ODB2_HUMAN
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 03-AUG-2022, entry version 248.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Chuang D.T.;
RT "The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human
RT branched-chain alpha-keto acid dehydrogenase complex.";
RL Biochim. Biophys. Acta 1132:319-321(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3245861; DOI=10.1016/s0021-9258(18)68766-6;
RA Hummel K.B., Litwer S., Bradford A.P., Aitken A., Danner D.J., 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; DOI=10.1016/s0021-9258(18)83297-5;
RA Danner D.J., Litwer S., Herring W.J., Pruckler J.;
RT "Construction and nucleotide sequence of a cDNA encoding the full-length
RT 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 human
RT 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 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., 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 [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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., 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 [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 project:
RT 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 dihydrolipoyl
RT dehydrogenase binding domains of mammalian branched-chain alpha-keto acid
RT dehydrogenase complex: molecular cloning of human and bovine transacylase
RT (E2) cDNAs.";
RL Biochemistry 27:1972-1981(1988).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RX PubMed=1429740; DOI=10.1016/s0021-9258(18)35950-7;
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) component
RT of human branched chain alpha-keto acid dehydrogenase complex and
RT 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., Dickson E.R.,
RA Gershwin M.E.;
RT "Reactivity of primary biliary cirrhosis sera with a human fetal liver cDNA
RT clone of branched-chain alpha-keto acid dehydrogenase dihydrolipoamide
RT acyltransferase, the 52 kD mitochondrial autoantigen.";
RL Hepatology 9:63-68(1989).
RN [14]
RP INVOLVEMENT IN PBC.
RX PubMed=7543435; DOI=10.1002/hep.1840220220;
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 cirrhosis
RT 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., Lake J.,
RA Bjoerkland A., Toetterman T.H., Peters M., Worman H.J., Ansari A.A.,
RA Coppel R.L., Gershwin M.E.;
RT "Comparative studies of antimitochondrial autoantibodies in sera and bile
RT in primary biliary cirrhosis.";
RL Hepatology 25:1085-1089(1997).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-295, 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 [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., 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND IDENTIFICATION BY
RP 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 [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., 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 [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 human
RT mitochondrial branched-chain alpha-keto acid dehydrogenase 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 branched
RT 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 syrup
RT 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., Kinugasa A.,
RA Ishitsu T., Matsuda I., Indo Y.;
RT "Molecular basis of intermittent maple syrup urine disease: novel mutations
RT in the E2 gene of the branched-chain alpha-keto acid dehydrogenase
RT complex.";
RL J. Hum. Genet. 43:91-100(1998).
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). Within this complex, the catalytic
CC function of this enzyme is to accept, and to transfer to coenzyme A,
CC acyl groups that are generated by the branched-chain alpha-keto acid
CC decarboxylase component.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + 2-methylpropanoyl-
CC CoA = (R)-N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC [protein] + CoA; Xref=Rhea:RHEA:18865, Rhea:RHEA-COMP:10475,
CC Rhea:RHEA-COMP:10497, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338,
CC ChEBI:CHEBI:83100, ChEBI:CHEBI:83142; EC=2.3.1.168;
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-keto
CC acid dehydrogenase complex. PBC is a chronic, progressive cholestatic
CC liver disease characterized by the presence of antimitochondrial
CC autoantibodies in patients serum. It manifests with inflammatory
CC obliteration of intra-hepatic bile duct, leading to liver cell damage
CC and cirrhosis. {ECO:0000269|PubMed:2908870, ECO:0000269|PubMed:7543435,
CC ECO:0000269|PubMed:9141421}.
CC -!- DISEASE: Maple syrup urine disease 2 (MSUD2) [MIM:248600]: A metabolic
CC disorder due to an enzyme defect in the catabolic pathway of the
CC 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:1847055, ECO:0000269|PubMed:9621512}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {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};
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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; -; NOT_ANNOTATED_CDS; 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 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 AlphaFoldDB; P11182; -.
DR BMRB; P11182; -.
DR SMR; P11182; -.
DR BioGRID; 107997; 195.
DR ComplexPortal; CPX-2216; Mitochondrial 2-oxoisovalerate dehydrogenase complex.
DR IntAct; P11182; 64.
DR MINT; P11182; -.
DR STRING; 9606.ENSP00000359151; -.
DR GlyGen; P11182; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P11182; -.
DR MetOSite; P11182; -.
DR PhosphoSitePlus; P11182; -.
