ODBB_HUMAN
ID ODBB_HUMAN Reviewed; 392 AA.
AC P21953; Q5T2J3; Q9BQL0;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, mitochondrial;
DE EC=1.2.4.4;
DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE Short=BCKDE1B;
DE Short=BCKDH E1-beta;
DE Flags: Precursor;
GN Name=BCKDHB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2365818; DOI=10.1172/jci114690;
RA Matsuda I., Asaka J., Akaboshi I., Endo F., Mitsubuchi H., Nobukuni Y.;
RT "Maple syrup urine disease. Complete primary structure of the E1 beta
RT subunit of human branched chain alpha-ketoacid dehydrogenase complex
RT deduced from the nucleotide sequence and a gene analysis of patients with
RT this disease.";
RL J. Clin. Invest. 86:242-247(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8651316;
RA Chuang J.L., Cox R.P., Chuang D.T.;
RT "Maple syrup urine disease: the E1beta gene of human branched-chain alpha-
RT ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR
RT in one of the two E1beta mRNAs arises from intronic sequences.";
RL Am. J. Hum. Genet. 58:1373-1377(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 20-392 (ISOFORM 1).
RX PubMed=2335211; DOI=10.1016/0014-5793(90)80215-5;
RA Chuang J.L., Cox R.P., Chuang D.T.;
RT "Molecular cloning of the mature E1b-beta subunit of human branched-chain
RT alpha-keto acid dehydrogenase complex.";
RL FEBS Lett. 262:305-309(1990).
RN [9]
RP PROTEIN SEQUENCE OF 36-62.
RX PubMed=7918575; DOI=10.1016/0304-4165(94)90161-9;
RA Wynn R.M., Kochi H., Cox R.P., Chuang D.T.;
RT "Differential processing of human and rat E1 alpha precursors of the
RT branched-chain alpha-keto acid dehydrogenase complex caused by an N-
RT terminal proline in the rat sequence.";
RL Biochim. Biophys. Acta 1201:125-128(1994).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLN-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP VARIANT MSUD1B ARG-206.
RX PubMed=8161368; DOI=10.1016/0925-4439(93)90123-i;
RA Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y.,
RA Endo F., Matsuda I.;
RT "Heterogeneity of mutations in maple syrup urine disease (MSUD): screening
RT and identification of affected E1 alpha and E1 beta subunits of the
RT branched-chain alpha-keto-acid dehydrogenase multienzyme complex.";
RL Biochim. Biophys. Acta 1225:64-70(1993).
RN [15]
RP VARIANTS MSUD1B PRO-183 AND SER-278.
RX PubMed=11509994; DOI=10.1086/323677;
RA Edelmann L., Wasserstein M.P., Kornreich R., Sansaricq C., Snyderman S.E.,
RA Diaz G.A.;
RT "Maple syrup urine disease: identification and carrier-frequency
RT determination of a novel founder mutation in the Ashkenazi Jewish
RT population.";
RL Am. J. Hum. Genet. 69:863-868(2001).
RN [16]
RP VARIANTS MSUD1B HIS-170 AND ARG-346.
RX PubMed=22326532; DOI=10.1016/j.gene.2012.01.082;
RA Wang Y.P., Qi M.L., Li T.T., Zhao Y.J.;
RT "Two novel mutations in the BCKDHB gene (R170H, Q346R) cause the classic
RT form of maple syrup urine disease (MSUD).";
RL Gene 498:112-115(2012).
CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex catalyzes
CC the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It
CC contains multiple copies of three enzymatic components: branched-chain
CC alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and
CC lipoamide dehydrogenase (E3).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta chains.
CC -!- INTERACTION:
CC P21953; P12694: BCKDHA; NbExp=14; IntAct=EBI-1029067, EBI-1029053;
CC P21953-1; P12694-1: BCKDHA; NbExp=3; IntAct=EBI-15489569, EBI-15489562;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21953-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P21953-2; Sequence=VSP_056370, VSP_056371;
CC -!- DISEASE: Maple syrup urine disease 1B (MSUD1B) [MIM:248600]: A
CC metabolic disorder due to an enzyme defect in the catabolic pathway of
CC the branched-chain amino acids leucine, isoleucine, and valine.
