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Reviewed, UniProtKB/Swiss-Prot P51267 (ODPA_PORPU)

Last modified November 4, 2008. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information

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
Taxonomic identifier2787 [NCBI]
Taxonomic lineageEukaryotaRhodophytaBangiophyceaeBangialesBangiaceaePorphyra

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). 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 + CO(2).

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 processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: 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
P51267-1 [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

U38804 Genomic DNA. Translation: AAC08153.1.
PIRS73188.
RefSeqNP_053877.1.

3D structure databases

HSSPHSSP built from PDB template 1NI4 based on UniProtKB P08559.
ModBaseSearch...

Genome annotation databases

GeneID809896.

Family and domain databases

InterProIPR001017. DHase_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
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: November 4, 2008
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information