ID   A0A178DUY5_9PLEO        Unreviewed;       618 AA.
AC   A0A178DUY5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   28-JUN-2023, entry version 20.
DE   SubName: Full=Choline dehydrogenase-like protein {ECO:0000313|EMBL:OAL47215.1};
GN   ORFNames=IQ07DRAFT_590073 {ECO:0000313|EMBL:OAL47215.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL47215.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL47215.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL47215.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441652; OAL47215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178DUY5; -.
DR   STRING; 765867.A0A178DUY5; -.
DR   InParanoid; A0A178DUY5; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000077535; 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:SF115; DEHYDROGENASE XPTC-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.
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:UP000077535};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..618
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008084688"
FT   DOMAIN          40..345
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          469..607
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   BINDING         117
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         266
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         596..597
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   618 AA;  66881 MW;  B75A3B1710B32198 CRC64;
     MLLRIVFSLS FAIGVYSRPS QLGRYAKVID ARDIYNDAEY DFIVAGGGIA GLTVADRLTE
     NPNVTVLVIE YGPFDQREDG VMIPGAYFPV PYLWLPLMST PQIALGGTSY GVPCGRVVGG
     GSVVNAMFFH RSDAELYDAW AELGATGWSW KDLLPYFQKS ETFHPPDPAY AAERNITWDT
     SVHGLDGPVK SSYAPYDYPG SANLYNGAIS LGIQSAKEPN NGRAQGLFRL LRSVDPRTQT
     RSSARVNRYD RDALRHNYHI LPSTAVARVL FNGTTAVGVE YASSVNGTRG VARARKEVII
     AAGGVHTPQI LQLSGVGDAA LLTKIGLEVI SDLPGIGQNL QDHLVLKVNY NYTNNHFPNG
     GSLQSNNTYA TEQRALYDQG KPSAYDLTGT TGNLIIQLPL SNWTSNSSSI IARAERFDPA
     VFLGDSPDER VLRGIKKQRT VIIKDIDTET VGGISWNTGP ETSIYMTRPF SRGSIKINST
     SILDAPLIDY GAITDPTDLD ILTSIYLKNR ELMLTPDLAV LGPSETSPAP GVTDEIEIKE
     RIKKTLAPSN AHQCCTAMMM SKEDGGVVGS DNLVYGTKKL SVVDASVWPL IVGGGPQASV
     YATAEKAADL IQKRHGLL
//