CC Accumulation of these 3 amino acids and their corresponding keto acids
CC leads to encephalopathy and progressive neurodegeneration. Clinical
CC features include mental and physical retardation, feeding problems, and
CC a maple syrup odor to the urine. The keto acids of the branched-chain
CC amino acids are present in the urine. If untreated, maple syrup urine
CC disease can lead to seizures, coma, and death. The disease is often
CC classified by its pattern of signs and symptoms. The most common and
CC severe form of the disease is the classic type, which becomes apparent
CC soon after birth. Variant forms of the disorder become apparent later
CC in infancy or childhood and are typically milder, but they still
CC involve developmental delay and other medical problems if not treated.
CC {ECO:0000269|PubMed:11509994, ECO:0000269|PubMed:22326532,
CC ECO:0000269|PubMed:8161368}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; M55575; AAA51812.1; -; mRNA.
DR EMBL; D90391; BAA14389.1; -; Genomic_DNA.
DR EMBL; AK289977; BAF82666.1; -; mRNA.
DR EMBL; BT020063; AAV38866.1; -; mRNA.
DR EMBL; AL049696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48696.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48697.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48698.1; -; Genomic_DNA.
DR EMBL; BC034481; AAH34481.1; -; mRNA.
DR EMBL; BC040139; AAH40139.1; -; mRNA.
DR EMBL; U50708; AAB16763.1; -; mRNA.
DR EMBL; X52446; CAA36685.1; -; mRNA.
DR CCDS; CCDS4994.1; -. [P21953-1]
DR PIR; A37157; A37157.
DR RefSeq; NP_000047.1; NM_000056.4. [P21953-1]
DR RefSeq; NP_001305904.1; NM_001318975.1.
DR RefSeq; NP_898871.1; NM_183050.3. [P21953-1]
DR PDB; 1DTW; X-ray; 2.70 A; B=51-392.
DR PDB; 1OLS; X-ray; 1.85 A; B=51-392.
DR PDB; 1OLU; X-ray; 1.90 A; B=51-392.
DR PDB; 1OLX; X-ray; 2.25 A; B=51-392.
DR PDB; 1U5B; X-ray; 1.83 A; B=51-392.
DR PDB; 1V11; X-ray; 1.95 A; B=51-392.
DR PDB; 1V16; X-ray; 1.90 A; B=51-392.
DR PDB; 1V1M; X-ray; 2.00 A; B=51-392.
DR PDB; 1V1R; X-ray; 1.80 A; B=51-392.
DR PDB; 1WCI; X-ray; 1.84 A; B=51-392.
DR PDB; 1X7W; X-ray; 1.73 A; B=51-392.
DR PDB; 1X7X; X-ray; 2.10 A; B=51-392.
DR PDB; 1X7Y; X-ray; 1.57 A; B=51-392.
DR PDB; 1X7Z; X-ray; 1.72 A; B=51-392.
DR PDB; 1X80; X-ray; 2.00 A; B=51-392.
DR PDB; 2BEU; X-ray; 1.89 A; B=51-392.
DR PDB; 2BEV; X-ray; 1.80 A; B=51-392.
DR PDB; 2BEW; X-ray; 1.79 A; B=51-392.
DR PDB; 2BFB; X-ray; 1.77 A; B=51-392.
DR PDB; 2BFC; X-ray; 1.64 A; B=51-392.
DR PDB; 2BFD; X-ray; 1.39 A; B=51-392.
DR PDB; 2BFE; X-ray; 1.69 A; B=51-392.
DR PDB; 2BFF; X-ray; 1.46 A; B=51-392.
DR PDB; 2J9F; X-ray; 1.88 A; B/D=51-392.
DR PDBsum; 1DTW; -.
