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Database: UniProt
Entry: A0A0D2DFQ8_9EURO
LinkDB: A0A0D2DFQ8_9EURO
Original site: A0A0D2DFQ8_9EURO 
ID   A0A0D2DFQ8_9EURO        Unreviewed;       455 AA.
AC   A0A0D2DFQ8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha {ECO:0000256|RuleBase:RU365014};
DE            EC=1.2.4.4 {ECO:0000256|RuleBase:RU365014};
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain {ECO:0000256|RuleBase:RU365014};
GN   ORFNames=PV06_06843 {ECO:0000313|EMBL:KIW41270.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW41270.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW41270.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW41270.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU365014}.
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:0000256|RuleBase:RU365014};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|RuleBase:RU365014};
CC   -!- SIMILARITY: Belongs to the BCKDHA family.
CC       {ECO:0000256|RuleBase:RU365014}.
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DR   EMBL; KN847337; KIW41270.1; -; Genomic_DNA.
DR   RefSeq; XP_016261486.1; XM_016408006.1.
DR   AlphaFoldDB; A0A0D2DFQ8; -.
DR   STRING; 215243.A0A0D2DFQ8; -.
DR   GeneID; 27358917; -.
DR   VEuPathDB; FungiDB:PV06_06843; -.
DR   HOGENOM; CLU_029393_1_2_1; -.
DR   OrthoDB; 952at2759; -.
DR   Proteomes; UP000053342; Unassembled WGS sequence.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU365014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT   DOMAIN          103..409
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   455 AA;  51147 MW;  CDD4DF048C7BF0C2 CRC64;
     MKTRAIIRPL LRGCRYREGV LLRRQGLRWA SDTWASGPAQ KAGAESVNFP GALNSSFTAT
     MKFHNPAEAT AMPTYRIMDA DGNIVDNTRD PQSASDEDVI RWYKNMLTVS IMDLIMFDAQ
     RQGRTSFYMV SAGEEGIAVG SASALIPEDV CFLQYREQGV LIQRGFTLKE MMSQLFANKD
     DHGKGRNMPV HYGSGKLNVH TISSPLATQI PQASGAAYAL KMQRLINPNI PPRIVACYFG
     EGAASEGDFH AALNIAATKS CPIVFVCRNN GFAISTASIE QYKGDGIASR GMGYGIDTIR
     VDGNDIFAVR EVMIEARKRA LEGNCKPILV EAMSYRVSHH STSDDSFAYR AKREVEEWKR
     RDNPITRLRK WMENKGIWDE DKEREARASI RKEVLREFSA AEKVKKPAIR EMFTDMYEEL
     TPEARNQMKQ LKEIIEKYPK EYDVSVHEGG VKTLE
//
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