ID   ODPB_ASCSU              Reviewed;         361 AA.
AC   P26269;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   04-NOV-2008, entry version 54.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Ascaridida; Ascaridoidea;
OC   Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 28-42.
RX   MEDLINE=91270304; PubMed=2052042; DOI=10.1016/0166-6851(91)90022-X;
RA   Wheelock M.J., Komuniecki R., Duran E., Johnson K.R.;
RT   "Characterization of cDNA clones for the beta subunit of pyruvate
RT   dehydrogenase from Ascaris suum.";
RL   Mol. Biochem. Parasitol. 45:9-17(1991).
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: Tetramer of 2 alpha and 2 beta subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; M38017; AAA29379.1; -; mRNA.
DR   HSSP; P11177; 1NI4.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; 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; Mitochondrion; Oxidoreductase;
KW   Pyruvate; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     27       Mitochondrion.
FT   CHAIN        28    361       Pyruvate dehydrogenase E1 component
FT                                subunit beta, mitochondrial.
FT                                /FTId=PRO_0000020456.
FT   BINDING      90     90       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   361 AA;  39136 MW;  F04D1C379C28196B CRC64;
     MAVNGCMRLL RNGLTSACAL EQSVRRLASG TLNVTVRDAL NAALDEEIKR DDRVFLIGEE
     VAQYDGAYKI SKGLWKKYGD GRIWDTPITE MAIAGLSVGA AMNGLRPICE FMSMNFSMQG
     IDHIINSAAK AHYMSAGRFH VPIVFRGANG AAVGVAQQHS QDFTAWFMHC PGVKVVVPYD
     CEDARGLLKA AVRDDNPVIC LENEILYGMK FPVSPEAQSP DFVLPFGQAK IQRPGKDITI
     VSLSIGVDVS LHAADELAKS GIDCEVINLR CVRPLDFQTV KDSVIKTKHL VTVESGWPNC
     GVGAEISARV TESDAFGYLD GPILRVTGVD VPMPYAQPLE TAALPQPADV VKMVKKCLNV
     Q
//