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 24-JAN-2024, entry version 102.
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=3-methyl-2-oxobutanoate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] = CO2 +
CC N(6)-[(R)-S(8)-2-methylpropanoyldihydrolipoyl]-L-lysyl-
CC [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase];
CC Xref=Rhea:RHEA:13457, Rhea:RHEA-COMP:10488, Rhea:RHEA-COMP:10489,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC 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 STRING; 44689.Q55FN7; -.
DR PaxDb; 44689-DDB0230185; -.
DR EnsemblProtists; EAL73463; EAL73463; DDB_G0268020.
DR GeneID; 8616303; -.
DR KEGG; ddi:DDB_G0268020; -.
DR dictyBase; DDB_G0268020; bkdB.
DR eggNOG; KOG0525; Eukaryota.
DR HOGENOM; CLU_012907_1_0_1; -.
DR InParanoid; Q55FN7; -.
DR OMA; SEAYYMA; -.
DR PhylomeDB; Q55FN7; -.
DR Reactome; R-DDI-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR PRO; PR:Q55FN7; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:UniProtKB.
DR GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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
//
