ID   ODPB_PEA                Reviewed;         359 AA.
AC   P52904;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-MAY-2009, entry version 60.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Fabales; Fabaceae; Papilionoideae; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Luethy M.H., Miernyk J.A., Randall D.D.;
RL   Submitted (MAY-1996) 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).
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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DR   EMBL; U56697; AAB01223.1; -; mRNA.
DR   PIR; T06532; T06532.
DR   HSSP; P11177; 1NI4.
DR   IntAct; P52904; 1.
DR   BRENDA; 1.2.4.1; 287.
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; 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   2: Evidence at transcript level;
KW   Glycolysis; Mitochondrion; Oxidoreductase; Pyruvate;
KW   Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     19       Mitochondrion (By similarity).
FT   CHAIN        20    359       Pyruvate dehydrogenase E1 component
FT                                subunit beta, mitochondrial.
FT                                /FTId=PRO_0000020463.
FT   BINDING      82     82       Thiamine pyrophosphate (By similarity).
SQ   SEQUENCE   359 AA;  38793 MW;  5AFE49F165C13C83 CRC64;
     MLGVIRNKTI RPSFSAFRFF SSAKQMTVRD ALNSALDVEM SADSKVFLMG EEVGEYQGAY
     KVTKGLLEKY GPERVLDTPI TEAGFTGIGV GAAYYGLKPV VEFMTFNFSM QAIDHIINSA
     AKSNYMSAGQ ISVPIVFRGL NGDAAGVGAQ HSHCYASWYG SCPGLKVLVP HSAEDARGLL
     KAAIRDPDPV VFLENELLYG ESFPVSAEVL DSSFWLPIGK AKIEREGKDV TITAFSKMVG
     FALKAAEILE KEGISAEVIN LRSIRPLDRP TINASVRKTN RLVTVEEGFP QHGVGAEICT
     SVIEESFGYL DATVERIGGA DVPMPYAGNL ERLVVPHVED IVRAAKRACH RSVPLAAAA
//