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Database: UniProt
Entry: A0A2J6QJP1_9HELO
LinkDB: A0A2J6QJP1_9HELO
Original site: A0A2J6QJP1_9HELO 
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
//
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