ID   ODB2_MOUSE              Reviewed;         482 AA.
AC   P53395; Q3TMF5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial {ECO:0000305};
DE            EC=2.3.1.168 {ECO:0000250|UniProtKB:P11181};
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=8605244; DOI=10.1016/0167-4781(95)00212-x;
RA   Costeas P.A., Tonelli L.A., Chinsky J.M.;
RT   "Molecular cloning of the murine branched chain alpha-ketoacid
RT   dehydrogenase E2 subunit: presence of 3' B1 repeat elements.";
RL   Biochim. Biophys. Acta 1305:25-28(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-196; LYS-261; LYS-289
RP   AND LYS-440, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-196; LYS-202; LYS-243; LYS-250;
RP   LYS-289; LYS-295; LYS-304; LYS-435 AND LYS-440, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: The 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. {ECO:0000250|UniProtKB:P11181}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-methylpropanoyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-
CC         [protein] = CoA + N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-
CC         lysyl-[protein]; 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         Evidence={ECO:0000250|UniProtKB:P11181};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18866;
CC         Evidence={ECO:0000250|UniProtKB:P11181};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000250|UniProtKB:P11181};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000250|UniProtKB:P11181};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry that represents the E2 component of the branched-chain alpha-
CC       ketoacid dehydrogenase (BCKDH) complex. The BCKDH complex is composed
CC       of three major building blocks E1, E2 and E3. It is organized around
CC       E2, a 24-meric cubic core composed of DBT, to which are associated 6 to
CC       12 copies of E1, and approximately 6 copies of the dehydrogenase E3, a
CC       DLD dimer (By similarity). Interacts with PPM1K with a 24:1
CC       stoichiometry; the N-terminal region (residues 49-61) of PPM1K and C-
CC       terminal linker of the lipoyl domain of DBT/E2 (residues 145-160) are
CC       critical for this interaction whereas the lipoyl prosthetic group is
CC       dispensable. This interaction requires colocalization in mitochondria
CC       (By similarity). PPM1K competes with BCKDK for binding to DBT; this
CC       interaction is modulated by branched-chain alpha-keto acids (BCKAs). At
CC       steady state, BCKDH holoenzyme preferentially binds BCKDK and BCKDHA is
CC       phosphorylated. In response to high levels of BCKAs, BCKDK is replaced
CC       by PPM1K leading to BCKDHA dephosphorylation (By similarity).
CC       {ECO:0000250|UniProtKB:P11182, ECO:0000250|UniProtKB:P12694}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P11181}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; L42996; AAC37681.1; -; mRNA.
DR   EMBL; AK165959; BAE38487.1; -; mRNA.
DR   EMBL; CH466532; EDL12381.1; -; Genomic_DNA.
DR   CCDS; CCDS17787.1; -.
DR   PIR; S65760; S65760.
DR   RefSeq; NP_034152.2; NM_010022.3.
DR   AlphaFoldDB; P53395; -.
DR   SMR; P53395; -.
DR   BioGRID; 199061; 24.
DR   IntAct; P53395; 6.
DR   MINT; P53395; -.
DR   STRING; 10090.ENSMUSP00000000349; -.
DR   GlyGen; P53395; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P53395; -.
DR   PhosphoSitePlus; P53395; -.
DR   SwissPalm; P53395; -.
DR   EPD; P53395; -.
DR   jPOST; P53395; -.
DR   MaxQB; P53395; -.
DR   PaxDb; 10090-ENSMUSP00000000349; -.
DR   PeptideAtlas; P53395; -.
DR   ProteomicsDB; 293918; -.
DR   Pumba; P53395; -.
DR   Antibodypedia; 19986; 213 antibodies from 25 providers.
DR   DNASU; 13171; -.
DR   Ensembl; ENSMUST00000000349.11; ENSMUSP00000000349.7; ENSMUSG00000000340.11.
DR   GeneID; 13171; -.
DR   KEGG; mmu:13171; -.
DR   UCSC; uc008rcg.2; mouse.
DR   AGR; MGI:105386; -.
DR   CTD; 1629; -.
DR   MGI; MGI:105386; Dbt.
DR   VEuPathDB; HostDB:ENSMUSG00000000340; -.
DR   eggNOG; KOG0558; Eukaryota.
DR   GeneTree; ENSGT00940000156750; -.
DR   HOGENOM; CLU_016733_10_0_1; -.
DR   InParanoid; P53395; -.
DR   OMA; MPFCIKA; -.
DR   OrthoDB; 1399at2759; -.
DR   PhylomeDB; P53395; -.
DR   TreeFam; TF314182; -.
DR   Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-MMU-70895; Branched-chain amino acid catabolism.
DR   Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR   BioGRID-ORCS; 13171; 3 hits in 79 CRISPR screens.
DR   ChiTaRS; Dbt; mouse.
DR   PRO; PR:P53395; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; P53395; Protein.
DR   Bgee; ENSMUSG00000000340; Expressed in brown adipose tissue and 264 other cell types or tissues.
DR   ExpressionAtlas; P53395; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISO:MGI.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; ISO:MGI.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; ISO:MGI.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 4.10.320.10; E3-binding domain; 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   PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR   PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
DR   Genevisible; P53395; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Lipoyl; Mitochondrion; Phosphoprotein;
KW   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_0000020490"
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          145..160
FT                   /note="Critical for association with PPM1K"
FT                   /evidence="ECO:0000250|UniProtKB:P11182"
FT   REGION          217..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..239
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        452
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000255"
FT   BINDING         291
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         306
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         349
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         378
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         399
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         400
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         403
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         424
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   BINDING         426
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250|UniProtKB:P11181"
FT   MOD_RES         105
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11181,
FT                   ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         133
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         196
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         196
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         202
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11182"
FT   MOD_RES         243
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         250
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         261
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         289
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         289
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         295
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         304
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         435
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         440
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         440
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        369..371
FT                   /note="EIA -> GIG (in Ref. 1; AAC37681)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   482 AA;  53247 MW;  79E440D1B4B9B948 CRC64;
     MAAARVLRTW SQNAVRLTCV RYFQTFNSAR VLKPKCVCSV GYPLFKYSQP RHSLRTAAVL
     QGQVVQFKLS DIGEGIREVT IKEWYVKEGD TVSQFDSICE VQSDKASVTI TSRYDGVIKR
     LYYNLDDIAY VGKPLIDIET EALKDSEEDV VETPAVSHDE HTHQEIKGQK TLATPAVRRL
     AMENNIKLSE VVGSGKDGRI LKEDILSFLE KQTGAILPPS PKSEITPPPP QPKDRTFPTP
     IAKPPVFTGK DRTEPVTGFQ KAMVKTMSAA LKIPHFGYCD EIDLTQLVKL REELKPVALA
     RGIKLSFMPF FLKAASLGLL QFPILNASVD ENCQNITYKA SHNIGIAMDT ELGLIVPNVK
     NVQVRSVFEI AMELNRLQKL GSSGQLGTTD LTGGTFTLSN IGSIGGTYAK PVILPPEVAI
     GALGAIKALP RFDQKGDVYK AQIMNVSWSA DHRVIDGATM SRFSNLWKSY LENPAFMLLD
     LK
//