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 24-JAN-2024, entry version 167. 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=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)- CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue CC acetyltransferase]; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSRNOP00000075450; -. DR CarbonylDB; P49432; -. DR GlyGen; P49432; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P49432; -. DR PhosphoSitePlus; P49432; -. DR jPOST; P49432; -. DR PaxDb; 10116-ENSRNOP00000010545; -. DR Ensembl; ENSRNOT00055023148; ENSRNOP00055018787; ENSRNOG00055013498. DR Ensembl; ENSRNOT00060035467; ENSRNOP00060029151; ENSRNOG00060020329. DR Ensembl; ENSRNOT00065013621; ENSRNOP00065010121; ENSRNOG00065008560. DR GeneID; 289950; -. DR KEGG; rno:289950; -. DR AGR; RGD:1359146; -. 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; 5473567at2759; -. 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 cell types or tissues. DR ExpressionAtlas; P49432; baseline and differential. DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISO: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 CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 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; DEHYDROGENASE RELATED; 1. DR PANTHER; PTHR11624:SF96; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA, MITOCHONDRIAL; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1. DR SUPFAM; SSF52922; TK C-terminal domain-like; 1. DR UCD-2DPAGE; P49432; -. DR World-2DPAGE; 0004:P49432; -. DR Genevisible; P49432; RN. 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 //