ID   ODPB_PORPU              Reviewed;         331 AA.
AC   P51266;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 97.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; Synonyms=odpB;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RX   DOI=10.1007/BF02669187;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H(+) = N(6)-
CC         [(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10478,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         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|UniProtKB:P11177};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
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DR   EMBL; U38804; AAC08152.1; -; Genomic_DNA.
DR   PIR; S73187; S73187.
DR   RefSeq; NP_053876.1; NC_000925.1.
DR   AlphaFoldDB; P51266; -.
DR   SMR; P51266; -.
DR   GeneID; 809895; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   FunFam; 3.40.50.920:FF:000001; Pyruvate dehydrogenase E1 beta subunit; 1.
DR   FunFam; 3.40.50.970:FF:000001; Pyruvate dehydrogenase E1 beta subunit; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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   NCBIfam; NF006667; PRK09212.1; 1.
DR   PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR   PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Metal-binding; Oxidoreductase; Plastid; Potassium; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN           1..331
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta"
FT                   /id="PRO_0000162219"
FT   BINDING         60
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /ligand_note="ligand shared with alpha subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         113
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         161
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         162
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         164
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         166
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
SQ   SEQUENCE   331 AA;  36394 MW;  12D1B9467D4DC993 CRC64;
     MSKVFMFDAL RAATDEEMEK DLTVCVIGED VGHYGGSYKV TKDLHSKYGD LRVLDTPIAE
     NSFTGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM LRYTSGGNFT LPLVIRGPGG
     VGRQLGAEHS QRLEAYFQAI PGLKIVACST PYNAKGLLKS AIRDNNPVVF FEHVLLYNLQ
     EEIPEDEYLI PLDKAEVVRK GKDITILTYS RMRHHVTEAL PLLLNDGYDP EVLDLISLKP
     LDIDSISVSV KKTHRVLIVE ECMKTAGIGA ELIAQINEHL FDELDAPVVR LSSQDIPTPY
     NGSLEQATVI QPHQIIDAVK NIVNSSKTIT T
//