ID   ODPB_PORYE              Reviewed;         331 AA.
AC   Q1XDM1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta;
DE            EC=1.2.4.1;
GN   Name=pdhB; Synonyms=odpB;
OS   Porphyra yezoensis.
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U-51; TISSUE=Gametophyte;
RA   Kunimoto M., Morishima K., Yoshikawa M., Fukuda S., Kobayashi T.,
RA   Kobayashi M., Okazaki T., Ohara I., Nakayama I.;
RT   "Whole genome sequence of Porphyra yezoensis chloroplast.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AP006715; BAE92390.1; -; Genomic_DNA.
DR   RefSeq; YP_536947.1; -.
DR   GeneID; 3978894; -.
DR   BRENDA; 1.2.4.1; 257472.
DR   GO; GO:0009507; C:chloroplast; 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   3: Inferred from homology;
KW   Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    331       Pyruvate dehydrogenase E1 component
FT                                subunit beta.
FT                                /FTId=PRO_0000277254.
FT   BINDING      60     60       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   331 AA;  36385 MW;  8F8C892E9684F733 CRC64;
     MSKIFMFDAL RAATDEEMAK DPTVCVIGED VGHYGGSYKV TKDLHSKYGD LRVLDTPIAE
     NSFTGMAIGA AITGLRPIVE GMNMSFLLLA FNQISNNAGM LRYTSGGNFT LPLVIRGPGG
     VGRQLGAEHS QRLEAYFQAI PGLKIVACST PYNAKGLLKS AIRDNNPVVF FEHVLLYNLQ
     EEIPQEEYFL PLNKVEFVRK GKDITILTYS RMRHHVIQAL PALLKEGYDP EVIDLISLKP
     LDIDSISISV KKTHKVLIVE ECMKTAGIGA ELIAQINEYL FDELDAPVVR LSSQDIPTPY
     NGSLEQATVI QPSQIVDSVK SIITSVKAII T
//