DR PDBsum; 1OLS; -.
DR PDBsum; 1OLU; -.
DR PDBsum; 1OLX; -.
DR PDBsum; 1U5B; -.
DR PDBsum; 1V11; -.
DR PDBsum; 1V16; -.
DR PDBsum; 1V1M; -.
DR PDBsum; 1V1R; -.
DR PDBsum; 1WCI; -.
DR PDBsum; 1X7W; -.
DR PDBsum; 1X7X; -.
DR PDBsum; 1X7Y; -.
DR PDBsum; 1X7Z; -.
DR PDBsum; 1X80; -.
DR PDBsum; 2BEU; -.
DR PDBsum; 2BEV; -.
DR PDBsum; 2BEW; -.
DR PDBsum; 2BFB; -.
DR PDBsum; 2BFC; -.
DR PDBsum; 2BFD; -.
DR PDBsum; 2BFE; -.
DR PDBsum; 2BFF; -.
DR PDBsum; 2J9F; -.
DR AlphaFoldDB; P21953; -.
DR SMR; P21953; -.
DR BioGRID; 107066; 73.
DR ComplexPortal; CPX-2216; Mitochondrial 2-oxoisovalerate dehydrogenase complex.
DR DIP; DIP-6147N; -.
DR IntAct; P21953; 20.
DR MINT; P21953; -.
DR STRING; 9606.ENSP00000318351; -.
DR GlyGen; P21953; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P21953; -.
DR PhosphoSitePlus; P21953; -.
DR BioMuta; BCKDHB; -.
DR DMDM; 129034; -.
DR REPRODUCTION-2DPAGE; IPI00011276; -.
DR EPD; P21953; -.
DR jPOST; P21953; -.
DR MassIVE; P21953; -.
DR PaxDb; P21953; -.
DR PeptideAtlas; P21953; -.
DR PRIDE; P21953; -.
DR ProteomicsDB; 53944; -. [P21953-1]
DR ProteomicsDB; 64342; -.
DR TopDownProteomics; P21953-1; -. [P21953-1]
DR Antibodypedia; 49986; 104 antibodies from 22 providers.
DR DNASU; 594; -.
DR Ensembl; ENST00000320393.9; ENSP00000318351.5; ENSG00000083123.15. [P21953-1]
DR Ensembl; ENST00000356489.9; ENSP00000348880.5; ENSG00000083123.15. [P21953-1]
DR Ensembl; ENST00000369760.8; ENSP00000358775.4; ENSG00000083123.15. [P21953-2]
DR GeneID; 594; -.
DR KEGG; hsa:594; -.
DR MANE-Select; ENST00000320393.9; ENSP00000318351.5; NM_183050.4; NP_898871.1.
DR UCSC; uc003pjd.3; human. [P21953-1]
DR CTD; 594; -.
DR DisGeNET; 594; -.
DR GeneCards; BCKDHB; -.
DR GeneReviews; BCKDHB; -.
DR HGNC; HGNC:987; BCKDHB.
DR HPA; ENSG00000083123; Tissue enhanced (liver).
DR MalaCards; BCKDHB; -.
DR MIM; 248600; phenotype.
DR MIM; 248611; gene.
DR neXtProt; NX_P21953; -.
DR OpenTargets; ENSG00000083123; -.
DR Orphanet; 268145; Classic maple syrup urine disease.
DR Orphanet; 268162; Intermediate maple syrup urine disease.
DR Orphanet; 268173; Intermittent maple syrup urine disease.
DR Orphanet; 268184; Thiamine-responsive maple syrup urine disease.
DR PharmGKB; PA25298; -.
DR VEuPathDB; HostDB:ENSG00000083123; -.
DR eggNOG; KOG0525; Eukaryota.
DR GeneTree; ENSGT00940000156533; -.
DR HOGENOM; CLU_012907_1_5_1; -.
DR InParanoid; P21953; -.
DR OMA; SEAYYMA; -.
DR PhylomeDB; P21953; -.
