ID   A0A1Y2WHU8_9PEZI        Unreviewed;       782 AA.
AC   A0A1Y2WHU8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OTB08536.1};
GN   ORFNames=M426DRAFT_317160 {ECO:0000313|EMBL:OTB08536.1};
OS   Hypoxylon sp. CI-4A.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX   NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB08536.1, ECO:0000313|Proteomes:UP000242955};
RN   [1] {ECO:0000313|EMBL:OTB08536.1, ECO:0000313|Proteomes:UP000242955}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CI-4A {ECO:0000313|EMBL:OTB08536.1,
RC   ECO:0000313|Proteomes:UP000242955};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; KZ111526; OTB08536.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2WHU8; -.
DR   STRING; 1001833.A0A1Y2WHU8; -.
DR   InParanoid; A0A1Y2WHU8; -.
DR   OrthoDB; 2291769at2759; -.
DR   Proteomes; UP000242955; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd02002; TPP_BFDC; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR045229; TPP_enz.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000242955};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          204..334
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          408..512
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          618..775
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  84232 MW;  F4182FAF39D7D360 CRC64;
     MLRRRLGIPL TPPRSSAAPP PIRVSTPISL LPTPPQEYYR VDDLPQCLYV SKPTGAALKQ
     RYALSIQSIQ SIQSIPSSWT ETAPPSSACS RYGGAPLGNN SLVSHGTTNG KPICESCNGQ
     ASISSAHHKR SSTWYKAAIP ATNTTRNLAF AARPYSTKAL KQLASNSPAS LTSFTRRQVA
     LDVFKTQQQR VLSTSTSTPA MYTASFAFFE AIWEAGITHC FVNLGSDHPS IIEAMVKGQR
     ENKGNFPRII TCPNEMVAMS MADGYARLTG KPQCVIVHVD VGTQGLGAAV HNASTGRAPV
     FVFAGLSPFT LEGEMRGSRT EYIHWIQNVP DQTQIIGQYC RYAGEIKTGK NIKQMVNRAL
     QFATSAPQGP VYLVGAREVM EEEINPYSLE QGVWDSVELG GLTPGAPKEI AEALLGAEHP
     LLITGYAGRN EKIPDALVEL ANTVKGLRVL DTGGSDMCFP ASHPGWLGLR FGVEPAIEKS
     DVIIILDCDV PWIPTHNKPK DGTKVYHIDV DPLKQLMPLF YVPAQHRYRA DPLVAVQQIT
     SEAKEQAGKL DATILTKKWD ALQASHKERL GAIVAKTTPA EDGSFGTGYL SKTLRALCPE
     DTIWAIEAVT NTAFVHDNLQ PELAKSWINC GGGGLGWSGG GALGIKLATD AENGGKGKFV
     VQIVGDGTFL FSVPGSVYWI SRRYNIPVLT VVLNNKGWNA PRKSMLLVHP EGLGSTATNE
     EINISFDPVP DYSGIAKAAA GGDLFAAKVE KVEDLERTIK EAIKAVEGGQ SAVLDCKVTL
     NC
//