ID   A0A2P4ZU49_9HYPO        Unreviewed;      1006 AA.
AC   A0A2P4ZU49;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:PON27825.1};
GN   ORFNames=TGAM01_v203592 {ECO:0000313|EMBL:PON27825.1};
OS   Trichoderma gamsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=398673 {ECO:0000313|EMBL:PON27825.1, ECO:0000313|Proteomes:UP000054821};
RN   [1] {ECO:0000313|EMBL:PON27825.1, ECO:0000313|Proteomes:UP000054821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6085 {ECO:0000313|EMBL:PON27825.1,
RC   ECO:0000313|Proteomes:UP000054821};
RX   PubMed=26893428;
RA   Baroncelli R., Zapparata A., Piaggeschi G., Sarrocco S., Vannacci G.;
RT   "Draft Whole-Genome Sequence of Trichoderma gamsii T6085, a Promising
RT   Biocontrol Agent of Fusarium Head Blight on Wheat.";
RL   Genome Announc. 4:e01747-15(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533}.
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:PON27825.1}.
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DR   EMBL; JPDN02000009; PON27825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P4ZU49; -.
DR   STRING; 398673.A0A2P4ZU49; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000054821; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
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   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
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   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054821}.
FT   DOMAIN          690..704
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   MOD_RES         288
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   1006 AA;  109657 MW;  2D73895764E3BF60 CRC64;
     MSERSFTELA QKVLDHCVLE RQNIPSQPIV KVIPWDKERD IGNIARPPQF PASIDTTLSN
     AETIFGYRVR MDHPKFFGFI PSPASDLSWL GEVLNSAYNT HAGSWFQSSG PSAIEKHFLS
     WLTRDIIGYP ETAGGCFVSG GSMANLSALM LARDQKLSLE ERNKAVAYTS SQTHSSLAKG
     LAILGFYPAQ IRKVACDDSM RIDTTLLRSA IEQDKAAGRI PFLIVGNAGT TNTGTVDPFT
     ELAAISREQN LWLHADGAYG ASALLCQARR AILNGVELCD SISWDAHKWL FQTYGCGMVL
     VRHRKFLTES FGTTAEYTQD AAETAESLPN FWNYGPELTR PARAMKLWFS FQLLGLDAID
     KAINRGFELA EIAQSSLERL KDWDILSPAQ MGIICFRFHP PHVPAASLDG LNMKISQKAI
     ENNVAAPLTT RIREVLVVVG GGTAGSALAT RLSQGLPNKS ILLIEAGPEA LDEDRINIPG
     MKGSTLGTIY DWNFTTVPQN ALNGRVLGAN RGKVLGGSSA LNLMTWDRSS SEEYDGWERL
     GNPSWNWENM ITAMEMVETF TGINTSSYGD QGVGTSGPIH TVINRVIPAQ QDLWLQSMAD
     LGIPHNLNSL GGNPIGYMNQ PSNVDPRTWA RSYAANSYIP AAGKNLHLLL GARVAKVNLR
     KGQSSYTAIG VTLQDGTVIQ ATREVILSCG TIQSPGLLEL SGIGNKAVLL KAGVDQIIDL
     DGVGENLQDH VRYQASYQLK DNFTSFDILK YNATYAAAQL ALWRAKQPSL YDYTGSGYGY
     LNWHQVVGSL ATKLNSLAQH VVLSLGSIVD KRKLQYIGSL LSPQVEIIFS DGYTGVKGYP
     ANGSSLYGKG FFTLIGVVMH PLSRGTIHIT SMDIDATPQI DPQYLSNEYD VQAAIEAAKY
     CRKIANSAPL SSAWVTEYEP GGAVQTDEDW RQYVLNTTLS IYHPVGTCAM LPQRDGGVVS
     PELIVYGTTN LRVVDASIIP VLPSAHIQTA VYGIAERAAR MIIQDS
//