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Reviewed, UniProtKB/Swiss-Prot Q6B8T1 (ODPB_GRATL)

Last modified June 16, 2009. Version 31. 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

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Names and origin

Protein namesRecommended name:
    Pyruvate dehydrogenase E1 component subunit beta
    EC=1.2.4.1
Gene names
Name: pdhB
Synonyms: odpB
Ordered Locus Names: Grc000123
Encoded onPlastid; Chloroplast
OrganismGracilaria tenuistipitata var. liui (Red alga)
Taxonomic identifier285951 [NCBI]
Taxonomic lineageEukaryota › Rhodophyta › Florideophyceae › Gracilariales › Gracilariaceae › Gracilaria

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Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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

Plastid › chloroplast.

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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-SubCell

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Pyruvate dehydrogenase E1 component subunit beta
PRO_0000280108

Sites

Binding site601Thiamine pyrophosphate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q6B8T1-1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: EF7821FA426BFEED

FASTA32335,742
        10         20         30         40         50         60 
MTEVLMFDAL REATDEEMQN DSSVFILGED VGHYGGSYKV TKDLHSKYGD LRVLDTPIAE 

        70         80         90        100        110        120 
NSFMGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM LRYTSGGNFQ IPIVIRGPGG 

       130        140        150        160        170        180 
VGRQLGAEHS QRLEAYFQAI PGLKIVACST PYNAKGLLKS AIRDNNPVIF FEHVLLYNLK 

       190        200        210        220        230        240 
DELPNDEYFL PLDKAELVRD GLDVTILTYS RMRHHVMQAV VDLVNDGYNP EVIDLISLKP 

       250        260        270        280        290        300 
LDITSIAQSL MKTHKLIIVE ECMKTGGIGA EIIAQINDNY FDFLDAPIVR LSSQDIPTPY 

       310        320 
NGKLEKATVI YPQQIIEAVK SIV

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References

[1]"Comparative analysis of the complete plastid genome sequence of the red alga Gracilaria tenuistipitata var. liui provides insights into the evolution of rhodoplasts and their relationship to other plastids."
Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.
J. Mol. Evol. 59:464-477(2004) [PubMed: 15638458] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

AY673996 Genomic DNA. Translation: AAT79704.1.
RefSeqYP_063629.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2943994.

Enzyme and pathway databases

BRENDA1.2.4.1. 302087.

Family and domain databases

InterProIPR005476. Transketo_C.
IPR015941. Transketolase_C-like.
IPR005475. Transketolase_central-reg.
[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...

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Entry information

Entry nameODPB_GRATL
AccessionPrimary (citable) accession number: Q6B8T1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: September 13, 2004
Last modified: June 16, 2009
This is version 31 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