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   16-JUN-2009, entry version 69.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   Name=pdb1; ORFNames=SPBC30D10.13c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=95129904; 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
RT   beta subunit of Schizosaccharomyces pombe.";
RL   Gene 152:117-120(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate.
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; -.
DR   HSSP; P11177; 1NI4.
DR   GeneID; 2540273; -.
DR   KEGG; spo:SPBC30D10.13c; -.
DR   NMPDR; fig|4896.1.peg.2138; -.
DR   GeneDB_Spombe; SPBC30D10.13c; -.
DR   OMA; Q09171; QDYAAWY.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004295-MON; -.
DR   BRENDA; 1.2.4.1; 653.
DR   ArrayExpress; Q09171; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR005476; Transketo_C.
DR   InterPro; IPR015941; Transketolase_C-like.
DR   InterPro; IPR005475; Transketolase_central-reg.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Pyruvate; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    366       Pyruvate dehydrogenase E1 component
FT                                subunit beta, mitochondrial.
FT                                /FTId=PRO_0000020460.
FT   BINDING      94     94       Thiamine pyrophosphate (By similarity).
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
//