ODPB_MOUSE
ID ODPB_MOUSE Reviewed; 359 AA.
AC Q9D051; Q3TL86; Q505N8; Q99LW9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Liver, and Mammary tumor;
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 309-324, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-354, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02188.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK011810; BAB27855.1; -; mRNA.
DR EMBL; AK153058; BAE31684.1; -; mRNA.
DR EMBL; AK166631; BAE38906.1; -; mRNA.
DR EMBL; BC002188; AAH02188.1; ALT_INIT; mRNA.
DR EMBL; BC019512; AAH19512.1; -; mRNA.
DR EMBL; BC094468; AAH94468.1; -; mRNA.
DR CCDS; CCDS36800.1; -.
DR PIR; PT0096; PT0096.
DR RefSeq; NP_077183.1; NM_024221.3.
DR AlphaFoldDB; Q9D051; -.
DR SMR; Q9D051; -.
DR BioGRID; 212768; 52.
DR ComplexPortal; CPX-377; Pyruvate dehydrogenase E1 heterotetramer.
DR IntAct; Q9D051; 19.
DR MINT; Q9D051; -.
DR STRING; 10090.ENSMUSP00000022268; -.
DR iPTMnet; Q9D051; -.
DR PhosphoSitePlus; Q9D051; -.
DR SwissPalm; Q9D051; -.
DR REPRODUCTION-2DPAGE; Q9D051; -.
DR UCD-2DPAGE; Q9D051; -.
DR EPD; Q9D051; -.
DR jPOST; Q9D051; -.
DR MaxQB; Q9D051; -.
DR PaxDb; Q9D051; -.
DR PeptideAtlas; Q9D051; -.
DR PRIDE; Q9D051; -.
DR ProteomicsDB; 293496; -.
DR Antibodypedia; 31652; 240 antibodies from 34 providers.
DR DNASU; 68263; -.
DR Ensembl; ENSMUST00000022268; ENSMUSP00000022268; ENSMUSG00000021748.
DR GeneID; 68263; -.
DR KEGG; mmu:68263; -.
DR UCSC; uc007sev.1; mouse.
DR CTD; 5162; -.
DR MGI; MGI:1915513; Pdhb.
DR VEuPathDB; HostDB:ENSMUSG00000021748; -.
DR eggNOG; KOG0524; Eukaryota.
DR GeneTree; ENSGT00940000155146; -.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; Q9D051; -.
DR OMA; SRMRHHC; -.
DR OrthoDB; 875272at2759; -.
DR PhylomeDB; Q9D051; -.
DR TreeFam; TF105674; -.
DR BRENDA; 1.2.1.104; 3474.
DR Reactome; R-MMU-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR Reactome; R-MMU-70268; Pyruvate metabolism.
DR BioGRID-ORCS; 68263; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Pdhb; mouse.
DR PRO; PR:Q9D051; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9D051; protein.
DR Bgee; ENSMUSG00000021748; Expressed in spermatocyte and 248 other tissues.
DR Genevisible; Q9D051; MM.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; ISS:UniProtKB.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; ISS:UniProtKB.
DR GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; ISO:MGI.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; ISO:MGI.
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:0000250"
FT CHAIN 31..359
FT /note="Pyruvate dehydrogenase E1 component subunit beta,
FT mitochondrial"
FT /id="PRO_0000020458"
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:0007744|PubMed:18034455"
FT MOD_RES 354
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 237
FT /note="I -> M (in Ref. 1; BAE38906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 38937 MW; F5CD2A186DF58DDE CRC64;
MAVVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD EKVFLLGEEV
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
DQVINSAAKT YYMSAGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS
EDAKGLIKSA IRDNNPVVML ENELMYGVAF ELPAEAQSKD FLIPIGKAKI ERQGTHITVV
AHSRPVGHCL EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKVLED NSVPQVKDII FAVKKTLNI
