ID A0A318ZTN7_ASPLB Unreviewed; 555 AA.
AC A0A318ZTN7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:PYH50891.1};
GN ORFNames=BO96DRAFT_489943 {ECO:0000313|EMBL:PYH50891.1};
OS Aspergillus lacticoffeatus (strain CBS 101883).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=1450533 {ECO:0000313|EMBL:PYH50891.1, ECO:0000313|Proteomes:UP000247441};
RN [1] {ECO:0000313|EMBL:PYH50891.1, ECO:0000313|Proteomes:UP000247441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101883 {ECO:0000313|EMBL:PYH50891.1,
RC ECO:0000313|Proteomes:UP000247441};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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; KZ821387; PYH50891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318ZTN7; -.
DR OrthoDB; 3714148at2759; -.
DR Proteomes; UP000247441; 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; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 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}.
FT DOMAIN 278..292
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 107
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 555 AA; 61648 MW; A39FB56F5ACE25CE CRC64;
MATTNEFPAS DVNSYDYVIV GGGTAGCVIA SRLAEYLPNK RILIIEGGPS DFMDDRVLKL
KDWLNLLGGE LDYDYPTVEQ PMGISNFSCL FFYCTGNSYI RHSRAKVLGG CSSHNTLISF
RPFEYDCKRW EQAGCTGWSF DTFTRVLDNL RNTVQPVHNR HRNQLCKDWV QACSSAMNIP
VIEDFNKEIR SKGELTEGVG FFSVSYNPDD GRRSSASVAY IHPILRGEEK RPNLTILTNA
WVSRVNVDGD SVTGVDVTLQ SGVKHTLRAK KETILCAGAV DTPRLMMLSG LGPREQLSGL
GIPVVKDIPG VGENLLDHPE SIIIWELNRP VPPNQTTMDS DAGIFLRREL PNANGFDGRA
ADIMMHCYQI PFCLNTERLG YDTPVDAFCM TPNIPRPRSR GRIYLTSADP SVKPALDFRY
FTDPEGYDAA TIVAGLKAAR EIAKQSPFKD WIKREVAPGP NVQTDEELSE YGRRVAHTVY
HPAGTTKMGN LTRDPMAVVD PKLKVRGLKN VRIADAGVFP EMPTINPMLT VLAIGERAAE
LIAEEAGWKR EQPRL
//
