ODPB_RAT
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 03-AUG-2022, entry version 161.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX 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 rat
RT pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii
RT 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 project:
RT 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 IDENTIFICATION BY 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), and thereby links the
CC glycolytic pathway to the tricarboxylic cycle. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits. The
CC heterotetramer interacts with DLAT, and is part of the multimeric
CC pyruvate dehydrogenase complex that contains multiple copies of
CC pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT,
CC E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to
CC an inner core composed of about 48 DLAT and 12 PDHX molecules.
CC Interacts with DLAT. {ECO:0000250|UniProtKB:P11177}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
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DR EMBL; BC079137; AAH79137.1; -; mRNA.
DR PIR; S15892; S15892.
DR RefSeq; NP_001007621.1; NM_001007620.1.
DR RefSeq; XP_006251816.1; XM_006251754.1.
DR AlphaFoldDB; P49432; -.
DR SMR; P49432; -.
DR BioGRID; 253064; 4.
DR ComplexPortal; CPX-378; Pyruvate dehydrogenase E1 heterotetramer.
DR IntAct; P49432; 4.
DR MINT; P49432; -.
DR STRING; 10116.ENSRNOP00000010545; -.
DR CarbonylDB; P49432; -.
DR iPTMnet; P49432; -.
DR PhosphoSitePlus; P49432; -.
DR UCD-2DPAGE; P49432; -.
DR World-2DPAGE; 0004:P49432; -.
DR jPOST; P49432; -.
DR PaxDb; P49432; -.
DR PRIDE; P49432; -.
DR GeneID; 289950; -.
DR KEGG; rno:289950; -.
DR CTD; 5162; -.
DR RGD; 1359146; Pdhb.
DR VEuPathDB; HostDB:ENSRNOG00000007895; -.
DR eggNOG; KOG0524; Eukaryota.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; P49432; -.
DR OrthoDB; 875272at2759; -.
DR PhylomeDB; P49432; -.
DR TreeFam; TF105674; -.
DR Reactome; R-RNO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-RNO-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
DR Reactome; R-RNO-70268; Pyruvate metabolism.
DR PRO; PR:P49432; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000007895; Expressed in heart and 20 other tissues.
DR ExpressionAtlas; P49432; baseline and differential.
DR Genevisible; P49432; RN.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:RGD.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IDA:RGD.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:RGD.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR11624; PTHR11624; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW Acetylation; Carbohydrate metabolism; Direct protein sequencing;
KW Glucose metabolism; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW Pyruvate; Reference proteome; Thiamine pyrophosphate; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 31..359
FT /note="Pyruvate dehydrogenase E1 component subunit beta,
FT mitochondrial"
FT /id="PRO_0000020459"
FT BINDING 89
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT SITE 319
FT /note="Important for interaction with DLAT"
FT /evidence="ECO:0000250|UniProtKB:P11177"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D051"
FT MOD_RES 354
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D051"
FT CONFLICT 3
FT /note="A -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 11..15
FT /note="PLRQA -> LCGRL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="R -> L (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="R -> C (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="T -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 241..242
FT /note="AH -> CY (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="E -> G (in Ref. 1)"
FT /evidence="ECO:0000305"
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
