ID   ODPB_CHAGL              Reviewed;         326 AA.
AC   Q8MA03;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 35.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; Synonyms=odpB;
OS   Chaetosphaeridium globosum.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae;
OC   Coleochaetales; Chaetosphaeridiaceae; Chaetosphaeridium.
OX   NCBI_TaxID=96477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1311;
RX   MEDLINE=22177139; PubMed=12161560; DOI=10.1073/pnas.162203299;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The chloroplast and mitochondrial genome sequences of the charophyte
RT   Chaetosphaeridium globosum: insights into the timing of the events
RT   that restructured organelle DNAs within the green algal lineage that
RT   led to land plants.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:11275-11280(2002).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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DR   EMBL; AF494278; AAM96525.1; -; Genomic_DNA.
DR   RefSeq; NP_683783.1; -.
DR   HSSP; Q8ZUR7; 1IK6.
DR   GeneID; 860807; -.
DR   BRENDA; 1.2.4.1; 312444.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005476; Transketo_C.
DR   InterPro; IPR015941; Transketolase_C-like.
DR   InterPro; IPR005475; Transketolase_central-reg.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    326       Pyruvate dehydrogenase E1 component
FT                                subunit beta.
FT                                /FTId=PRO_0000280101.
FT   BINDING      60     60       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   326 AA;  35969 MW;  9E99DFC6EBABDB3C CRC64;
     MAEVLLFEAL RDALDEEMQR DPSVLVMGED VGHYGGSYKV TKGFHEKYGD LRLLDTPIAE
     NSFTGMAIGA AMTGLRPIVE GMNMGFLLLA FNQIANNAGM LHYTSGGNFK IPIVIRGPGG
     VGRQLGAEHS QRLESYFQSV PGLQMVACST PYNGKGLLKS AIRNDNPVIF FEHVLLYNLN
     ENLIEQEYLL CLEKAEVVRP GNDITILTYS RMRHHVLQAA KVLVNKGYDP EIIDILSLKP
     LDMGTISLSV RKTHKVLIVE ECMRTGGIGA SLRAAILEDL FDYLDAPIQC LSSQDVPTPY
     SGPLEELTVI QPNQIIQAVE EMCKIE
//