ID   A0A2T4AS26_TRIHA        Unreviewed;       607 AA.
AC   A0A2T4AS26;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:PTB59874.1};
GN   ORFNames=M431DRAFT_71053 {ECO:0000313|EMBL:PTB59874.1};
OS   Trichoderma harzianum CBS 226.95.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983964 {ECO:0000313|EMBL:PTB59874.1, ECO:0000313|Proteomes:UP000241690};
RN   [1] {ECO:0000313|EMBL:PTB59874.1, ECO:0000313|Proteomes:UP000241690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 226.95 {ECO:0000313|EMBL:PTB59874.1,
RC   ECO:0000313|Proteomes:UP000241690};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; KZ679675; PTB59874.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4AS26; -.
DR   STRING; 983964.A0A2T4AS26; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000241690; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF138; DEHYDROGENASE PKFF-RELATED; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241690};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..607
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015604438"
FT   DOMAIN          307..321
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         588..589
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   607 AA;  64898 MW;  21D8766741DDCF8C CRC64;
     MAKSKALAVL AAISRCGLVI AAPLETAPDL TFDYVVVGGG PGGLTVATRL SEDPNVSVAI
     IEAGTWSQSV TGNQSQVPAY DFFYNGKSAN DTNPLVEWDF VTSPQAGING QSVHYTRAKS
     LGGCTNLNYM GYTQTAKGAL QKWADTVGDS SYAWETASKY YKKSLNFTGA IENRDLRNVT
     TSESPGSISV DGPLHVSYAS WAQSFSTWVA LAMDSEGIPS TDAFINGNLN GSSWLTSTIN
     PTNGHRESAA TAYLQPVLSR QNLKVFDLTL GERILFDANK TAVGVQVTTG NQTYTLNAKR
     EVIVSGGTFM SPQLLQVSGV GPADLLKKHN IPVVADRPGV GQNMGDHVFF GIAYRVNLET
     ATSLEDPATM LQAEDQFNRD GTGPLSSPGG DYAGYEKIPQ SLRSSFSAAT LEELAEVPAD
     WPEMQYLTLP TFVGDFESAT AASPDDGFKY ATLLATLIAP SSLGNVTIAS PNMSDKPIIN
     PNWLTTQRDI ELVVAGFKRI RQILEAPVMG NITIGPEYYP GSAVQTDDEI HAQVQTSFNT
     MYHASASCRM GKSSDPDAVV DTHARVYGVK NLRVVDASAF PFVLPGLPQA SVYMLAEKIA
     DDIKNGN
//