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2-oxoisovalerate dehydrogenase subunit beta, mitochondrial (EC 1.2.4.4) (Branched-chain alpha-keto acid dehydrogenase E1 component beta chain) (BCKDE1B) (BCKDH E1-beta)

 ODBB_HUMAN              Reviewed;         392 AA.
P21953; Q5T2J3; Q9BQL0;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 2.
20-JUN-2018, entry version 196.
RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, mitochondrial;
EC=1.2.4.4;
AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
Short=BCKDE1B;
Short=BCKDH E1-beta;
Flags: Precursor;
Name=BCKDHB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2365818; DOI=10.1172/JCI114690;
Matsuda I., Asaka J., Akaboshi I., Endo F., Mitsubuchi H.,
Nobukuni Y.;
"Maple syrup urine disease. Complete primary structure of the E1 beta
subunit of human branched chain alpha-ketoacid dehydrogenase complex
deduced from the nucleotide sequence and a gene analysis of patients
with this disease.";
J. Clin. Invest. 86:242-247(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8651316;
Chuang J.L., Cox R.P., Chuang D.T.;
"Maple syrup urine disease: the E1beta gene of human branched-chain
alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and
the 3' UTR in one of the two E1beta mRNAs arises from intronic
sequences.";
Am. J. Hum. Genet. 58:1373-1377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Eye, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-392 (ISOFORM 1).
PubMed=2335211; DOI=10.1016/0014-5793(90)80215-5;
Chuang J.L., Cox R.P., Chuang D.T.;
"Molecular cloning of the mature E1b-beta subunit of human branched-
chain alpha-keto acid dehydrogenase complex.";
FEBS Lett. 262:305-309(1990).
[9]
PROTEIN SEQUENCE OF 36-62.
PubMed=7918575; DOI=10.1016/0304-4165(94)90161-9;
Wynn R.M., Kochi H., Cox R.P., Chuang D.T.;
"Differential processing of human and rat E1 alpha precursors of the
branched-chain alpha-keto acid dehydrogenase complex caused by an N-
terminal proline in the rat sequence.";
Biochim. Biophys. Acta 1201:125-128(1994).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER GLN-50, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
VARIANT MSUD1B ARG-206.
PubMed=8161368;
Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y.,
Endo F., Matsuda I.;
"Heterogeneity of mutations in maple syrup urine disease (MSUD):
screening and identification of affected E1 alpha and E1 beta subunits
of the branched-chain alpha-keto-acid dehydrogenase multienzyme
complex.";
Biochim. Biophys. Acta 1225:64-70(1993).
[15]
VARIANTS MSUD1B PRO-183 AND SER-278.
PubMed=11509994; DOI=10.1086/323677;
Edelmann L., Wasserstein M.P., Kornreich R., Sansaricq C.,
Snyderman S.E., Diaz G.A.;
"Maple syrup urine disease: identification and carrier-frequency
determination of a novel founder mutation in the Ashkenazi Jewish
population.";
Am. J. Hum. Genet. 69:863-868(2001).
[16]
VARIANTS MSUD1B HIS-170 AND ARG-346.
PubMed=22326532; DOI=10.1016/j.gene.2012.01.082;
Wang Y.P., Qi M.L., Li T.T., Zhao Y.J.;
"Two novel mutations in the BCKDHB gene (R170H, Q346R) cause the
classic form of maple syrup urine disease (MSUD).";
Gene 498:112-115(2012).
-!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex
catalyzes the overall conversion of alpha-keto acids to acyl-CoA
and CO(2). It contains multiple copies of three enzymatic
components: branched-chain alpha-keto acid decarboxylase (E1),
lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
-!- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate +
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
lipoyllysine = [dihydrolipoyllysine-residue (2-
methylpropanoyl)transferase] S-(2-
methylpropanoyl)dihydrolipoyllysine + CO(2).
-!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta chains.