DR SwissPalm; P11182; -.
DR BioMuta; DBT; -.
DR DMDM; 400668; -.
DR EPD; P11182; -.
DR jPOST; P11182; -.
DR MassIVE; P11182; -.
DR MaxQB; P11182; -.
DR PaxDb; P11182; -.
DR PeptideAtlas; P11182; -.
DR PRIDE; P11182; -.
DR ProteomicsDB; 52718; -.
DR ABCD; P11182; 1 sequenced antibody.
DR Antibodypedia; 19986; 193 antibodies from 24 providers.
DR DNASU; 1629; -.
DR Ensembl; ENST00000370132.8; ENSP00000359151.3; ENSG00000137992.15.
DR GeneID; 1629; -.
DR KEGG; hsa:1629; -.
DR UCSC; uc001dta.4; human.
DR CTD; 1629; -.
DR DisGeNET; 1629; -.
DR GeneCards; DBT; -.
DR GeneReviews; DBT; -.
DR HGNC; HGNC:2698; DBT.
DR HPA; ENSG00000137992; Low tissue specificity.
DR MalaCards; DBT; -.
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 VEuPathDB; HostDB:ENSG00000137992; -.
DR eggNOG; KOG0558; Eukaryota.
DR HOGENOM; CLU_016733_10_0_1; -.
DR InParanoid; P11182; -.
DR OrthoDB; 854035at2759; -.
DR PhylomeDB; P11182; -.
DR TreeFam; TF314182; -.
DR BioCyc; MetaCyc:MON-12007; -.
DR BRENDA; 2.3.1.168; 2681.
DR PathwayCommons; P11182; -.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR Reactome; R-HSA-9013407; RHOH GTPase cycle.
DR SABIO-RK; P11182; -.
DR SignaLink; P11182; -.
DR BioGRID-ORCS; 1629; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; DBT; human.
DR EvolutionaryTrace; P11182; -.
DR GeneWiki; DBT_(gene); -.
DR GenomeRNAi; 1629; -.
DR Pharos; P11182; Tbio.
DR PRO; PR:P11182; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P11182; protein.
DR Bgee; ENSG00000137992; Expressed in buccal mucosa cell and 208 other tissues.
DR ExpressionAtlas; P11182; baseline and differential.
DR Genevisible; P11182; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IPI:ComplexPortal.
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:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0043754; F:dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0031405; F:lipoic acid binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IDA:ComplexPortal.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
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.
DR PROSITE; PS51826; PSBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Acyltransferase; Direct protein sequencing;
KW Disease variant; Lipoyl; Maple syrup urine disease; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..61
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 62..482
FT /note="Lipoamide acyltransferase component of branched-
FT chain alpha-keto acid dehydrogenase complex, mitochondrial"
FT /id="PRO_0000020489"
FT DOMAIN 64..139
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 172..209
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT REGION 147..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 452
FT /evidence="ECO:0000255"
FT ACT_SITE 456
FT /evidence="ECO:0000255"
FT MOD_RES 105
FT /note="N6-lipoyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT MOD_RES 133
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 196
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 196
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 202
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 243
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 250
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 261
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 289
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 289
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 295
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 304
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 440
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT MOD_RES 440
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P53395"
FT VARIANT 98
FT /note="I -> M (in MSUD2; dbSNP:rs121965001)"
FT /evidence="ECO:0000269|PubMed:9621512"
FT /id="VAR_015099"
FT VARIANT 276
FT /note="F -> C (in MSUD2; dbSNP:rs121964999)"
FT /evidence="ECO:0000269|PubMed:1847055"
FT /id="VAR_004978"
FT VARIANT 384
FT /note="G -> S (in MSUD2; dbSNP:rs12021720)"
FT /evidence="ECO:0000269|PubMed:16710414,
FT ECO:0000269|PubMed:9621512"
FT /id="VAR_015100"
FT CONFLICT 321
FT /note="Q -> P (in Ref. 4; AAA64512)"
FT /evidence="ECO:0000305"
FT CONFLICT 354
FT /note="L -> V (in Ref. 4; AAA64512)"
FT /evidence="ECO:0000305"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1K8M"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1K8M"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1K8M"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1K8M"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1K8M"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1K8M"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1K8O"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:1K8M"
FT HELIX 175..183
FT /evidence="ECO:0007829|PDB:3RNM"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3RNM"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3RNM"
FT HELIX 202..213
FT /evidence="ECO:0007829|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
