ID ODPB_CHAVU Reviewed; 326 AA. AC Q1ACL0; DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 16-JUN-2009, entry version 20. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta; DE EC=1.2.4.1; GN Name=pdhB; Synonyms=odpB; OS Chara vulgaris (Common stonewort). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; OC Characeae; Chara. OX NCBI_TaxID=55564; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16611644; DOI=10.1093/molbev/msk018; RA Turmel M., Otis C., Lemieux C.; RT "The chloroplast genome sequence of Chara vulgaris sheds new light RT into the closest green algal relatives of land plants."; RL Mol. Biol. Evol. 23:1324-1338(2006). 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). 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; DQ229107; ABA61922.1; -; Genomic_DNA. DR RefSeq; YP_635737.1; -. DR GeneID; 4100209; -. DR BRENDA; 1.2.4.1; 292055. 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 1 326 Pyruvate dehydrogenase E1 component FT subunit beta. FT /FTId=PRO_0000280102. FT BINDING 60 60 Thiamine pyrophosphate (By similarity). SQ SEQUENCE 326 AA; 36005 MW; DF4773E0A838D07A CRC64; MSEKLLYEAL NEGIHEEIER DPKVFVIGED IGHYGGSYKV TKGLFEKYGN LRILDTPIAE NSFTGIAIGA AMTGLRPIIE GMNMGFLLLA FNQIANNAGM LHYTSGGNFT TPLVVRGPGG VGRQLGAEHS QRLESYFQSV PGLQMVACST PYNAKGLIKS AIRSQNPIIF FEHVLLYNIK ENIPQKEYLV PLEKAELVRS GNQITILTYS RMRYHVLQAA KTLIEKGYDP EIIDIISLKP LDMGTISTSL RKTHKVLIVE ECMKTGGIGT TLKSAILESL FDFLDTPIMS LSSQDVPTPY NGFLEDLTVI QPSQIVEAAE KIILYS //