ID   ODBB_RAT                Reviewed;         390 AA.
AC   P35738;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   02-SEP-2026, entry version 166.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, mitochondrial {ECO:0000250|UniProtKB:P21953};
DE            EC=1.2.4.4 {ECO:0000250|UniProtKB:P21953};
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component beta chain;
DE            Short=BCKDE1B;
DE            Short=BCKDH E1-beta;
DE   Flags: Precursor;
GN   Name=Bckdhb {ECO:0000312|RGD:2197};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-230.
RG   The MGC Project Team;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-390, AND PROTEIN SEQUENCE OF 49-75.
RX   PubMed=1390893;
RA   Zhao Y., Kuntz M.J., Harris R.A., Crabb D.W.;
RT   "Molecular cloning of the E1 beta subunit of the rat branched chain alpha-
RT   ketoacid dehydrogenase.";
RL   Biochim. Biophys. Acta 1132:207-210(1992).
RN   [4]
RP   ERRATUM OF PUBMED:1390893.
RX   PubMed=7841205;
RA   Zhao Y., Kuntz M.J., Harris R.A., Crabb D.W.;
RL   Biochim. Biophys. Acta 1260:243-243(1995).
CC   -!- FUNCTION: Together with BCKDHA forms the heterotetrameric E1 subunit of
CC       the mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD)
CC       complex. The BCKD complex catalyzes the multi-step oxidative
CC       decarboxylation of alpha-ketoacids derived from the branched-chain
CC       amino-acids valine, leucine and isoleucine producing CO2 and acyl-CoA
CC       which is subsequently utilized to produce energy. The E1 subunit
CC       catalyzes the first step with the decarboxylation of the alpha-ketoacid
CC       forming an enzyme-product intermediate. A reductive acylation mediated
CC       by the lipoylamide cofactor of E2 extracts the acyl group from the E1
CC       active site for the next step of the reaction.
CC       {ECO:0000250|UniProtKB:P21839}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 3-methyl-2-oxobutanoate
CC         + H(+) = N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC         [protein] + CO2; Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10474,
CC         Rhea:RHEA-COMP:10497, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83142; EC=1.2.4.4;
CC         Evidence={ECO:0000250|UniProtKB:P21839};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13458;
CC         Evidence={ECO:0000250|UniProtKB:P21839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 4-methyl-2-oxopentanoate
CC         + H(+) = N(6)-[(R)-S(8)-3-methylbutanoyldihydrolipoyl]-L-lysyl-
CC         [protein] + CO2; Xref=Rhea:RHEA:84639, Rhea:RHEA-COMP:10474,
CC         Rhea:RHEA-COMP:20408, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17865, ChEBI:CHEBI:83099, ChEBI:CHEBI:233973;
CC         Evidence={ECO:0000250|UniProtKB:P21839};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84640;
CC         Evidence={ECO:0000250|UniProtKB:P21839};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + (S)-3-methyl-2-
CC         oxopentanoate + H(+) = N(6)-{(R)-S(8)-[(2S)-2-
CC         methylbutanoyl]dihydrolipoyl}-L-lysyl-[protein] + CO2;
CC         Xref=Rhea:RHEA:84643, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:20409,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:35146,
CC         ChEBI:CHEBI:83099, ChEBI:CHEBI:233974;
CC         Evidence={ECO:0000250|UniProtKB:P21839};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:84644;
CC         Evidence={ECO:0000250|UniProtKB:P21839};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P21953};
CC   -!- SUBUNIT: Heterotetramer of 2 alpha/BCKDHA and 2 beta chains/BCKDHB that
CC       forms the branched-chain alpha-keto acid decarboxylase (E1) component
CC       of the BCKD complex. The branched-chain alpha-ketoacid dehydrogenase is
CC       a large complex composed of three major building blocks E1, E2 and E3.
CC       It is organized around E2, a 24-meric cubic core composed of DBT, to
CC       which are associated 6 to 12 copies of E1, and approximately 6 copies
CC       of the dehydrogenase E3, a DLD dimer. {ECO:0000250|UniProtKB:P21953}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P21953}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA73899.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA73899.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR   EMBL; AABR03062593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03062720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03063125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR03063398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M94040; AAA73899.1; ALT_SEQ; mRNA.
