ID   P79932_XENLA            Unreviewed;       339 AA.
AC   P79932;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   04-NOV-2026, entry version 83.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|RuleBase:RU364074};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU364074};
DE   Flags: Fragment;
GN   Name=PdhE1beta-2 {ECO:0000313|EMBL:AAC60044.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAC60044.1};
RN   [1] {ECO:0000313|EMBL:AAC60044.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8918224; DOI=10.1016/0378-1119(96)00199-0;
RA   Islam N., Poitras L., Gagnon F., Moss T.;
RT   "Antisense and sense poly(A)-RNAs from the Xenopus laevis pyruvate
RT   dehydrogenase gene loci are regulated with message production during
RT   embryogenesis.";
RL   Gene 176:9-16(1996).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO2.
CC       {ECO:0000256|RuleBase:RU364074}.
CC   -!- FUNCTION: Together with PDHA1 forms the heterotetrameric E1 subunit of
CC       the pyruvate dehydrogenase (PDH) complex. The PDH complex catalyzes the
CC       overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby
CC       links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid
CC       (TCA) cycle. It contains multiple copies of three enzymatic components:
CC       pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2)
CC       and dihydrolipoamide dehydrogenase (E3). The E1 subunit catalyzes both
CC       the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvate
CC       and the reductive acetylation of a lipoyl group covalently linked to
CC       the lipoyl-bearing domains of E2. {ECO:0000256|ARBA:ARBA00094116}.
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         Evidence={ECO:0000256|ARBA:ARBA00094031};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19190;
CC         Evidence={ECO:0000256|ARBA:ARBA00094031};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|RuleBase:RU364074};
CC   -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The
CC       heterotetramer interacts with DLAT, and is part of the multimeric
CC       pyruvate dehydrogenase (PDH) complex that contains multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT,
CC       E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to
CC       an inner core composed of about 48 DLAT and 12 PDHX molecules.
CC       Interacts with DLAT. {ECO:0000256|ARBA:ARBA00094772}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U39669; AAC60044.1; -; mRNA.
DR   PIR; JC5089; JC5089.
DR   AlphaFoldDB; P79932; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
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:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, 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   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Glucose metabolism {ECO:0000256|ARBA:ARBA00022526};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU364074}; Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU364074};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU364074};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          12..187
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAC60044.1"
SQ   SEQUENCE   339 AA;  36924 MW;  A43A0BC57082EC91 CRC64;
     SFHRSGPAAL QVTVRDALNQ AMDEEIERDE RVFLLGEEVA QYDGAYKISR GLWKKYGDKR
     VMDTPITEMG FAGIAVGAAM AGLRPICEFM TFNFSMQAID QVINSAAKTH YMSGGLVSVP
     IVFRGPNGAS AGVAAQHSQC FAAWYGHCPG LKVVSPWNAE DAKGLLKASI RDDNPVVFLE
     NELMYGVPFE LSEEVQSKDF VVPIGKAKIE RPGSQITLVS HSRSVGHCLE AASVLEKEGI
     DCEVINMRTI RPMDTETIEA SVVKTNHLVT VEGGWPQFGV GAEICANIME GPAFNYLDAP
     VVRVTGTDVP MPYAKILEEN CVPQVKDIIF AVKKTLNVL
//