ID   A0A1V6R4B7_9EURO        Unreviewed;       615 AA.
AC   A0A1V6R4B7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=PENSOL_c016G01632 {ECO:0000313|EMBL:OQD96294.1};
OS   Penicillium solitum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD96294.1, ECO:0000313|Proteomes:UP000191612};
RN   [1] {ECO:0000313|Proteomes:UP000191612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:OQD96294.1}.
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DR   EMBL; MDYO01000016; OQD96294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6R4B7; -.
DR   STRING; 60172.A0A1V6R4B7; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000191612; 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; 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   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; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191612}.
FT   DOMAIN          95..118
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          288..302
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         253
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         373
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   615 AA;  66452 MW;  0E8E43AD8F6AAF96 CRC64;
     MAENPTCTVE EFTRTTFDYV ICGGGTAGLV LAARLSENPA VTVGVIEAGK YRIGDPLVDT
     PAAFAQMFEN PDYDWCVYTT PQEGNHGLSH HVPRGKLLGG SSGINYMMYV RGSTQDYDNW
     AELVEDDGWS GEHMQGYMRK HETLEPIDPA ITDRSTMPFV GEFHGTSGPI RTSFNDSIMP
     VENDIIRACE DVTGIPKKPT DPWSGDHIGF YHTLGAVARS GPNKGKRSYS ARAYYEENRA
     TRPNLKVLCE ALVNRVVLDG NKATGVSLTH NGVEYQVSAR REVIVSGGTI QSPQILELSG
     IGDPEVLKAA GVECKIANKG VGANVLDHAL TFSVMEVQPG IITLDTLYQV PEAMEAATKQ
     YAETSGGPLS AVCSMQGFFP AKKILSEAEL AEIIQSIRDI KPNSAFHAKQ LAQTIANLES
     DHSANMQFVT LGGSINPDAI GHQGKIIQPR LPDEPAGLTL AVCIEYPVSR GTIHIGSADP
     TKPPIINPNY GGHPADISLL AAFLRWSDKV TESEYVKSSF LRRAYPDPSL NLQDMDTARE
     AVHDLIAGEY HISGSVAMGD ALDSRLRVKG VEGLRVVDAS VFPNNVSGNI VSSVYAVAEK
     ASDMIREDWD SRAGL
//