ID   U4KXZ2_PYROM            Unreviewed;       280 AA.
AC   U4KXZ2;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Similar to Glucose oxidase acc. no. P81156 {ECO:0000313|EMBL:CCX06811.1};
GN   ORFNames=PCON_06398 {ECO:0000313|EMBL:CCX06811.1};
OS   Pyronema omphalodes (strain CBS 100304) (Pyronema confluens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pyronemataceae; Pyronema.
OX   NCBI_TaxID=1076935 {ECO:0000313|EMBL:CCX06811.1};
RN   [1] {ECO:0000313|EMBL:CCX06811.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS100304 {ECO:0000313|EMBL:CCX06811.1};
RC   TISSUE=Vegetative mycelium {ECO:0000313|EMBL:CCX06811.1};
RX   PubMed=24068976; DOI=10.1371/journal.pgen.1003820;
RA   Traeger S., Altegoer F., Freitag M., Gabaldon T., Kempken F., Kumar A.,
RA   Marcet-Houben M., Poggeler S., Stajich J.E., Nowrousian M.;
RT   "The genome and development-dependent transcriptomes of Pyronema confluens:
RT   a window into fungal evolution.";
RL   PLoS Genet. 9:E1003820-E1003820(2013).
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HF935315; CCX06811.1; -; Genomic_DNA.
DR   AlphaFoldDB; U4KXZ2; -.
DR   STRING; 1076935.U4KXZ2; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   OMA; RESWFLI; -.
DR   OrthoDB; 2694542at2759; -.
DR   Proteomes; UP000018144; 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   PANTHER; PTHR11552:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..280
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004650854"
FT   DOMAIN          113..136
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
SQ   SEQUENCE   280 AA;  31292 MW;  B6A8F10A6622A35B CRC64;
     MRFPSSHLQT LAITCLFTLT TALPATVIKR EEDLKSSYDY IIVGGGTSGL VIANRLTEDP
     KTTVLVIEAE FHLSKKMKSF PGYVGRTGAK YEWGYNTSAI SGLNDRKFRI PAAKVVGGGS
     VINGMFYTRG SKEDYDSWEK LGNPGWGWED LRKWFNKSET FHRQPEDSGV TFDLSTHGTT
     GPIQTSYPPL RYPQLRESWF LIHVNHELSL TAGVRAEKII NAMKSFGIPT ALDGTNGHSL
     GKFWVLNTLD PRNQTRSYAQ LIMTQPSRGK LSFDHTATSY
//