ID A0A2J6QJP1_9HELO Unreviewed; 605 AA.
AC A0A2J6QJP1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:PMD26492.1};
GN ORFNames=NA56DRAFT_591037 {ECO:0000313|EMBL:PMD26492.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD26492.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD26492.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD26492.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-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; KZ613467; PMD26492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6QJP1; -.
DR STRING; 1745343.A0A2J6QJP1; -.
DR OrthoDB; 2392848at2759; -.
DR Proteomes; UP000235672; 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:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000235672}.
FT DOMAIN 281..295
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 139..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 537..538
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 605 AA; 65992 MW; 823247E43889CD26 CRC64;
MSTYDGSDVD IIFAGGGTAA CVAAGRLAKA NPDLKILLVE GGKNNYNDPT VTNPAVYLSH
LAPDSKTALF YKSKASQHLN GREAIVPMGG LLGGGSSINF MMYTRAQGVD FDSWDTDGWR
AEDMIPLCNK LETYHSKGAN TDQSKHGHDG PIHISDGGFR GKSEQEFSKT VQGMGYQMIE
DLQDFEAVGG FSHWQRYVSP DGKRQDAAHC YIHPLLQDGN HPNLHILTDS KVIRVLFDES
TPPRAIGIEY KPSGEHQPQT SLSKPVHKTI KANKLVVVSA GALGTPQILE RSGVGNADHL
KQVGVSVVAD VPGVGEQYQD HHLLLYPYRT KNLNDEETLD GILSGRKDFV KALTGKDPML
GWNGIDICAK LRPSDQDIEK LGPDFKRDWD NDFKSVPTKP LILCGVVNAF LADPSLVEPG
QYVTMGTYTA YPYSRGNIHI TDKENVVDGY EFDTGFLNHP TDLKKQLWGY KMSREIARRL
PYYSGELELG HPKFPAGSKA ALSTSAHPEG EVKDIEYSKE DDEAIEDWIR GNLNTTWHSL
GTCAMRPKEK GGVVDKELSV YGTAGLKVAD LSIVPENVGA NTNNTALAVG EKAAVIIGNE
LGIKV
//