DR TreeFam; TF105947; -.
DR BioCyc; MetaCyc:MON-12006; -.
DR PathwayCommons; P21953; -.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SABIO-RK; P21953; -.
DR SignaLink; P21953; -.
DR BioGRID-ORCS; 594; 14 hits in 1078 CRISPR screens.
DR ChiTaRS; BCKDHB; human.
DR EvolutionaryTrace; P21953; -.
DR GeneWiki; BCKDHB; -.
DR GenomeRNAi; 594; -.
DR Pharos; P21953; Tbio.
DR PRO; PR:P21953; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P21953; protein.
DR Bgee; ENSG00000083123; Expressed in right lobe of liver and 164 other tissues.
DR ExpressionAtlas; P21953; baseline and differential.
DR Genevisible; P21953; HS.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IMP:HGNC-UCL.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; TAS:ProtInc.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IDA:ComplexPortal.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR Gene3D; 3.40.50.920; -; 1.
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 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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; Lipid metabolism; Maple syrup urine disease;
KW Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Mitochondrion"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 51..392
FT /note="2-oxoisovalerate dehydrogenase subunit beta,
FT mitochondrial"
FT /id="PRO_0000020470"
FT MOD_RES 232
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P3A8"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 212..218
FT /note="VVIPRSP -> IKVISLS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056370"
FT VAR_SEQ 219..392
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056371"
FT VARIANT 41
FT /note="T -> I (in dbSNP:rs35470366)"
FT /id="VAR_050437"
FT VARIANT 170
FT /note="R -> H (in MSUD1B; dbSNP:rs371518124)"
FT /evidence="ECO:0000269|PubMed:22326532"
FT /id="VAR_068348"
FT VARIANT 183
FT /note="R -> P (in MSUD1B; dbSNP:rs79761867)"
FT /evidence="ECO:0000269|PubMed:11509994"
FT /id="VAR_024851"
FT VARIANT 206
FT /note="H -> R (in MSUD1B)"
FT /evidence="ECO:0000269|PubMed:8161368"
FT /id="VAR_004974"
FT VARIANT 278
FT /note="G -> S (in MSUD1B; dbSNP:rs386834233)"
FT /evidence="ECO:0000269|PubMed:11509994"
FT /id="VAR_024852"
FT VARIANT 346
FT /note="Q -> R (in MSUD1B)"
FT /evidence="ECO:0000269|PubMed:22326532"
FT /id="VAR_068349"
FT CONFLICT 20..23
FT /note="EGHW -> RLPP (in Ref. 8)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="T -> S (in Ref. 8; CAA36685)"
FT /evidence="ECO:0000305"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:2BFD"
FT TURN 96..101
FT /evidence="ECO:0007829|PDB:2BFD"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:2BFD"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:2BFD"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 201..205
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:2BFD"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:2BEW"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 280..295
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 337..349
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:2BFD"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:2BFD"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:2BFD"
SQ SEQUENCE 392 AA; 43122 MW; D78097834D063BB7 CRC64;
MAVVAAAAGW LLRLRAAGAE GHWRRLPGAG LARGFLHPAA TVEDAAQRRQ VAHFTFQPDP
EPREYGQTQK MNLFQSVTSA LDNSLAKDPT AVIFGEDVAF GGVFRCTVGL RDKYGKDRVF
NTPLCEQGIV GFGIGIAVTG ATAIAEIQFA DYIFPAFDQI VNEAAKYRYR SGDLFNCGSL
TIRSPWGCVG HGALYHSQSP EAFFAHCPGI KVVIPRSPFQ AKGLLLSCIE DKNPCIFFEP
KILYRAAAEE VPIEPYNIPL SQAEVIQEGS DVTLVAWGTQ VHVIREVASM AKEKLGVSCE
VIDLRTIIPW DVDTICKSVI KTGRLLISHE APLTGGFASE ISSTVQEECF LNLEAPISRV
CGYDTPFPHI FEPFYIPDKW KCYDALRKMI NY
