ID   ODPB_LEIXX              Reviewed;         337 AA.
AC   Q6ABX8;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; OrderedLocusNames=Lxx25060;
OS   Leifsonia xyli subsp. xyli.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Microbacteriaceae; Leifsonia.
OX   NCBI_TaxID=59736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A.,
RA   Kitajima J.P., Truffi D., do Amaral A.M., Harakava R.,
RA   de Oliveira J.C.F., Wood D., de Oliveira M.C., Miyaki C.Y.,
RA   Takita M.A., da Silva A.C.R., Furlan L.R., Carraro D.M., Camarotte G.,
RA   Almeida N.F. Jr., Carrer H., Coutinho L.L., El-Dorry H.A.,
RA   Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia
RT   xyli subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
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DR   EMBL; AE016822; AAT90114.1; -; Genomic_DNA.
DR   RefSeq; YP_063219.1; -.
DR   GeneID; 2940400; -.
DR   GenomeReviews; AE016822_GR; Lxx25060.
DR   KEGG; lxx:Lxx25060; -.
DR   NMPDR; fig|281090.3.peg.2006; -.
DR   HOGENOM; Q6ABX8; -.
DR   OMA; Q6ABX8; ARVEEHY.
DR   BioCyc; LXYL281090:LXX25060-MON; -.
DR   BRENDA; 1.2.4.1; 297084.
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   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    337       Pyruvate dehydrogenase E1 component
FT                                subunit beta.
FT                                /FTId=PRO_0000232457.
FT   BINDING      73     73       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   337 AA;  36087 MW;  2B45A895DC8D84E2 CRC64;
     MERAPALAEP EPRVQSLPMV KALNAGLRQA LVADPKVLIL GEDVGPLGGV FRVTEGLQSE
     FGASRVVDTP LAEAGIVGTA IGLAMRGYRP VVEIQFNGFV FPGFDQITTQ LAKMANRHSG
     AVSMPVVIRI PHGGHIGAVE HHQEAPEAYF AHTAGLRIVA PSTPHDAYWM IQEAIASDDP
     VIFFEPMSRY WPKGEVDTLE NPLPLHASRI VRSGTDATIV AWAGMVPVAL RAAEIAAEEG
     RSLEVVDLRS LAPIDYAPVL RSVQKTGRLV VAQEAPGIVS VGSEVAAVVG EKAFYSLEAP
     VLRVAGFDTP FPPAKLESLY LPDADRILEV VDRSLAY
//