ID   ODPB_ACHLA              Reviewed;         327 AA.
AC   P35488;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   04-NOV-2008, entry version 46.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB;
OS   Acholeplasma laidlawii.
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=2148;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=92138635; PubMed=1735725;
RA   Wallbrandt P., Tegman V., Jonsson B.-H., Wieslander A.;
RT   "Identification and analysis of the genes coding for the putative
RT   pyruvate dehydrogenase enzyme complex in Acholeplasma laidlawii.";
RL   J. Bacteriol. 174:1388-1396(1992).
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: Heterodimer of an alpha and a beta chain.
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DR   EMBL; M81753; AAA21908.1; -; Genomic_DNA.
DR   PIR; B42653; B42653.
DR   HSSP; Q8ZUR7; 1IK6.
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; IPR005475; Transketo_Cen_R.
DR   InterPro; IPR015941; Transketolase_C-like.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    327       Pyruvate dehydrogenase E1 component
FT                                subunit beta.
FT                                /FTId=PRO_0000162220.
FT   BINDING      60     60       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   327 AA;  35682 MW;  F71D6DE807CDBE1C CRC64;
     MAIITLLEAI NQAIDQAMEK DESIVVFGED AGFEGGVFRV TAGLQKKYGE TRVFDTPIAE
     SAIVGSAVGM AINGLKPIAE IQFDGFIFPG YTDLVTHAAR MRNRSRGQFT VPMVLRLPHG
     GGIRALEHHS EALEVLFGSI PGLKVVTPST PYDAKGLLLA AINDPDPVVF LEPKRIYRAG
     KQEVPAEMYE IPIGKAKVVK QGTDMTVVAW GSIVREVEKA VKLVEAEGIS VEIIDLRTIS
     PIDEETILNS VKKTGKFMVV TEAVKSYGPA AELITMVNEK AFFHLEAAPV RFTGFDITVP
     LARGEHYHFP QPEKIAAYIR KLAKARP
//