ID   A0A066XN64_COLSU        Unreviewed;       713 AA.
AC   A0A066XN64;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Putative choline dehydrogenase {ECO:0000313|EMBL:KDN70352.1};
GN   ORFNames=CSUB01_08406 {ECO:0000313|EMBL:KDN70352.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN70352.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN70352.1}.
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DR   EMBL; JMSE01000357; KDN70352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XN64; -.
DR   STRING; 1173701.A0A066XN64; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_4_1_1; -.
DR   OMA; HDLWIGG; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000027238; 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; 2.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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:SF80; -; 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; 2.
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:UP000027238};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..713
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001634160"
FT   DOMAIN          416..430
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         361
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   713 AA;  77789 MW;  A97DB9C14C793A34 CRC64;
     MRLAVSWHLL WVPVTLAAKQ LGGGFDFNYP RHPNQVRYEA LGPQLTAAPP PEKEYEYIIV
     GSGPGGSPLA ARLAMAGHSV LLIDAGGDHG ALREVQIPAM SIWSSERTEL SWGYYTHHYE
     DEQMAKRDRK LTYRTKEGDL YSGTNPPEGA EVLGNYYPRV GGLGGCAEHN AMLAIYPHKR
     DWNYIKEITG DESWDAENMR KYFTKLERNE APFPSDLDAH GYSGWLKIAL TPLTLIAQDL
     KLLTVVLGGA AAAGIEVDGL LTKVNRIVNG LPILGGLITK LLPLDYVTGL VDGLASLLLH
     DVNNNSPDRD STPMLTQIPL SMGAPDYTRS SPRDLVYSVA TAKNPDGSRK YKLDIALHTL
     VTKVNFNTSG TVPQATGVEY LFGESLYRAD TRASDSEDGG VPGSVSASRE VIISAGTFNT
     PQILKLSGVG PKDELEKFGI PVVKDIPGVG TNLQDRYELS VTAETKDGFA LVEDCTFLAE
     GDPCYKRWLE GIGPLKGVYT TGGISLGMFM LSSQAEGEHD IWVGGIPAYF QGYYPGYSQN
     VLTATSKNHW TWLVLKAHTR NNGGTVNLTS TNPRDTPKIT FHNFYEGASQ ADADKDLQAI
     IEGMRFGMKA IEDIPPVVGE FERIWPPSEI NSDEDLKQWI QEEAWGHHAS SSCPIGSDSD
     PMAVLDGSFR VRGINGLRVV DMSAFPKIMG VFPVISLYMA SEKAADSILQ DAQ
//