Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q1ACL0 (ODPB_CHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 35. 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

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.
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 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

   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 – 326326Pyruvate dehydrogenase E1 component subunit beta
PRO_0000280102

Sites

Binding site601Thiamine pyrophosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1ACL0 [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ229107 Genomic DNA. Translation: ABA61922.1.
RefSeqYP_635737.1. NC_008097.1.

3D structure databases

ProteinModelPortalQ1ACL0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4100209.

Phylogenomic databases

ProtClustDBCHL00144.

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...

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: October 16, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program