ID ODB2_HUMAN Reviewed; 482 AA. AC P11182; B2R811; Q5VVL8; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 3. DT 11-NOV-2015, entry version 196. DE RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial; DE EC=2.3.1.168; DE AltName: Full=52 kDa mitochondrial autoantigen of primary biliary cirrhosis {ECO:0000303|PubMed:2908870}; DE AltName: Full=Branched chain 2-oxo-acid dehydrogenase complex component E2 {ECO:0000303|PubMed:7543435, ECO:0000303|PubMed:9141421}; DE Short=BCOADC-E2 {ECO:0000303|PubMed:7543435, ECO:0000303|PubMed:9141421}; DE AltName: Full=Branched-chain alpha-keto acid dehydrogenase complex component E2; DE Short=BCKAD-E2; DE Short=BCKADE2; DE AltName: Full=Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex; DE AltName: Full=Dihydrolipoamide branched chain transacylase; DE AltName: Full=Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase; DE Flags: Precursor; GN Name=DBT; Synonyms=BCATE2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Kidney; RX PubMed=1420314; DOI=10.1016/0167-4781(92)90169-Z; RA Lau K.S., Chuang J.L., Herring W.J., Danner D.J., Cox R.P., RA Chuang D.T.; RT "The complete cDNA sequence for dihydrolipoyl transacylase (E2) of RT human branched-chain alpha-keto acid dehydrogenase complex."; RL Biochim. Biophys. Acta 1132:319-321(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3245861; RA Hummel K.B., Litwer S., Bradford A.P., Aitken A., Danner D.J., RA Yeaman S.J.; RT "Nucleotide sequence of a cDNA for branched chain acyltransferase with RT analysis of the deduced protein structure."; RL J. Biol. Chem. 263:6165-6168(1988). RN [3] RP SEQUENCE REVISION. RX PubMed=2708389; RA Danner D.J., Litwer S., Herring W.J., Pruckler J.; RT "Construction and nucleotide sequence of a cDNA encoding the full- RT length preprotein for human branched chain acyltransferase."; RL J. Biol. Chem. 264:7742-7746(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2742576; DOI=10.1016/0006-291X(89)91347-8; RA Nobukuni Y., Mitsubuchi H., Endo F., Matsuda I.; RT "Complete primary structure of the transacylase (E2b) subunit of the RT human branched chain alpha-keto acid dehydrogenase complex."; RL Biochem. Biophys. Res. Commun. 161:1035-1041(1989). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-384. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-313. RX PubMed=2837277; DOI=10.1021/bi00406a025; RA Lau K.S., Griffin T.A., Hu C.-W.C., Chuang D.T.; RT "Conservation of primary structure in the lipoyl-bearing and RT dihydrolipoyl dehydrogenase binding domains of mammalian branched- RT chain alpha-keto acid dehydrogenase complex: molecular cloning of RT human and bovine transacylase (E2) cDNAs."; RL Biochemistry 27:1972-1981(1988). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6. RX PubMed=1429740; RA Lau K.S., Herring W.J., Chuang J.L., McKean M., Danner D.J., Cox R.P., RA Chuang D.T.; RT "Structure of the gene encoding dihydrolipoyl transacylase (E2) RT component of human branched chain alpha-keto acid dehydrogenase RT complex and characterization of an E2 pseudogene."; RL J. Biol. Chem. 267:24090-24096(1992). RN [12] RP PROTEIN SEQUENCE OF 47-81. 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 [13] RP INVOLVEMENT IN PBC. RX PubMed=2908870; DOI=10.1002/hep.1840090110; RA Surh C.D., Danner D.J., Ahmed A., Coppel R.L., Mackay I.R., RA Dickson E.R., Gershwin M.E.; RT "Reactivity of primary biliary cirrhosis sera with a human fetal liver RT cDNA clone of branched-chain alpha-keto acid dehydrogenase RT dihydrolipoamide acyltransferase, the 52 kD mitochondrial RT autoantigen."; RL Hepatology 9:63-68(1989). RN [14] RP INVOLVEMENT IN PBC. RX PubMed=7543435; DOI=10.1016/0270-9139(95)90572-3; RA Leung P.S., Chuang