ID   ODBB_DICDI              Reviewed;         370 AA.
AC   Q55FN7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   02-SEP-2026, entry version 111.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, mitochondrial;
DE            EC=1.2.4.4 {ECO:0000250|UniProtKB:P21953};
DE   AltName: Full=3-methyl-2-oxobutanoate dehydrogenase;
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=bkdB; ORFNames=DDB_G0268020;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
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) (By similarity).
CC       {ECO:0000250|UniProtKB:P21953}.
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:P21953};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13458;
CC         Evidence={ECO:0000250|UniProtKB:P21953};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P21953};
CC   -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta chains.
CC       {ECO:0000250|UniProtKB:P21953}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P21953}.
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DR   EMBL; AAFI02000003; EAL73463.1; -; Genomic_DNA.
DR   RefSeq; XP_647496.1; XM_642404.1.
DR   AlphaFoldDB; Q55FN7; -.
DR   SMR; Q55FN7; -.
DR   FunCoup; Q55FN7; 149.
DR   STRING; 44689.Q55FN7; -.
DR   PaxDb; 44689-Q55FN7; -.
DR   GeneID; 8616303; -.
DR   KEGG; ddi:DDB_G0268020; -.
DR   dictyBase; DDB_G0268020; bkdB.
DR   VEuPathDB; AmoebaDB:DDB_G0268020; -.
DR   eggNOG; KOG0525; Eukaryota.
DR   HOGENOM; CLU_012907_1_0_1; -.
DR   InParanoid; Q55FN7; -.
DR   OMA; SEAYYMA; -.
DR   PhylomeDB; Q55FN7; -.
DR   Reactome; R-DDI-9859138; BCKDH synthesizes BCAA-CoA from KIC, KMVA, KIV.
DR   PRO; PR:Q55FN7; -.
DR   Proteomes; UP000002195; Chromosome 1.
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:0003863; F:branched-chain 2-oxo acid dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; ISS:UniProtKB.
DR   GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
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   3: Inferred from homology;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Potassium;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..25
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..370
FT                   /note="2-oxoisovalerate dehydrogenase subunit beta,
FT                   mitochondrial"
FT                   /id="PRO_0000327589"
FT   BINDING         130
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         156
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         158
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         159
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
FT   BINDING         209
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="structural"
FT                   /evidence="ECO:0000250|UniProtKB:P21953"
SQ   SEQUENCE   370 AA;  40725 MW;  083E690721B9559D CRC64;
     MLRGNNIKKV NSLLVRSFHS TVGNRSGGPS TPINYPSLEI ENAGEKQKMN LFQAINNGMD
     IAMQKDSKAV VFGEDVGFGG VFRCTVGLRD KYGASRVFNT PLCEQGIAGF AIGLAAQGAT
     PIAEIQFADY IFPAFDQIVN EAAKYRYRSG GQFDCGSLTI RSPYGAVGHG GHYHSQSPES
     YFGHTPGLKV VIPSTPIEAK GLLLASIREK DPVIFFEPKL MYRSAVEEVP IGDYEIPLGK
     ARIVKEGKDI TIIGWGAQMR VLLQAVNMAE EKLGISCELI DLRTIQPWDV ETVVESVKKT
     GRVVISHEAP KTGGWAAEIS ATIQERCFLH LEAPIQRVCG YDTPFPLIFE KFYVPDHLKN
     FESIKKTMVY
//