ID A0A2J6T4A9_9HELO Unreviewed; 656 AA.
AC A0A2J6T4A9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:PMD57868.1};
GN ORFNames=K444DRAFT_653787 {ECO:0000313|EMBL:PMD57868.1};
OS Hyaloscypha bicolor E.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD57868.1, ECO:0000313|Proteomes:UP000235371};
RN [1] {ECO:0000313|EMBL:PMD57868.1, ECO:0000313|Proteomes:UP000235371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E {ECO:0000313|EMBL:PMD57868.1,
RC ECO:0000313|Proteomes:UP000235371};
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 (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; KZ613843; PMD57868.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6T4A9; -.
DR STRING; 1095630.A0A2J6T4A9; -.
DR InParanoid; A0A2J6T4A9; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000235371; 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:SF213; DEHYDROGENASE, PUTATIVE-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 Reference proteome {ECO:0000313|Proteomes:UP000235371};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..656
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014317045"
FT DOMAIN 363..377
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 656 AA; 71053 MW; B904B63384646994 CRC64;
MTSLLLFFIS VASFCNFFQS VEGVLPRGNT SSGPYLTDYD YIVVGSGPGG APLAARLGLA
GNKVLVIEAG SDVTTSDWNI TVPFFNAKAS EDPRINWAFY VNHYPTEEQN AKDPKYLYQL
ANGTLIEGPN PPADATPKGF LYPRSAAIGG CVNHNALIMM KPLDDDWSQI QSITGDAAWS
PANMSPYFEK FENCQYCSSG AAGHGFNGWL STNRAEESIF LGDPQVLSML NAASTVSANA
VGSTGGLNDS LARDLNAPAG YPTHQGLFNT PLNMNQYQRS SPRDFLVNTV QYLNTHPRVG
GKIDIRTDCL ATRVLFKPNS KQVIGVEFMD GQSLYRADPR ATSSSAGVLG TALTRKEVII
SAGTFNTPQL IKLSGIGPAD ELHKLGIPLV VDLPGVGQNL QDRYENGVIV NLTNPFSVFK
GCTQGADASD PCLVEWNTLQ SNKTKYATNG RPVAIPRRSS VALSTPNDMI ITGRPGYFAG
YFPGYSKIGA KFPNSWTWPV LKARTQNRAG NVTLASKDPR DVPSINFNYF SSGSGNWQYD
LAATVEGMQF ARSIIAQYVQ DTNSIINELV PGPGYETQEQ LTQWVRDTSW GHHACCTAKI
GADSDKMAVL DSKFRVRGTT GLRVVDASVF PQIPGYYIQT PIYMVSEKAA DVILGH
//
