ID   ODPB_CHLAT              Reviewed;         335 AA.
AC   A2CI50;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; Synonyms=odpB;
OS   Chlorokybus atmophyticus (Soil alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales;
OC   Chlorokybaceae; Chlorokybus.
OX   NCBI_TaxID=3144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.80;
RX   PubMed=17222354; DOI=10.1186/1741-7007-5-2;
RA   Lemieux C., Otis C., Turmel M.;
RT   "A clade uniting the green algae Mesostigma viride and Chlorokybus
RT   atmophyticus represents the deepest branch of the Streptophyta in
RT   chloroplast genome-based phylogenies.";
RL   BMC Biol. 5:2-2(2007).
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; DQ422812; ABM87959.1; -; Genomic_DNA.
DR   RefSeq; YP_001019115.1; NC_008822.1.
DR   AlphaFoldDB; A2CI50; -.
DR   SMR; A2CI50; -.
DR   GeneID; 4783272; -.
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..335
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000280103"
FT   BINDING         60
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   335 AA;  36680 MW;  E846941B42AF42AF CRC64;
     MAVRFLFEAL QKAIDEEMER EKRVVLIGED IGHYGGSYKV TQGLYGKYGK HRVIDTPIAE
     YSFVGAAVGA AATGLIPVVE GMNMAFILLA YSQISNNMGM LCATSGGHFQ VPMVLRGPGG
     IGKQLGAEHS QRLESYFQSV PGLQIVTCST PYNAKGLLKS AIRSKNPILF IEHVLLYNLK
     GEVPDNDYLL PLEKAELVRE GSDITVLTYS RQRYNVIQAV KVLVEEGYDP EVIDLISLKP
     FDMETIGKSI QKTHKVLIVE ECMMTGGISN VLQSLIIDNF FDALDAAPLI LSSPNVPTPY
     TGPLEEATVV QTIDIIESIE YGITGKPPKP RTAKK