMTFNFSM QAIDHIINSA 

       130        140        150        160        170        180 
AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ HSHCYASWYG SCPGLKVLVP HSAEDARGLL 

       190        200        210        220        230        240 
KAAIRDPDPV VFLENELLYG ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG 

       250        260        270        280        290        300 
FALKAAEILE KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT 

       310        320        330        340        350 
SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH RSVPLAAAA 

« Hide

References

[1]Luethy M.H., Miernyk J.A., Randall D.D.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U56697 mRNA. Translation: AAB01223.1.
PIRT06532.

3D structure databases

ProteinModelPortalP52904.
SMRP52904. Positions 25-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP52904. 1 interaction.

Proteomic databases

PRIDEP52904.
ProMEXP52904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.920. 1 hit.
InterProIPR027110. PDHB.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERPTHR11624:SF11. PTHR11624:SF11. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPB_PEA
AccessionPrimary (citable) accession number: P52904
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program