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Database: UniProt
Entry: A0A161WF92_9PEZI
LinkDB: A0A161WF92_9PEZI
Original site: A0A161WF92_9PEZI 
ID   A0A161WF92_9PEZI        Unreviewed;       431 AA.
AC   A0A161WF92;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) {ECO:0000256|ARBA:ARBA00012277};
DE            EC=1.2.4.4 {ECO:0000256|ARBA:ARBA00012277};
DE   Flags: Fragment;
GN   ORFNames=CI238_06478 {ECO:0000313|EMBL:KZL83128.1};
OS   Colletotrichum incanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum spaethianum species complex.
OX   NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL83128.1, ECO:0000313|Proteomes:UP000076584};
RN   [1] {ECO:0000313|EMBL:KZL83128.1, ECO:0000313|Proteomes:UP000076584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL83128.1,
RC   ECO:0000313|Proteomes:UP000076584};
RA   Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA   Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA   Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA   O'Connell R.J.;
RT   "Survival trade-offs in plant roots during colonization by closely related
RT   pathogenic and mutualistic fungi.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00043720};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13458;
CC         Evidence={ECO:0000256|ARBA:ARBA00043720};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KZL83128.1}.
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DR   EMBL; LFIW01001209; KZL83128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161WF92; -.
DR   STRING; 1573173.A0A161WF92; -.
DR   Proteomes; UP000076584; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProt.
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   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT   DOMAIN          107..283
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KZL83128.1"
SQ   SEQUENCE   431 AA;  47322 MW;  853EF1E7AC9EBA66 CRC64;
     LAGRPQFHLW HPSNLGIDCS WHFLWFSFSF TMRSSISIRP LRRALAPSAS TQLPLAASRL
     YSTHPPNAKL NIPVDYATTS LLAHSSQTAL STAELPAEVR NGTTKKMNLF QAINDALSIA
     LAEDDSVMVF GEDVAFGGVF RCTMKLAETY GADRIFNTPL TEQGIMGFAI GAAAEGMRPV
     AEIQFADYIY PAFDQLVNEA AKYRYRDGAC GRSVGGLTVR MPCGGVGHGA LYHSQSPESL
     FTHIPGLRVI MPRSPLQAKG LLLSAIRSND PCIFMEPKIL YRAAVEQVPA GAYTLPLSKA
     EVLKEGKDVT IISYGQPLYT CMSAIRRAEE DLGISVELID LRTLYPWDKE TVLESVRKTG
     HCIVVHEAMV NAGIGAEVAA TIQEDPDTFL RLEAPVARVA GWSIHTPLLY EKFNIPDVAR
     VYDNIKRVLD Y
//
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