-!- INTERACTION:
P12694:BCKDHA; NbExp=13; IntAct=EBI-1029067, EBI-1029053;
P12694-1:BCKDHA; NbExp=3; IntAct=EBI-15489569, EBI-15489562;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P21953-1; Sequence=Displayed;
Name=2;
IsoId=P21953-2; Sequence=VSP_056370, VSP_056371;
Note=No experimental confirmation available.;
-!- DISEASE: Maple syrup urine disease 1B (MSUD1B) [MIM:248600]: A
metabolic disorder due to an enzyme defect in the catabolic
pathway of the branched-chain amino acids leucine, isoleucine, and
valine. Accumulation of these 3 amino acids and their
corresponding keto acids leads to encephalopathy and progressive
neurodegeneration. Clinical features include mental and physical
retardation, feeding problems, and a maple syrup odor to the
urine. The keto acids of the branched-chain amino acids are
present in the urine. If untreated, maple syrup urine disease can
lead to seizures, coma, and death. The disease is often classified
by its pattern of signs and symptoms. The most common and severe
form of the disease is the classic type, which becomes apparent
soon after birth. Variant forms of the disorder become apparent
later in infancy or childhood and are typically milder, but they
still involve developmental delay and other medical problems if
not treated. {ECO:0000269|PubMed:11509994,
ECO:0000269|PubMed:22326532, ECO:0000269|PubMed:8161368}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
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EMBL; M55575; AAA51812.1; -; mRNA.
EMBL; D90391; BAA14389.1; -; Genomic_DNA.
EMBL; AK289977; BAF82666.1; -; mRNA.
EMBL; BT020063; AAV38866.1; -; mRNA.
EMBL; AL049696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48696.1; -; Genomic_DNA.
EMBL; CH471051; EAW48697.1; -; Genomic_DNA.
EMBL; CH471051; EAW48698.1; -; Genomic_DNA.
EMBL; BC034481; AAH34481.1; -; mRNA.
EMBL; BC040139; AAH40139.1; -; mRNA.
EMBL; U50708; AAB16763.1; -; mRNA.
EMBL; X52446; CAA36685.1; -; mRNA.
CCDS; CCDS4994.1; -. [P21953-1]
PIR; A37157; A37157.
RefSeq; NP_000047.1; NM_000056.4. [P21953-1]
RefSeq; NP_001305904.1; NM_001318975.1.
RefSeq; NP_898871.1; NM_183050.3. [P21953-1]
UniGene; Hs.156414; -.
UniGene; Hs.386402; -.
UniGene; Hs.654441; -.
PDB; 1DTW; X-ray; 2.70 A; B=51-392.
PDB; 1OLS; X-ray; 1.85 A; B=51-392.
PDB; 1OLU; X-ray; 1.90 A; B=51-392.
PDB; 1OLX; X-ray; 2.25 A; B=51-392.
PDB; 1U5B; X-ray; 1.83 A; B=51-392.
PDB; 1V11; X-ray; 1.95 A; B=51-392.
PDB; 1V16; X-ray; 1.90 A; B=51-392.
PDB; 1V1M; X-ray; 2.00 A; B=51-392.
PDB; 1V1R; X-ray; 1.80 A; B=51-392.
PDB; 1WCI; X-ray; 1.84 A; B=51-392.
PDB; 1X7W; X-ray; 1.73 A; B=51-392.
PDB; 1X7X; X-ray; 2.10 A; B=51-392.
PDB; 1X7Y; X-ray; 1.57 A; B=51-392.
PDB; 1X7Z; X-ray; 1.72 A; B=51-392.
PDB; 1X80; X-ray; 2.00 A; B=51-392.
PDB; 2BEU; X-ray; 1.89 A; B=51-392.
PDB; 2BEV; X-ray; 1.80 A; B=51-392.
PDB; 2BEW; X-ray; 1.79 A; B=51-392.
PDB; 2BFB; X-ray; 1.77 A; B=51-392.
PDB; 2BFC; X-ray; 1.64 A; B=51-392.
PDB; 2BFD; X-ray; 1.39 A; B=51-392.
PDB; 2BFE; X-ray; 1.69 A; B=51-392.
PDB; 2BFF; X-ray; 1.46 A; B=51-392.
PDB; 2J9F; X-ray; 1.88 A; B/D=51-392.
PDBsum; 1DTW; -.
PDBsum; 1OLS; -.
PDBsum; 1OLU; -.
PDBsum; 1OLX; -.
PDBsum; 1U5B; -.
PDBsum; 1V11; -.
PDBsum; 1V16; -.
PDBsum; 1V1M; -.
PDBsum; 1V1R; -.
PDBsum; 1WCI; -.
