ID   ODPB_ASCSU              Reviewed;         361 AA.
AC   P26269;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-42.
RX   PubMed=2052042; DOI=10.1016/0166-6851(91)90022-x;
RA   Wheelock M.J., Komuniecki R., Duran E., Johnson K.R.;
RT   "Characterization of cDNA clones for the beta subunit of pyruvate
RT   dehydrogenase from Ascaris suum.";
RL   Mol. Biochem. Parasitol. 45:9-17(1991).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the
CC       glycolytic pathway to the tricarboxylic cycle.
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   -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The
CC       heterotetramer interacts with DLAT, and is part of the multimeric
CC       pyruvate dehydrogenase complex that contains multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT,
CC       E2) and lipoamide dehydrogenase (DLD, E3) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; M38017; AAA29379.1; -; mRNA.
DR   AlphaFoldDB; P26269; -.
DR   SMR; P26269; -.
DR   PRIDE; P26269; -.
DR   BioCyc; MetaCyc:MON-18300; -.
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:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; 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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glucose metabolism;
KW   Mitochondrion; Oxidoreductase; Pyruvate; Thiamine pyrophosphate;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:2052042"
FT   CHAIN           28..361
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000020456"
FT   BINDING         90
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   361 AA;  39136 MW;  F04D1C379C28196B CRC64;
     MAVNGCMRLL RNGLTSACAL EQSVRRLASG TLNVTVRDAL NAALDEEIKR DDRVFLIGEE
     VAQYDGAYKI SKGLWKKYGD GRIWDTPITE MAIAGLSVGA AMNGLRPICE FMSMNFSMQG
     IDHIINSAAK AHYMSAGRFH VPIVFRGANG AAVGVAQQHS QDFTAWFMHC PGVKVVVPYD
     CEDARGLLKA AVRDDNPVIC LENEILYGMK FPVSPEAQSP DFVLPFGQAK IQRPGKDITI
     VSLSIGVDVS LHAADELAKS GIDCEVINLR CVRPLDFQTV KDSVIKTKHL VTVESGWPNC
     GVGAEISARV TESDAFGYLD GPILRVTGVD VPMPYAQPLE TAALPQPADV VKMVKKCLNV
     Q