ID   ODBB_CHATD              Reviewed;         469 AA.
AC   P9WF02; G0SA92;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit beta, mitochondrial {ECO:0000250|UniProtKB:P21953};
DE            EC=1.2.4.4 {ECO:0000250|UniProtKB:P21953};
DE   Flags: Precursor;
GN   ORFNames=CTHT_0041430, CTHT_0041430-1;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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). {ECO:0000250|UniProtKB:P21953}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue (2-
CC         methylpropanoyl)transferase] + 3-methyl-2-oxobutanoate + H(+) = (R)-
CC         N(6)-(S(8)-2-methylpropanoyldihydrolipoyl)-L-lysyl-
CC         [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] + CO2;
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   -!- SUBUNIT: Heterotetramer of 2 alpha and 2 beta chains.
CC       {ECO:0000250|UniProtKB:P21953}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGS19664.1; Type=Erroneous gene model prediction; Note=The predicted gene CTHT_0041430 has been split into 2 genes: CTHT_0041430-1 and CTHT_0041430-2.; Evidence={ECO:0000305};
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DR   EMBL; GL988043; EGS19664.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_006694549.1; XM_006694486.1.
DR   AlphaFoldDB; P9WF02; -.
DR   SMR; P9WF02; -.
DR   GeneID; 18258181; -.
DR   KEGG; cthr:CTHT_0041430; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.920; -; 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   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 1.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR   PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE   3: Inferred from homology;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..40
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           41..469
FT                   /note="2-oxoisovalerate dehydrogenase subunit beta,
FT                   mitochondrial"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000450358"
SQ   SEQUENCE   469 AA;  50998 MW;  9EEB2BBC99C13B42 CRC64;
     MKRSTVVIRP SARALSRQAS SQSFLLARSS ALTSRQRRLY STHPPNARLN LPIDYATTPL
     LAHTSQAALS NPELPASVRN GTTKRMNLFQ AINDALSTAL AEDESVLIFG EDVAFGGVFR
     CTTKLAETYG GDRVFNTPLT EQGIMGFAIG AAAEGMRPVA EIQFADYVFP AFDQLVNEAA
     KFRYRDGAGG RSAGGLTVRM PCGGVGHGAL YHSQSPEALF THIPGLKVII PRGPVQAKGL
     LLAAIRSNDP CVVMEPKILY RAAVEQVPTT AYELPLGKAE ILKEGKDVTV VSYGQPLYKC
     MAALKAAEQD FGVSVELIDL RTIYPWDKET VFNSVRKTGR CVVVHEAMVN AGVGAEVAAA
     IQEDPETFVR LEAPVARIAG WSIPTPLVFE QFNLPDVTSK CYLTLGLADV YADGMPRDIR
     RHQKGDEFLR DLSMNSGILK QSMLHSSRRG VDWLMGIVLD DIILSVFLV