ID ODPB_MESVI Reviewed; 327 AA. AC Q9MUR4; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 04-NOV-2008, entry version 43. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta; DE EC=1.2.4.1; GN Name=pdhB; Synonyms=odpB; OS Mesostigma viride. OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Mesostigmatophyceae; OC Mesostigmatales; Mesostigmataceae; Mesostigma. OX NCBI_TaxID=41882; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIES-296; RX MEDLINE=20150907; PubMed=10688199; DOI=10.1038/35001059; RA Lemieux C., Otis C., Turmel M.; RT "Ancestral chloroplast genome in Mesostigma viride reveals an early RT branch of green plant evolution."; RL Nature 403:649-652(2000). 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; AF166114; AAF43837.1; -; Genomic_DNA. DR RefSeq; NP_038396.1; -. DR HSSP; Q8ZUR7; 1IK6. DR GeneID; 800962; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. 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 3: Inferred from homology; KW Chloroplast; Glycolysis; Oxidoreductase; Plastid; Pyruvate; KW Thiamine pyrophosphate. FT CHAIN 1 327 Pyruvate dehydrogenase E1 component FT subunit beta. FT /FTId=PRO_0000162218. FT BINDING 60 60 Thiamine pyrophosphate (By similarity). SQ SEQUENCE 327 AA; 36005 MW; 8E8D7CD1ADD64E5A CRC64; MTVRFLFEAL NMAIDEEMAR NDKVALLGED IGHYGGSYKV TQNLYAKYGE HRVIDTPIAE NSFVGAAIGA AMTGLVTVVE GMNMGFILLA FSQISNNMGM LSATSGGHYH IPIVLRGPGG VGKQLGAEHS QRLECYFQSV PGLQIVACST PYNAKGLLKS AIRSKNPIFF LEHVLLYNLK AEVPDNDYVL PLEKAEIVRQ GNDITILTYS RMRYNVIQAV KVLVEKGYDP EIIDLISLKP FDIETIGKSI QKTHKVLIVE ESMMTGGISN VLQSLILENF FDDLDNRPMC LSSPNVPTPY SGPLEEVSIV QTADIIESVE QILTNKM //