ID   D4DFT9_TRIVH            Unreviewed;       416 AA.
AC   D4DFT9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit, putative {ECO:0000313|EMBL:EFE39315.1};
GN   ORFNames=TRV_06041 {ECO:0000313|EMBL:EFE39315.1};
OS   Trichophyton verrucosum (strain HKI 0517).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39315.1, ECO:0000313|Proteomes:UP000008383};
RN   [1] {ECO:0000313|Proteomes:UP000008383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
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:EFE39315.1}.
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DR   EMBL; ACYE01000341; EFE39315.1; -; Genomic_DNA.
DR   RefSeq; XP_003019939.1; XM_003019893.1.
DR   AlphaFoldDB; D4DFT9; -.
DR   GeneID; 9584690; -.
DR   KEGG; tve:TRV_06041; -.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   OrthoDB; 166915at2759; -.
DR   Proteomes; UP000008383; Unassembled WGS sequence.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
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; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Pyruvate {ECO:0000313|EMBL:EFE39315.1}.
FT   DOMAIN          80..385
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   416 AA;  46587 MW;  A176EAA4781F67F9 CRC64;
     MFSRLIRARG VAQVGRQPST QLFRRSVTTD AASAHAEDIP VEDDKPFSVK LSDESFETYE
     LDPPPYTLKT TKKELKQMYY DMVSIRRMEM AADRLYKEKK IRGFCHLSTG QEAVATGIEH
     AITPDDKLIT AYRCHGFAMM RGGTVRSIIG ELLGRREGIA YGKGGSMHMF AKNFFGGNGI
     VGAQVPVGAG LAFAQQYNGE ANTTICLYGD GASNQGQVFE AFNMAKLWNL PVIFGCESTF
     QIVFYPFLDN KYGMGTAANR SSALTDYYKR GQYIPGIKIN GMDVLAIKAA VQYGREYTVS
     GQGPLVFEYV TYRYGGHSMS DPGTTYRTRE EIQRMRSTND PIAGLKQKLL DWNITSEEEL
     KAIDKDARSM VDEEVAIAEK MPVPDATSRI LFEDIYVRGS EPKWMRGRTA DETFYY
//