ID   ODPB_SCHPO              Reviewed;         366 AA.
AC   Q09171;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1 {ECO:0000269|PubMed:7828917};
DE   Flags: Precursor;
GN   Name=pdb1; ORFNames=SPBC30D10.13c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=7828917; DOI=10.1016/0378-1119(94)00705-w;
RA   Cavan G., Macdonald D.;
RT   "Cloning and sequence of a gene encoding the pyruvate dehydrogenase E1 beta
RT   subunit of Schizosaccharomyces pombe.";
RL   Gene 152:117-120(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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=(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:7828917};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; X75648; CAA53303.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB10808.1; -; Genomic_DNA.
DR   PIR; JC4080; JC4080.
DR   RefSeq; NP_596272.1; NM_001022193.2.
DR   AlphaFoldDB; Q09171; -.
DR   SMR; Q09171; -.
DR   BioGRID; 276804; 9.
DR   STRING; 4896.SPBC30D10.13c.1; -.
DR   iPTMnet; Q09171; -.
DR   MaxQB; Q09171; -.
DR   PaxDb; Q09171; -.
DR   PRIDE; Q09171; -.
DR   EnsemblFungi; SPBC30D10.13c.1; SPBC30D10.13c.1:pep; SPBC30D10.13c.
DR   GeneID; 2540273; -.
DR   KEGG; spo:SPBC30D10.13c; -.
DR   PomBase; SPBC30D10.13c; pdb1.
DR   VEuPathDB; FungiDB:SPBC30D10.13c; -.
DR   eggNOG; KOG0524; Eukaryota.
DR   HOGENOM; CLU_012907_1_1_1; -.
DR   InParanoid; Q09171; -.
DR   OMA; SRMRHHC; -.
DR   PhylomeDB; Q09171; -.
DR   Reactome; R-SPO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR   Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-SPO-5362517; Signaling by Retinoic Acid.
DR   Reactome; R-SPO-70268; Pyruvate metabolism.
DR   PRO; PR:Q09171; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISS:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IMP:PomBase.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IMP:PomBase.
DR   GO; GO:0006096; P:glycolytic process; 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   Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..366
FT                   /note="Pyruvate dehydrogenase E1 component subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000020460"
FT   BINDING         94
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  39624 MW;  5835A6872F6EDC0A CRC64;
     MIRLQKFGEI VGTSRSWKLL SSTIAKRYSS SSNGVKEMTV RDALNSAMEE EMKRDDRVFL
     IGEEVAQYNG AYKISRGLLD KFGPKRVIDT PITEMGFTGL ATGAAFAGLR PICEFMTFNF
     SMQAIDHIVN SAARTLYMSG GIQACPIVFR GPNGPAAAVA AQHSQHFAPW YGSIPGLKVV
     SPYSAEDARG LLKAAIRDPN PVVVLENEIL YGKTFPISKE ALSEDFVLPF GLAKVERPGK
     DITIVGESIS VVTALEAADK LKADYGVEAE VINLRSIRPL DINTIAASVK KTNRIVTVDQ
     AYSQHGIGSE IAAQIMESDA FDYLDAPVER VSMADVPMPY SHPVEAASVP NADVVVAAAK
     KCLYIK