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Database: UniProt
Entry: N4WVI3_COCH4
LinkDB: N4WVI3_COCH4
Original site: N4WVI3_COCH4 
ID   N4WVI3_COCH4            Unreviewed;       683 AA.
AC   N4WVI3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=COCC4DRAFT_206281 {ECO:0000313|EMBL:ENI00268.1};
OS   Cochliobolus heterostrophus (strain C4 / ATCC 48331 / race T) (Southern
OS   corn leaf blight fungus) (Bipolaris maydis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX   NCBI_TaxID=665024 {ECO:0000313|EMBL:ENI00268.1, ECO:0000313|Proteomes:UP000012338};
RN   [1] {ECO:0000313|EMBL:ENI00268.1, ECO:0000313|Proteomes:UP000012338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
RN   [2] {ECO:0000313|Proteomes:UP000012338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C4 / ATCC 48331 / race T {ECO:0000313|Proteomes:UP000012338};
RX   PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA   Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA   Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA   Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA   LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA   Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT   "Comparative genome structure, secondary metabolite, and effector coding
RT   capacity across Cochliobolus pathogens.";
RL   PLoS Genet. 9:E1003233-E1003233(2013).
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; KB733476; ENI00268.1; -; Genomic_DNA.
DR   RefSeq; XP_014074177.1; XM_014218702.1.
DR   AlphaFoldDB; N4WVI3; -.
DR   GeneID; 25842521; -.
DR   HOGENOM; CLU_002865_4_1_1; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000012338; 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   Pfam; PF13450; NAD_binding_8; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..683
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004123747"
FT   DOMAIN          387..401
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         329
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   683 AA;  73979 MW;  068DC2FFDD5B6D56 CRC64;
     MIVIKAFTVL SLITSLAGAR IIDGAQHTPY SGANVKRATN GSDTTTLEDY EYVIVGSGAG
     GSPLAARLAL AGHKVLLLEA GDDQTNSTQY NVPALHAVAA EYEPMRWDYF VKHFDDEQEM
     RRDTKLTYEL PDGSRYTGAN PPADAKPLGI LYPRVGSLGG CTGHNALIAI YPYTSDWTNI
     QQLTGDDSWA PEKMRSFFTR LEKSRYLPSS IAGHGFSGWL ETSLTDLTLI VQDLKVVSLV
     LAAATGMGKS LLSALLTTVT GMAQVLLRDI NNPSPGRDSQ EGMWQVPLTM SIPDYKRAGP
     VDFLHQVIGA KNSDGSRKYH LDIQLNTLVT SIRFNQTADG KPKATGVNFL TGRSLYGADP
     RRQSGSATGQ GTKGAVTATR EVIISAGAFN TPQILKLSGV GPKAELEQFG IEVVKDLPGV
     GTNLQDRYEV PVIGQAPTKI SLLNGCTFLE GYDRCLEKWE KLPLGIGKGV YATNGVALAI
     TLKASNSIHG NADLLVAGWP AYFNGYYPDF FQNATKGQDH WTWLTLKAES RNNAGTVTLR
     SANPQDVPEI RKRNFAVGGD EDLQAVIEGM KYGRNVFKSL IPLDGKFEED WPGPSVQTDD
     ELKEFAKYQA WGHHASCTCP IGADDDDMAV LDSNFKVRGI ESLRVVDASV FPKIPGTFPV
     ISIYMISEKA SDVILADAQN SKA
//
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