D.T., Wynn R.M., Cha S., Danner D.J., Ansari A., RA Coppel R.L., Gershwin M.E.; RT "Autoantibodies to BCOADC-E2 in patients with primary biliary RT cirrhosis recognize a conformational epitope."; RL Hepatology 22:505-513(1995). RN [15] RP INVOLVEMENT IN PBC. RX PubMed=9141421; DOI=10.1002/hep.510250506; RA Nishio A., Van de Water J., Leung P.S., Joplin R., Neuberger J.M., RA Lake J., Bjoerkland A., Toetterman T.H., Peters M., Worman H.J., RA Ansari A.A., Coppel R.L., Gershwin M.E.; RT "Comparative studies of antimitochondrial autoantibodies in sera and RT bile in primary biliary cirrhosis."; RL Hepatology 25:1085-1089(1997). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [17] 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., RA Buerckstuemmer T., 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] 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., RA Ayoub D., 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 [20] RP STRUCTURE BY NMR OF 62-145. RX PubMed=11839747; DOI=10.1074/jbc.M110952200; RA Chang C.-F., Chou H.-T., Chuang J.L., Chuang D.T., Huang T.-H.; RT "Solution structure and dynamics of the lipoic acid-bearing domain of RT human mitochondrial branched-chain alpha-keto acid dehydrogenase RT complex."; RL J. Biol. Chem. 277:15865-15873(2002). RN [21] RP STRUCTURE BY NMR OF 163-220. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the E3-binding domain of dihydrolipoamide RT branched chain transacylase."; RL Submitted (NOV-2005) to the PDB data bank. RN [22] RP VARIANT MSUD2 CYS-276. RX PubMed=1847055; DOI=10.1016/0006-291X(91)91489-Y; RA Fisher C.W., Lau K.S., Fisher C.R., Wynn R.M., Cox R.P., Chuang D.T.; RT "A 17-bp insertion and a Phe215-->Cys missense mutation in the RT dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple RT syrup urine disease patient WG-34."; RL Biochem. Biophys. Res. Commun. 174:804-809(1991). RN [23] RP VARIANTS MSUD2 MET-98 AND SER-384. RX PubMed=9621512; DOI=10.1007/s100380050047; RA Tsuruta M., Mitsubuchi H., Mardy S., Miura Y., Hayashida Y., RA Kinugasa A., Ishitsu T., Matsuda I., Indo Y.; RT "Molecular basis of intermittent maple syrup urine disease: novel RT mutations in the E2 gene of the branched-chain alpha-keto acid RT dehydrogenase complex."; RL J. Hum. Genet. 43:91-100(1998). CC -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex CC catalyzes the overall conversion of alpha-keto acids to acyl-CoA CC and CO(2). It contains multiple copies of three enzymatic CC components: branched-chain alpha-keto acid decarboxylase (E1), CC lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). CC Within this complex, the catalytic function of this enzyme is to CC accept, and to transfer to coenzyme A, acyl groups that are CC generated by the branched-chain alpha-keto acid decarboxylase CC component. CC -!- CATALYTIC ACTIVITY: 2-methylpropanoyl-CoA + enzyme N(6)- CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2- CC methylpropanoyl)dihydrolipoyl)lysine. CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Note=Binds 1 lipoyl cofactor covalently.; CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- DISEASE: Note=Patients with primary biliary cirrhosis (PBC) show CC autoantibodies against the E2 component of branched-chain alpha- CC keto acid dehydrogenase complex. PBC is a chronic, progressive CC cholestatic liver disease characterized by the presence of CC antimitochondrial autoantibodies in patients serum. It manifests CC with inflammatory obliteration of intra-hepatic bile duct, leading CC to liver cell damage and cirrhosis. {ECO:0000269|PubMed:2908870, CC ECO:0000269|PubMed:7543435, ECO:0000269|PubMed:9141421}. CC -!