PDBsum; 1X7W; -.
PDBsum; 1X7X; -.
PDBsum; 1X7Y; -.
PDBsum; 1X7Z; -.
PDBsum; 1X80; -.
PDBsum; 2BEU; -.
PDBsum; 2BEV; -.
PDBsum; 2BEW; -.
PDBsum; 2BFB; -.
PDBsum; 2BFC; -.
PDBsum; 2BFD; -.
PDBsum; 2BFE; -.
PDBsum; 2BFF; -.
PDBsum; 2J9F; -.
ProteinModelPortal; P21953; -.
SMR; P21953; -.
BioGrid; 107066; 20.
DIP; DIP-6147N; -.
IntAct; P21953; 9.
STRING; 9606.ENSP00000318351; -.
iPTMnet; P21953; -.
PhosphoSitePlus; P21953; -.
BioMuta; BCKDHB; -.
DMDM; 129034; -.
REPRODUCTION-2DPAGE; IPI00011276; -.
EPD; P21953; -.
PaxDb; P21953; -.
PeptideAtlas; P21953; -.
PRIDE; P21953; -.
ProteomicsDB; 53944; -.
TopDownProteomics; P21953-1; -. [P21953-1]
DNASU; 594; -.
Ensembl; ENST00000320393; ENSP00000318351; ENSG00000083123. [P21953-1]
Ensembl; ENST00000356489; ENSP00000348880; ENSG00000083123. [P21953-1]
Ensembl; ENST00000369760; ENSP00000358775; ENSG00000083123. [P21953-2]
GeneID; 594; -.
KEGG; hsa:594; -.
UCSC; uc003pjd.3; human. [P21953-1]
CTD; 594; -.
DisGeNET; 594; -.
EuPathDB; HostDB:ENSG00000083123.14; -.
GeneCards; BCKDHB; -.
GeneReviews; BCKDHB; -.
HGNC; HGNC:987; BCKDHB.
HPA; HPA031580; -.
MalaCards; BCKDHB; -.
MIM; 248600; phenotype.
MIM; 248611; gene.
neXtProt; NX_P21953; -.
OpenTargets; ENSG00000083123; -.
Orphanet; 268145; Classic maple syrup urine disease.
Orphanet; 268162; Intermediate maple syrup urine disease.
Orphanet; 268173; Intermittent maple syrup urine disease.
Orphanet; 268184; Thiamine-responsive maple syrup urine disease.
PharmGKB; PA25298; -.
eggNOG; KOG0525; Eukaryota.
eggNOG; COG0022; LUCA.
GeneTree; ENSGT00530000063423; -.
HOGENOM; HOG000281451; -.
HOVERGEN; HBG108210; -.
InParanoid; P21953; -.
KO; K00167; -.
OMA; VQERCFH; -.
OrthoDB; EOG091G0B9T; -.
PhylomeDB; P21953; -.
TreeFam; TF105947; -.
BioCyc; MetaCyc:MONOMER-12006; -.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
SABIO-RK; P21953; -.
ChiTaRS; BCKDHB; human.
EvolutionaryTrace; P21953; -.
GeneWiki; BCKDHB; -.
GenomeRNAi; 594; -.
PRO; PR:P21953; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000083123; -.
CleanEx; HS_BCKDHB; -.
ExpressionAtlas; P21953; baseline and differential.
Genevisible; P21953; HS.
GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IMP:HGNC.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IMP:HGNC.
GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; TAS:ProtInc.
GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; IEA:Ensembl.
GO; GO:0009083; P:branched-chain amino acid catabolic process; IMP:HGNC.
Gene3D; 3.40.50.920; -; 1.
InterPro; IPR029061; THDP-binding.
InterPro; IPR009014; Transketo_C/PFOR_II.
InterPro; IPR005475; Transketolase-like_Pyr-bd.
InterPro; IPR033248; Transketolase_C.
Pfam; PF02779; Transket_pyr; 1.
Pfam; PF02780; Transketolase_C; 1.
SMART; SM00861; Transket_pyr; 1.
SUPFAM; SSF52518; SSF52518; 1.
SUPFAM; SSF52922; SSF52922; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation;
Maple syrup urine disease; Mitochondrion; Oxidoreductase;
Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 50 Mitochondrion.
