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P51267 (ODPA_PORPU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 60. 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 alpha

EC=1.2.4.1
Gene names
Name:pdhA
Synonyms:odpA
Encoded onPlastid; Chloroplast
OrganismPorphyra purpurea (Red seaweed)
Taxonomic identifier2787 [NCBI]
Taxonomic lineageEukaryotaRhodophytaBangiophyceaeBangialesBangiaceaePorphyra

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Catalytic activity

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

Cofactor

Thiamine pyrophosphate.

Subunit structure

Heterodimer of an alpha and a beta chain By similarity.

Subcellular location

Plastidchloroplast.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentChloroplast
Plastid
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchloroplast

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

Chain1 – 344344Pyruvate dehydrogenase E1 component subunit alpha
PRO_0000162215

Sequences

Sequence LengthMass (Da)Tools
P51267 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 799BD9AFA06FF455

FASTA34438,507
        10         20         30         40         50         60 
MSYPKKVELP LTNCNQINLT KHKLLVLYED MLLGRNFEDM CAQMYYKGKM FGFVHLYNGQ 

        70         80         90        100        110        120 
EAVSTGVIKL LDSKDYVCST YRDHVHALSK GVPSQNVMAE LFGKETGCSR GRGGSMHIFS 

       130        140        150        160        170        180 
APHNFLGGFA FIAEGIPVAT GAAFQSIYRQ QVLKEPGELR VTACFFGDGT TNNGQFFECL 

       190        200        210        220        230        240 
NMAVLWKLPI IFVVENNQWA IGMAHHRSSS IPEIHKKAEA FGLPGIEVDG MDVLAVRQVA 

       250        260        270        280        290        300 
EKAVERARQG QGPTLIEALT YRFRGHSLAD PDELRSRQEK EAWVARDPIK KLKKHILDNQ 

       310        320        330        340 
IASSDELNDI QSSVKIDLEQ SVEFAMSSPE PNISELKRYL FADN 

« Hide

References

[1]"Complete nucleotide sequence of the Porphyra purpurea chloroplast genome."
Reith M.E., Munholland J.
Plant Mol. Biol. Rep. 13:333-335(1995)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Avonport.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38804 Genomic DNA. Translation: AAC08153.1.
PIRS73188.
RefSeqNP_053877.1. NC_000925.1.

3D structure databases

ProteinModelPortalP51267.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID809896.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_PORPU
AccessionPrimary (citable) accession number: P51267
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)