- DISEASE: Maple syrup urine disease 2 (MSUD2) [MIM:248600]: A CC metabolic disorder due to an enzyme defect in the catabolic CC pathway of the branched-chain amino acids leucine, isoleucine, and CC valine. Accumulation of these 3 amino acids and their CC corresponding keto acids leads to encephalopathy and progressive CC neurodegeneration. Clinical features include mental and physical CC retardation, feeding problems, and a maple syrup odor to the CC urine. The keto acids of the branched-chain amino acids are CC present in the urine. If untreated, maple syrup urine disease can CC lead to seizures, coma, and death. The disease is often classified CC by its pattern of signs and symptoms. The most common and severe CC form of the disease is the classic type, which becomes apparent CC soon after birth. Variant forms of the disorder become apparent CC later in infancy or childhood and are typically milder, but they CC still involve developmental delay and other medical problems if CC not treated. {ECO:0000269|PubMed:1847055, CC ECO:0000269|PubMed:9621512}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 lipoyl-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA35589.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAA64512.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; X66785; CAA47285.1; -; mRNA. DR EMBL; J03208; AAA35589.1; ALT_INIT; mRNA. DR EMBL; M27093; AAA64512.1; ALT_INIT; mRNA. DR EMBL; BT007372; AAP36036.1; -; mRNA. DR EMBL; AL445928; CAH72257.1; -; Genomic_DNA. DR EMBL; AK313191; BAG36008.1; -; mRNA. DR EMBL; CH471097; EAW72963.1; -; Genomic_DNA. DR EMBL; BC016675; AAH16675.1; -; mRNA. DR EMBL; M19301; AAA59200.1; ALT_SEQ; mRNA. DR EMBL; X68104; CAA48225.1; -; Genomic_DNA. DR CCDS; CCDS767.1; -. DR PIR; A32422; A32422. DR RefSeq; NP_001909.3; NM_001918.3. DR UniGene; Hs.709187; -. DR PDB; 1K8M; NMR; -; A=62-145. DR PDB; 1K8O; NMR; -; A=62-145. DR PDB; 1ZWV; NMR; -; A=165-213. DR PDB; 2COO; NMR; -; A=163-220. DR PDB; 3RNM; X-ray; 2.40 A; E/F=165-213. DR PDBsum; 1K8M; -. DR PDBsum; 1K8O; -. DR PDBsum; 1ZWV; -. DR PDBsum; 2COO; -. DR PDBsum; 3RNM; -. DR ProteinModelPortal; P11182; -. DR SMR; P11182; 62-147, 163-220, 249-482. DR BioGrid; 107997; 32. DR IntAct; P11182; 8. DR MINT; MINT-1161634; -. DR STRING; 9606.ENSP00000359151; -. DR PhosphoSite; P11182; -. DR BioMuta; DBT; -. DR DMDM; 400668; -. DR MaxQB; P11182; -. DR PaxDb; P11182; -. DR PRIDE; P11182; -. DR DNASU; 1629; -. DR Ensembl; ENST00000370132; ENSP00000359151; ENSG00000137992. DR GeneID; 1629; -. DR KEGG; hsa:1629; -. DR UCSC; uc001dta.3; human. DR CTD; 1629; -. DR GeneCards; DBT; -. DR GeneReviews; DBT; -. DR H-InvDB; HIX0000815; -. DR HGNC; HGNC:2698; DBT. DR HPA; HPA026481; -. DR HPA; HPA026485; -. DR HPA; HPA026533; -. DR MIM; 248600; phenotype. DR MIM; 248610; gene. DR neXtProt; NX_P11182; -. 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; PA27167; -. DR eggNOG; KOG0558; Eukaryota. DR eggNOG; COG0508; LUCA. DR HOGENOM; HOG000281564; -. DR HOVERGEN; HBG104085; -. DR InParanoid; P11182; -. DR KO; K09699; -. DR OrthoDB; EOG7GFB4W; -. DR PhylomeDB; P11182; -. DR TreeFam; TF314182; -. DR BioCyc; MetaCyc:MONOMER-12007; -. DR BRENDA; 2.3.1.168; 2681. DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism. DR ChiTaRS; DBT; human. DR EvolutionaryTrace; P11182; -. DR GeneWiki; DBT_(gene); -. DR GenomeRNAi; 1629; -. DR NextBio; 6684; -. DR PRO; PR:P11182; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; P11182; -. DR CleanEx; HS_DBT; -. DR ExpressionAtlas; P11182; baseline and differential. DR Genevisible; P11182; HS. DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; TAS:ProtInc. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome. DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 3.30.559.10; -; 1. DR Gene3D; 4.10.320.10; -; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase. DR InterPro; IPR015761; BCKDC_E2. