ID   ODPB_CAEEL              Reviewed;         352 AA.
AC   O44451;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   ORFNames=C04C3.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 130-137; 237-246 AND 262-272, AND MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (SEP-2005) to UniProtKB.
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: Tetramer of 2 alpha and 2 beta subunits (By similarity).
CC   -!- INTERACTION:
CC       O45924:-; NbExp=1; IntAct=EBI-326559, EBI-330432;
CC       Q9NGT3:mdf-2; NbExp=1; IntAct=EBI-326559, EBI-328699;
CC       Q09620:sdz-38; NbExp=1; IntAct=EBI-326559, EBI-332504;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
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DR   EMBL; AF038606; AAB92024.2; -; Genomic_DNA.
DR   PIR; T32598; T32598.
DR   RefSeq; NP_500340.1; -.
DR   UniGene; Cel.7275; -.
DR   HSSP; P11177; 1NI4.
DR   DIP; DIP:24348N; -.
DR   IntAct; O44451; 6.
DR   Ensembl; C04C3.3; Caenorhabditis elegans.
DR   GeneID; 177108; -.
DR   KEGG; cel:C04C3.3; -.
DR   WormBase; WBGene00015413; C04C3.3.
DR   WormPep; C04C3.3; CE27647.
DR   OMA; O44451; QDYAAWY.
DR   BRENDA; 1.2.4.1; 672.
DR   NextBio; 895372; -.
DR   ArrayExpress; O44451; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IEA:EC.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Glycolysis;
KW   Mitochondrion; Oxidoreductase; Pyruvate; Thiamine pyrophosphate;
KW   Transit peptide.
FT   TRANSIT       1     21       Mitochondrion (Potential).
FT   CHAIN        22    352       Pyruvate dehydrogenase E1 component
FT                                subunit beta, mitochondrial.
FT                                /FTId=PRO_0000042638.
FT   BINDING      81     81       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   352 AA;  38141 MW;  37F4A4A28C8ADECA CRC64;
     MALRKCGNLF VARLAGTSTR AASTMTVRDA LNQAMDEEIK RDDRVFLMGE EVAQYDGAYK
     ISKGLWKKHG DKRVVDTPIT EMGFAGIAVG AAFAGLRPIC EFMTFNFSMQ AIDQIINSAA
     KTYYMSAGRV PVPIVFRGPN GAAAGVAAQH SQDFSAWYAH CPGLKVVCPY SAEDAKGLLK
     AAIRDDNPVV FLENEILYGQ SFPVGDEVLS DDFVVPIGKA KIERAGDHVT IVSYSRGVEF
     SLEAAKQLEA IGVSAEVINL RSLRPFDFES IRQSVHKTHH LVSVETGWPF AGIGSEIAAQ
     VMESDVFDQL DAPLLRVTGV DVPMPYTQTL EAAALPTAEH VVKAVKKSLN IA
//