ODB2_MOUSE
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 03-AUG-2022, entry version 172.
DE RecName: Full=Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial;
DE EC=2.3.1.168;
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, Pancreas,
RC 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.
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; Evidence={ECO:0000250};
CC Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
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; 19.
DR IntAct; P53395; 6.
DR MINT; P53395; -.
DR STRING; 10090.ENSMUSP00000000349; -.
DR iPTMnet; P53395; -.
DR PhosphoSitePlus; P53395; -.
DR SwissPalm; P53395; -.
DR EPD; P53395; -.
DR jPOST; P53395; -.
DR MaxQB; P53395; -.
DR PaxDb; P53395; -.
DR PeptideAtlas; P53395; -.
DR PRIDE; P53395; -.
DR ProteomicsDB; 293918; -.
DR Antibodypedia; 19986; 193 antibodies from 24 providers.
DR DNASU; 13171; -.
DR Ensembl; ENSMUST00000000349; ENSMUSP00000000349; ENSMUSG00000000340.
DR GeneID; 13171; -.
DR KEGG; mmu:13171; -.
DR UCSC; uc008rcg.2; mouse.
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; HPCIMAP; -.
DR OrthoDB; 854035at2759; -.
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 74 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 261 other tissues.
DR ExpressionAtlas; P53395; baseline and differential.
DR Genevisible; P53395; MM.
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 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 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 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 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: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