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR023213; CAT-like_dom. DR InterPro; IPR004167; E3-bd. DR InterPro; IPR011053; Single_hybrid_motif. DR PANTHER; PTHR23151:SF71; PTHR23151:SF71; 2. DR Pfam; PF00198; 2-oxoacid_dh; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR Pfam; PF02817; E3_binding; 1. DR SUPFAM; SSF47005; SSF47005; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Complete proteome; KW Direct protein sequencing; Disease mutation; Lipoyl; KW Maple syrup urine disease; Mitochondrion; Phosphoprotein; KW Reference proteome; Transferase; Transit peptide. FT TRANSIT 1 61 Mitochondrion. {ECO:0000255}. FT CHAIN 62 482 Lipoamide acyltransferase component of FT branched-chain alpha-keto acid FT dehydrogenase complex, mitochondrial. FT /FTId=PRO_0000020489. FT DOMAIN 64 139 Lipoyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT ACT_SITE 452 452 {ECO:0000255}. FT ACT_SITE 456 456 {ECO:0000255}. FT MOD_RES 105 105 N6-lipoyllysine. {ECO:0000250, FT ECO:0000255|PROSITE-ProRule:PRU01066}. FT MOD_RES 133 133 N6-succinyllysine. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 196 196 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 196 196 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 202 202 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 220 220 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 243 243 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 250 250 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 261 261 N6-succinyllysine. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 289 289 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 289 289 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 295 295 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 304 304 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 435 435 N6-acetyllysine. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 440 440 N6-acetyllysine; alternate. FT {ECO:0000250|UniProtKB:P53395}. FT MOD_RES 440 440 N6-succinyllysine; alternate. FT {ECO:0000250|UniProtKB:P53395}. FT VARIANT 98 98 I -> M (in MSUD2). FT {ECO:0000269|PubMed:9621512}. FT /FTId=VAR_015099. FT VARIANT 276 276 F -> C (in MSUD2). FT {ECO:0000269|PubMed:1847055}. FT /FTId=VAR_004978. FT VARIANT 384 384 G -> S (in MSUD2; dbSNP:rs12021720). FT {ECO:0000269|PubMed:16710414, FT ECO:0000269|PubMed:9621512}. FT /FTId=VAR_015100. FT CONFLICT 321 321 Q -> P (in Ref. 4; AAA64512). FT {ECO:0000305}. FT CONFLICT 354 354 L -> V (in Ref. 4; AAA64512). FT {ECO:0000305}. FT STRAND 65 68 {ECO:0000244|PDB:1K8M}. FT STRAND 79 84 {ECO:0000244|PDB:1K8M}. FT STRAND 94 96 {ECO:0000244|PDB:1K8M}. FT STRAND 99 102 {ECO:0000244|PDB:1K8M}. FT STRAND 107 109 {ECO:0000244|PDB:1K8M}. FT STRAND 116 121 {ECO:0000244|PDB:1K8M}. FT STRAND 125 129 {ECO:0000244|PDB:1K8O}. FT STRAND 133 139 {ECO:0000244|PDB:1K8M}. FT HELIX 175 183 {ECO:0000244|PDB:3RNM}. FT HELIX 188 190 {ECO:0000244|PDB:3RNM}. FT HELIX 196 198 {ECO:0000244|PDB:3RNM}. FT HELIX 202 213 {ECO:0000244|PDB:3RNM}. SQ SEQUENCE 482 AA; 53487 MW; A7CA728C8F33D126 CRC64; MAAVRMLRTW SRNAGKLICV RYFQTCGNVH VLKPNYVCFF GYPSFKYSHP HHFLKTTAAL RGQVVQFKLS DIGEGIREVT VKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKK LYYNLDDIAY VGKPLVDIET EALKDSEEDV VETPAVSHDE HTHQEIKGRK TLATPAVRRL AMENNIKLSE VVGSGKDGRI LKEDILNYLE KQTGAILPPS PKVEIMPPPP KPKDMTVPIL VSKPPVFTGK DKTEPIKGFQ KAMVKTMSAA LKIPHFGYCD EIDLTELVKL REELKPIAFA RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT EQGLIVPNVK NVQICSIFDI ATELNRLQKL GSVGQLSTTD LTGGTFTLSN IGSIGGTFAK PVIMPPEVAI GALGSIKAIP RFNQKGEVYK AQIMNVSWSA DHRVIDGATM SRFSNLWKSY LENPAFMLLD LK //