ID   ODPB_PEA                Reviewed;         359 AA.
AC   P52904;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   02-SEP-2026, entry version 119.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Lathyrus.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Luethy M.H., Miernyk J.A., Randall D.D.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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).
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: Tetramer of 2 alpha and 2 beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; U56697; AAB01223.1; -; mRNA.
DR   PIR; T06532; T06532.
DR   AlphaFoldDB; P52904; -.
DR   SMR; P52904; -.
DR   IntAct; P52904; 1.
DR   BindingDB; P52904; -.
DR   ChEMBL; CHEMBL2366570; -.
DR   ChEMBL; CHEMBL2366571; -.
DR   BRENDA; 1.2.1.104; 4872.
DR   SABIO-RK; P52904; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006086; P:pyruvate decarboxylation to acetyl-CoA; IEA:InterPro.
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:000006; Pyruvate dehydrogenase E1 component subunit beta; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR027110; PDHB_mito-type.
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   NCBIfam; NF008854; PRK11892.1; 1.
DR   PANTHER; PTHR11624; DEHYDROGENASE RELATED; 1.
DR   PANTHER; PTHR11624:SF112; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA-1, MITOCHONDRIAL; 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   2: Evidence at transcript level;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Potassium; Pyruvate;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..19
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..359
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000020463"
FT   BINDING         82
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         135
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         183
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         184
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
FT   BINDING         186
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P11177"
SQ   SEQUENCE   359 AA;  38793 MW;  5AFE49F165C13C83 CRC64;
     MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG EEVGEYQGAY
     KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV VEFMTFNFSM QAIDHIINSA
     AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ HSHCYASWYG SCPGLKVLVP HSAEDARGLL
     KAAIRDPDPV VFLENELLYG ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG
     FALKAAEILE KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT
     SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH RSVPLAAAA
//