ID J5K0J6_BEAB2 Unreviewed; 451 AA.
AC J5K0J6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=BBA_03556 {ECO:0000313|EMBL:EJP67776.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP67776.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP67776.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP67776.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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; JH725156; EJP67776.1; -; Genomic_DNA.
DR RefSeq; XP_008596875.1; XM_008598653.1.
DR AlphaFoldDB; J5K0J6; -.
DR STRING; 655819.J5K0J6; -.
DR GeneID; 19886568; -.
DR HOGENOM; CLU_029393_1_2_1; -.
DR InParanoid; J5K0J6; -.
DR OrthoDB; 952at2759; -.
DR Proteomes; UP000002762; 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:UP000002762};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU365014}.
FT DOMAIN 99..404
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 451 AA; 50513 MW; 0FDD0F76AA803B59 CRC64;
MRACMLQRVQ IRGAAAAARS RLSALGPVRA ASSVSQRPNS EFVQFPGALK SAFTHNLNFE
NPESYKALPT YRVVDQHGVV VDSSFTPDIS EEQVVKLYKD MLFISIMDLI MFDAQRQGRL
SFYMVSAGEE AVSVGTSSVL DPEDVVFCQY REQGLFKERG FTTKEFMSQL FSNRNDPGKG
RNMPIHYGSK KLNVHTISSP LATQLPQASG AGYALKLQKL QNPESKARVC AVFFGEGAAS
EGDFHAAMNI AATRSCPVIF ICRNNGYAIS TPTLEQYRGD GIASRGIGYG IDTIRVDGND
IWAVREATKK ARELALQDGG KPVLIEAMTY RVSHHSTSDD SFAYRARVEV EDWKRRDNPL
TRLRKWMEAK GYWDEAKEKE ARDALRKEVL REFSAAEKEK KPAIKTMFED VYAELTPGLK
AQMQELRELI DNYPDEYDVG EFEGGKETLK T
//
