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Reviewed, UniProtKB/Swiss-Prot Q1ACL0 (ODPB_CHAVU)

Last modified November 4, 2008. Version 17. 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 beta
    EC=1.2.4.1
Gene names
Name: pdhB
Synonyms: odpB
Encoded onPlastid; Chloroplast
OrganismChara vulgaris (Common stonewort)
Taxonomic identifier55564 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaCharophyceaeCharalesCharaceaeChara

Protein attributes

Sequence length326 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 By similarity.

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 – 326326Pyruvate dehydrogenase E1 component subunit beta
PRO_0000280102

Sites

Binding site601Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1ACL0-1 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: DF4773E0A838D07A

FASTA32636,005
        10         20         30         40         50         60 
MSEKLLYEAL NEGIHEEIER DPKVFVIGED IGHYGGSYKV TKGLFEKYGN LRILDTPIAE 

        70         80         90        100        110        120 
NSFTGIAIGA AMTGLRPIIE GMNMGFLLLA FNQIANNAGM LHYTSGGNFT TPLVVRGPGG 

       130        140        150        160        170        180 
VGRQLGAEHS QRLESYFQSV PGLQMVACST PYNAKGLIKS AIRSQNPIIF FEHVLLYNIK 

       190        200        210        220        230        240 
ENIPQKEYLV PLEKAELVRS GNQITILTYS RMRYHVLQAA KTLIEKGYDP EIIDIISLKP 

       250        260        270        280        290        300 
LDMGTISTSL RKTHKVLIVE ECMKTGGIGT TLKSAILESL FDFLDTPIMS LSSQDVPTPY 

       310        320 
NGFLEDLTVI QPSQIVEAAE KIILYS 

« Hide

References

[1]"The chloroplast genome sequence of Chara vulgaris sheds new light into the closest green algal relatives of land plants."
Turmel M., Otis C., Lemieux C.
Mol. Biol. Evol. 23:1324-1338(2006) [PubMed: 16611644] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

DQ229107 Genomic DNA. Translation: ABA61922.1.
RefSeqYP_635737.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4100209.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR005475. Transketo_Cen_R.
IPR015941. Transketolase_C-like.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameODPB_CHAVU
AccessionPrimary (citable) accession number: Q1ACL0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: July 11, 2006
Last modified: November 4, 2008
This is version 17 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