DR   PIR; S28950; S28950.
DR   RefSeq; NP_062140.1; NM_019267.1.
DR   AlphaFoldDB; P35738; -.
DR   SMR; P35738; -.
DR   BioGRID; 248328; 2.
DR   CORUM; P35738; -.
DR   FunCoup; P35738; 1135.
DR   IntAct; P35738; 1.
DR   STRING; 10116.ENSRNOP00000013249; -.
DR   PhosphoSitePlus; P35738; -.
DR   PaxDb; 10116-ENSRNOP00000013249; -.
DR   Ensembl; ENSRNOT00000013249.8; ENSRNOP00000013249.7; ENSRNOG00000009928.8.
DR   Ensembl; ENSRNOT00060036386; ENSRNOP00060029951; ENSRNOG00060020994.
DR   GeneID; 29711; -.
DR   KEGG; rno:29711; -.
DR   UCSC; RGD:2197; rat.
DR   AGR; RGD:2197; -.
DR   CTD; 594; -.
DR   RGD; 2197; Bckdhb.
DR   eggNOG; KOG0525; Eukaryota.
DR   GeneTree; ENSGT00940000156533; -.
DR   InParanoid; P35738; -.
DR   OMA; SEAYYMA; -.
DR   OrthoDB; 878at2759; -.
DR   PhylomeDB; P35738; -.
DR   BRENDA; 1.2.4.4; 5301.
DR   Reactome; R-RNO-70895; Branched-chain amino acid catabolism.
DR   Reactome; R-RNO-9859138; BCKDH synthesizes BCAA-CoA from KIC, KMVA, KIV.
DR   SABIO-RK; P35738; -.
DR   PRO; PR:P35738; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   ExpressionAtlas; P35738; baseline and differential.
DR   GO; GO:0160157; C:branched-chain alpha-ketoacid dehydrogenase complex; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:HGNC-UCL.
DR   GO; GO:0003863; F:branched-chain 2-oxo acid dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0120552; P:branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA; ISS:UniProtKB.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:HGNC-UCL.
DR   GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   FunFam; 3.40.50.920:FF:000004; 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial; 1.
DR   FunFam; 3.40.50.970:FF:000001; Pyruvate dehydrogenase E1 beta subunit; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Lipid metabolism; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Potassium; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..390
FT                   /note="2-oxoisovalerate dehydrogenase subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000020471"
FT   BINDING         150
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /ligand_note="ligand shared with alpha subunit"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         176
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         178
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         179
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         226
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         229
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         231
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   MOD_RES         230
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P3A8"
FT   MOD_RES         239
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   CONFLICT        255
FT                   /note="K -> R (in Ref. 3; AAA73899)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303
FT                   /note="R -> T (in Ref. 3; AAA73899)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   390 AA;  42823 MW;  7A562A868823A1BF CRC64;
     MAAVAARAGG LLRLGAAGAE RRRRGLRCAA LVQGFLQPAV DDASQKRRVA HFTFQPDPES
     LQYGQTQKMN LFQSITSALD NSLAKDPTAV IFGEDVAFGG VFRCTVGLRD KYGKDRVFNT
     PLCEQGIVGF GIGIAVTGAT AIAEIQFADY IFPAFDQIVN EAAKYRYRSG DLFNCGSLTI
     RAPWGCVGHG ALYHSQSPEA FFAHCPGIKV VIPRSPFQAK GLLLSCIEDK NPCIFFEPKI
     LYRAAVEQVP VEPYKIPLSQ AEVIQEGSDV TLVAWGTQVH VIREVASMAQ EKLGVSCEVI
     DLRTIVPWDV DTVCKSVIKT GRLLISHEAP LTGGFASEIS STVQEECFLN LEAPISRVCG
     YDTPFPHIFE PFYIPDKWKC YDALRKMINY
//