ID   A0A117E0D3_ASPNG        Unreviewed;       603 AA.
AC   A0A117E0D3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=ABL_03855 {ECO:0000313|EMBL:GAQ40865.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ40865.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ40865.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BCMY01000005; GAQ40865.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117E0D3; -.
DR   PaxDb; 5061-CADANGAP00011676; -.
DR   VEuPathDB; FungiDB:An15g02200; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1143523; -.
DR   VEuPathDB; FungiDB:ATCC64974_30910; -.
DR   VEuPathDB; FungiDB:M747DRAFT_294099; -.
DR   OMA; ILYEHPG; -.
DR   Proteomes; UP000068243; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF78; GMC_OXRDTASE_N DOMAIN-CONTAINING PROTEIN; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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         96
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         533..534
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   603 AA;  65181 MW;  77DDB88B836B95C8 CRC64;
     MGIYTRLPES IDEVDIIIAG GGTAGCVVAS RLADADPSLS ILVVEGGQNN KGNHLIAFPL
     LFPTALLPTS TATLFYKGNA EPQLDNREMI VPAGGVLGGG SSINLMMYSR AQRHDWDSWA
     TPGWSTDEMI PFLKKLETYH GPGPDSVHGK SGPIVVSPGT FYSERTAEQF IAAANEVGYP
     TVNDLQDLDT SNGVQRALRF VDKEGRRQDA ASNYLHPKLE DGAHPNLHVL VETKVVKILF
     KGKRAVGVEF KPNPAFQKED HTNVRCVKAR KLVISSCGAI GTPLLLERSG LGDEAILNKA
     GVPAVAHISG IGRDYQDHHL LIQAYYSALE PTETFDAPLA GRINMEELIK TNAPIMGWNG
     QDASCKLRPT EADVTALGPE FEAAYARDYR STPNKPMALM ALLGGFPGEP HTIESGQYLA
     TSLFTVYPYA RGHVHITSPD PDADISFETG FLKSDLDVKK LIWAYKKQRE IVRRMGVYRG
     EFAGMHPPFA EDSAAALVRL DKPNDKTISD IQYTAEDDKV IEGWVRKNVG TTWHSLGTCK
     MGALADGGVV DPELNVHGIE GLKLVDLSIV PQNIGANAAT TAYAIGEKAA TIIMKDLGLA
     GNE
//