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   03-AUG-2022, entry version 74.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; Synonyms=odpB;
OS   Chaetosphaeridium globosum (Charophycean green alga) (Herposteiron
OS   globosum).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC   Chaetosphaeridiaceae; Chaetosphaeridium.
OX   NCBI_TaxID=96477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1311;
RX   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 that
RT   restructured organelle DNAs within the green algal lineage that led to land
RT   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 multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC         acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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DR   EMBL; AF494278; AAM96525.1; -; Genomic_DNA.
DR   RefSeq; NP_683783.1; NC_004115.1.
DR   AlphaFoldDB; Q8MA03; -.
DR   SMR; Q8MA03; -.
DR   GeneID; 860807; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.920; -; 1.
DR   InterPro; IPR027110; PDHB.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR11624; PTHR11624; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..326
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000280101"
FT   BINDING         60
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
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