ID A0A1L7XCL7_9HELO Unreviewed; 579 AA.
AC A0A1L7XCL7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Probable alcohol dehydrogenase {ECO:0000313|EMBL:CZR62779.1};
GN ORFNames=PAC_12676 {ECO:0000313|EMBL:CZR62779.1};
OS Phialocephala subalpina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Mollisiaceae; Phialocephala;
OC Phialocephala fortinii species complex.
OX NCBI_TaxID=576137 {ECO:0000313|EMBL:CZR62779.1, ECO:0000313|Proteomes:UP000184330};
RN [1] {ECO:0000313|EMBL:CZR62779.1, ECO:0000313|Proteomes:UP000184330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11012 {ECO:0000313|EMBL:CZR62779.1,
RC ECO:0000313|Proteomes:UP000184330};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; FJOG01000021; CZR62779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L7XCL7; -.
DR STRING; 576137.A0A1L7XCL7; -.
DR OrthoDB; 3382025at2759; -.
DR Proteomes; UP000184330; 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:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 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; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000184330}.
FT DOMAIN 89..112
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT BINDING 91
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 579 AA; 63508 MW; 00B3A72C117B9BC7 CRC64;
MTVPTTKNFD FIVVGGGTAG NVVAGRLAEN PKVSVLVIEA GPGNPRQIPE ITTPARAFEL
RDSNYDWAYK TTMIDRPDYT RVEKPNTRGK VLGGSSCLNY YTWVPGSAAT FNDWEAFGGS
DWNWAGVEKY LKKPAKYFDD DNLYPAELKK VLASENGLLP ISHSDLVPEM APFRDALEKA
WVSKGEKLTD DIYSGEMHGL VKCINSIHKG FRSSSYVFVE NKPNVTILSS THSKKLILEG
TTVKGVEVIG PNGQELTFYA DREVIVSSGV FESPKLLLLS GIGPEEVLGE HGIKPVLKSA
HVGKNLLDHP IVPHVFMLKD GLGLDDHLLR NGPAKAGAIA TYKKDRSGPL GSGLLELVGF
PRIDERLQKS KDYLAAKSKN GGKDPFGPGG QPHFEIDFVP MFCDAFQWHI PTPPTGSWFT
IIVDLLRPVS APGQVKLNSA NCLDQPNINL NFLADDLDVM ALREGVRFVD DILMNGEGMK
DIIGSDYPWP MPRHSDAAMD KLVLERSQTG FHPCGTTRLS KSIEEGVVDS QLKVHGIKNL
RVIDASVFPI IPDCRIQNAV YMVAEKGADL IKAEYSSLY
//