ID   A0A177CEI0_9PLEO        Unreviewed;       613 AA.
AC   A0A177CEI0;
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:OAG05716.1};
GN   ORFNames=CC84DRAFT_1091449 {ECO:0000313|EMBL:OAG05716.1};
OS   Paraphaeosphaeria sporulosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC   Paraphaeosphaeria.
OX   NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG05716.1, ECO:0000313|Proteomes:UP000077069};
RN   [1] {ECO:0000313|EMBL:OAG05716.1, ECO:0000313|Proteomes:UP000077069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG05716.1,
RC   ECO:0000313|Proteomes:UP000077069};
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; KV441552; OAG05716.1; -; Genomic_DNA.
DR   RefSeq; XP_018036081.1; XM_018174401.1.
DR   AlphaFoldDB; A0A177CEI0; -.
DR   STRING; 1460663.A0A177CEI0; -.
DR   GeneID; 28757887; -.
DR   InParanoid; A0A177CEI0; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000077069; 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.
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:UP000077069};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..613
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008058088"
FT   DOMAIN          294..308
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        550
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        593
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         251
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   613 AA;  65369 MW;  646B10D2BEBE1FFC CRC64;
     MYCFREILAF FAFATHTSAL TDTYDYIIVG GGLTGLVVAN RLSEDSNRTV LVIENGYIDS
     SPNVQVPYLA GVLNSNPPLY QSLVSAPDPQ LGNRTFSVAV GNVVGGGSIV NGMMLDRGSD
     ADYNAWEELG NVGWGWKDLA PFFKKVFTFT PPSEETTKAI GITYDKTAYG NGPVQATIAS
     FQYPDYKGIF DAWKNESGIS LPKEGFASPL GAFWAPNTID NVTGERSNAR TAYYEPVKAR
     PNLKLLVGTH VDEILFNINS NGGSLRANGV KMTDRNTSST TSAWASREVI LAAGAIFTPH
     LLMVSGIGPA SDVGAANISV KVDLPAVGAN FQDHVPAYMT FNLSNLAFPN YSTLATNASF
     NASAAQEYAD HKTGPWTLSR GNALAFLTLP QLTPSYSSLA ATASSQTPTD FLPERYATSK
     PLQAGYLAQR SILLKQFTGE QGYAAAAGEL AIQPSNRAAV ALQKPLSRGT ITLNTSNPHG
     YPVVAYNSLQ NPVDAAILTA LVRFNRKHWA SPALSRYAPV ENVPGAEFVS DEQIMRALNE
     KAAVSSSFAH PSGSCAMLPR DLGGCVSDQL LVYGVDGLSI VDASILPMIP ATHLQATMYA
     VAEKAADIIK NRG
//