ID   ODPB_RAT                Reviewed;         359 AA.
AC   P49432; Q6AY95;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 74.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE            Short=PDHE1-B;
DE            EC=1.2.4.1;
DE   Flags: Precursor;
GN   Name=Pdhb;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91223087; PubMed=2025639; DOI=10.1016/0167-4781(91)90076-X;
RA   Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T.;
RT   "The alpha-ketoacid dehydrogenase complexes. Sequence similarity of
RT   rat pyruvate dehydrogenase with Escherichia coli and Azotobacter
RT   vinelandii alpha-ketoglutarate dehydrogenase.";
RL   Biochim. Biophys. Acta 1089:1-7(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 31-38.
RC   TISSUE=Heart;
RA   Dunn M.J.;
RL   Submitted (MAR-1996) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 286-324, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W.;
RL   Submitted (APR-2007) 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).
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; BC079137; AAH79137.1; -; mRNA.
DR   IPI; IPI00194324; -.
DR   PIR; S15892; S15892.
DR   RefSeq; NP_001007621.1; -.
DR   UniGene; Rn.102424; -.
DR   HSSP; P11177; 1NI4.
DR   SMR; P49432; 30-359.
DR   PhosphoSite; P49432; -.
DR   HSC-2DPAGE; P49432; -.
DR   PRIDE; P49432; -.
DR   Ensembl; ENSRNOG00000007895; Rattus norvegicus.
DR   GeneID; 289950; -.
DR   KEGG; rno:289950; -.
DR   NMPDR; fig|10116.3.peg.11094; -.
DR   RGD; 1359146; Pdhb.
DR   HOVERGEN; P49432; -.
DR   OMA; P49432; AAKMHYM.
DR   BRENDA; 1.2.4.1; 248.
DR   NextBio; 630523; -.
DR   ArrayExpress; P49432; -.
DR   GermOnline; ENSRNOG00000007895; Rattus norvegicus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:RGD.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring...; IDA:RGD.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:RGD.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycolysis; Mitochondrion; Oxidoreductase;
KW   Phosphoprotein; Pyruvate; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     30       Mitochondrion.
FT   CHAIN        31    359       Pyruvate dehydrogenase E1 component
FT                                subunit beta, mitochondrial.
FT                                /FTId=PRO_0000020459.
FT   BINDING      89     89       Thiamine pyrophosphate (By similarity).
FT   MOD_RES      67     67       Phosphotyrosine (By similarity).
FT   CONFLICT      3      3       A -> G (in Ref. 1).
FT   CONFLICT     11     15       PLRQA -> LCGRL (in Ref. 1).
FT   CONFLICT     22     22       R -> L (in Ref. 1).
FT   CONFLICT     25     25       R -> C (in Ref. 1).
FT   CONFLICT    238    238       T -> N (in Ref. 1).
FT   CONFLICT    241    242       AH -> CY (in Ref. 1).
FT   CONFLICT    259    259       E -> G (in Ref. 1).
SQ   SEQUENCE   359 AA;  38982 MW;  1B942D0A68C86D51 CRC64;
     MAAVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD EKVFLLGEEV
     AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
     DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS
     EDAKGLIKSA IRDDNPVVML ENELMYGVAF ELPTEAQSKD FLIPIGKAKI ERQGTHITVV
     AHSRPVGHCL EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG
     VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI
//