ID   A0A395MJ37_9HYPO        Unreviewed;       668 AA.
AC   A0A395MJ37;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:RFN47954.1};
GN   ORFNames=FIE12Z_7677 {ECO:0000313|EMBL:RFN47954.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN47954.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN47954.1, ECO:0000313|Proteomes:UP000265631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN47954.1,
RC   ECO:0000313|Proteomes:UP000265631};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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}.
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:RFN47954.1}.
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DR   EMBL; PXXK01000222; RFN47954.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395MJ37; -.
DR   STRING; 2594813.A0A395MJ37; -.
DR   Proteomes; UP000265631; 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   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..668
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017261235"
FT   DOMAIN          368..382
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         314
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   668 AA;  72130 MW;  00BE534B1C166061 CRC64;
     MRLSLIFAAI AVLSESVVGS SIPKAHNPFI AKRADSTEYD YVVVGSGAGG GPVAANLAIA
     GYKVLLIDAG GDAGDDLVER VPALNLASSE FEKTRWNYFV NHYSDLEQQK RDSKMTYENS
     DGSLYIGAEP SKDAKALGIL YPRSGTLGGC TRHNALISIL PHDSDWTNIA TLTGDSSWSP
     KNMQSYFKKL ERNRYLPSSI IGHGFNGWLG TSLTSLHLVV EDLKFLSLVI SAATAMGKNL
     LGLLLHTVTG LGNILLADIN APGQASRPGL YQVPLAMSDS VRSSPRELIL DTANAVNKDG
     SRKYHLDIKL NTLVSKIRFD KSGSKPRAAG VDYLEGPSLY SADPRSTSDK STDTGSVNAK
     REVIISAGAF NTPQLLKLSG VGPKKELESF DIPVVVDLPG VGTNLQDRYE ATVIGKSETD
     FTITSKCTFM TTDPDPCLEE YKKGKTPIGK GVYATNGIAL AAVMKSSVAE GEPDLLISGG
     PAKFTGYFHG YSREALADAK HWSWIILKAH SRNNAGTVTL KSKDPQDMPL INFNYYDTGV
     NANGEGDKDL QATYEGFQWG RKAFDKLIPL DGDFDEVWPG RNVTKKEDIK QYIKNEAWGH
     HASCTCPIGA DDDPMAVLDS QFRVRGVEGL RVVDASVFPK IPGFYIALPL YIVAEKASDV
     IVKAAKSA
//