{ECO:0000244|PubMed:25944712}.
CHAIN 51 392 2-oxoisovalerate dehydrogenase subunit
beta, mitochondrial.
/FTId=PRO_0000020470.
MOD_RES 232 232 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q6P3A8}.
MOD_RES 241 241 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 212 218 VVIPRSP -> IKVISLS (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056370.
VAR_SEQ 219 392 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056371.
VARIANT 41 41 T -> I (in dbSNP:rs35470366).
/FTId=VAR_050437.
VARIANT 170 170 R -> H (in MSUD1B; dbSNP:rs371518124).
{ECO:0000269|PubMed:22326532}.
/FTId=VAR_068348.
VARIANT 183 183 R -> P (in MSUD1B; dbSNP:rs79761867).
{ECO:0000269|PubMed:11509994}.
/FTId=VAR_024851.
VARIANT 206 206 H -> R (in MSUD1B).
{ECO:0000269|PubMed:8161368}.
/FTId=VAR_004974.
VARIANT 278 278 G -> S (in MSUD1B; dbSNP:rs386834233).
{ECO:0000269|PubMed:11509994}.
/FTId=VAR_024852.
VARIANT 346 346 Q -> R (in MSUD1B).
{ECO:0000269|PubMed:22326532}.
/FTId=VAR_068349.
CONFLICT 20 23 EGHW -> RLPP (in Ref. 8). {ECO:0000305}.
CONFLICT 322 322 T -> S (in Ref. 8; CAA36685).
{ECO:0000305}.
STRAND 68 71 {ECO:0000244|PDB:2BFD}.
HELIX 73 87 {ECO:0000244|PDB:2BFD}.
STRAND 92 95 {ECO:0000244|PDB:2BFD}.
TURN 96 101 {ECO:0000244|PDB:2BFD}.
TURN 106 109 {ECO:0000244|PDB:2BFD}.
HELIX 110 114 {ECO:0000244|PDB:2BFD}.
TURN 116 118 {ECO:0000244|PDB:2BFD}.
STRAND 119 121 {ECO:0000244|PDB:2BFD}.
HELIX 126 138 {ECO:0000244|PDB:2BFD}.
STRAND 143 146 {ECO:0000244|PDB:2BFD}.
HELIX 150 152 {ECO:0000244|PDB:2BFD}.
HELIX 154 156 {ECO:0000244|PDB:2BFD}.
HELIX 157 161 {ECO:0000244|PDB:2BFD}.
HELIX 164 166 {ECO:0000244|PDB:2BFD}.
HELIX 167 170 {ECO:0000244|PDB:2BFD}.
TURN 171 173 {ECO:0000244|PDB:2BFD}.
STRAND 180 187 {ECO:0000244|PDB:2BFD}.
HELIX 193 195 {ECO:0000244|PDB:2BFD}.
HELIX 201 205 {ECO:0000244|PDB:2BFD}.
STRAND 211 213 {ECO:0000244|PDB:2BFD}.
HELIX 218 230 {ECO:0000244|PDB:2BFD}.
STRAND 231 233 {ECO:0000244|PDB:2BFD}.
STRAND 235 240 {ECO:0000244|PDB:2BFD}.
HELIX 241 243 {ECO:0000244|PDB:2BFD}.
TURN 244 246 {ECO:0000244|PDB:2BEW}.
STRAND 249 254 {ECO:0000244|PDB:2BFD}.
STRAND 264 267 {ECO:0000244|PDB:2BFD}.
STRAND 270 276 {ECO:0000244|PDB:2BFD}.
HELIX 280 295 {ECO:0000244|PDB:2BFD}.
STRAND 299 303 {ECO:0000244|PDB:2BFD}.
STRAND 306 309 {ECO:0000244|PDB:2BFD}.
HELIX 312 322 {ECO:0000244|PDB:2BFD}.
STRAND 325 333 {ECO:0000244|PDB:2BFD}.
HELIX 337 349 {ECO:0000244|PDB:2BFD}.
HELIX 350 352 {ECO:0000244|PDB:2BFD}.
STRAND 358 362 {ECO:0000244|PDB:2BFD}.
HELIX 372 375 {ECO:0000244|PDB:2BFD}.
HELIX 379 390 {ECO:0000244|PDB:2BFD}.
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


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