ID   ODPB_CHATD              Reviewed;         382 AA.
AC   G0RYE0;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial {ECO:0000303|PubMed:33567276};
DE            EC=1.2.4.1 {ECO:0000269|PubMed:33567276, ECO:0000269|PubMed:34836937};
DE   AltName: Full=Pyruvate dehydrogenase complex component E1 beta {ECO:0000303|PubMed:33567276};
DE            Short=PDHE1-B {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=CTHT_0006350;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX   PubMed=33567276; DOI=10.1016/j.celrep.2021.108727;
RA   Kyrilis F.L., Semchonok D.A., Skalidis I., Tueting C., Hamdi F.,
RA   O'Reilly F.J., Rappsilber J., Kastritis P.L.;
RT   "Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase
RT   complex from native cell extracts.";
RL   Cell Rep. 34:108727-108727(2021).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=34836937; DOI=10.1038/s41467-021-27287-4;
RA   Tueting C., Kyrilis F.L., Mueller J., Sorokina M., Skalidis I., Hamdi F.,
RA   Sadian Y., Kastritis P.L.;
RT   "Cryo-EM snapshots of a native lysate provide structural insights into a
RT   metabolon-embedded transacetylase reaction.";
RL   Nat. Commun. 12:6933-6933(2021).
CC   -!- FUNCTION: The 10-megadalton pyruvate dehydrogenase complex contains
CC       multiple copies of three enzymatic components: pyruvate dehydrogenase
CC       (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide
CC       dehydrogenase (E3) and catalyzes the overall oxidative decarboxylation
CC       of pyruvate to form acetyl-CoA and CO(2) (PubMed:33567276,
CC       PubMed:34836937). Within the complex, pyruvate and thiamine
CC       pyrophosphate (TPP or vitamin B1) are bound by pyruvate dehydrogenase
CC       E1 subunits alpha and beta and pyruvate is decarboxylated leading to
CC       the 2-carbon hydrohyethyl bound to TPP. The E2 component contains
CC       covalently-bound lipoyl cofactors and transfers the hydroxyethyl group
CC       from TPP to an oxidized form of covalently bound lipoamide, and the
CC       resulting acetyl group is then transferred to free coenzyme A to form
CC       acetyl-CoA and reduced dihydrolipoamide-E2. Finally, the flavoprotein
CC       dihydrolipoamide dehydrogenase (E3) re-oxidizes the lipoyl group of
CC       dihydrolipoamide-E2 to form lipoamide-E2 and NADH. A fourth subunit,
CC       E3BP, is responsible for tethering E3 in proximity to the core, forming
CC       the entire metabolon (Probable). {ECO:0000269|PubMed:33567276,
CC       ECO:0000269|PubMed:34836937, ECO:0000305|PubMed:33567276}.
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         Evidence={ECO:0000269|PubMed:33567276, ECO:0000269|PubMed:34836937};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19190;
CC         Evidence={ECO:0000269|PubMed:33567276, ECO:0000269|PubMed:34836937};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P11177};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=148 uM for pyruvate {ECO:0000269|PubMed:34836937};
CC   -!- SUBUNIT: Eukaryotic pyruvate dehydrogenase (PDH) complexes are
CC       organized as a core consisting of the oligomeric dihydrolipoamide
CC       acetyl-transferase (E2), around which are arranged multiple copies of
CC       pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and
CC       protein X (E3BP) bound by non-covalent bonds (PubMed:33567276). The
CC       Chaetomium thermophilum PDH complex contains 60 E2 units, 12 E3BP
CC       units, about 20 E1 units, and 12 or more E3 units (PubMed:33567276).
CC       The units are organized in 1 E2 60-mer, 4 E3BP trimers, about 20 E1
CC       tetramers, and a maximum of 12 E3 dimers (PubMed:33567276). Pyruvate
CC       dehydrogenase (E1) is active as a tetramer of 2 alpha and 2 beta
CC       subunits (PubMed:33567276). The E3BP trimers are bound inside the
CC       icosahedral core with tetrahedral symmetry (PubMed:33567276).
CC       {ECO:0000269|PubMed:33567276}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
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DR   EMBL; GL988032; EGS23926.1; -; Genomic_DNA.
DR   RefSeq; XP_006691168.1; XM_006691105.1.
DR   STRING; 759272.G0RYE0; -.
DR   EnsemblFungi; EGS23926; EGS23926; CTHT_0006350.
DR   GeneID; 18254673; -.
DR   KEGG; cthr:CTHT_0006350; -.
DR   eggNOG; KOG0524; Eukaryota.
DR   HOGENOM; CLU_012907_1_1_1; -.
DR   OrthoDB; 875272at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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   Mitochondrion; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..382
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000456221"
SQ   SEQUENCE   382 AA;  41425 MW;  CA1995B8CF153A83 CRC64;
     MSRFLRPAFR LATTATRAST IRPTPSSLIT KAAAVPTTRL LQKRSYAAEA TGVKEYTVRE
     ALNEALAEEL ESNPKVFILG EEVAQYNGAY KVTKGLLDRF GEKRVIDTPI TEMGFAGLAV
     GAALAGLQPV CEFMTFNFAM QAIDHIVNSA AKTLYMSGGI QPCNITFRGP NGFAAGVAAQ
     HSQDYAAWYG SIPGLKVVSP WSAEDAKGLL KAAIRDPNPV VVLENELMYG VSFPMSEAAQ
     KDDFVLPFGK AKIERAGKDL TIVSLSRCVG QSLVAAENLK KKYGIEAEVI NLRSIKPLDV
     EAIVKSVKKT HRLLAVESGF PAFGVGAEIL ALTMEYAFDY LDTPAQRITG ADVPTPYAQK
     LEEMSFPTEQ LIEDYAAKML RV