ID A0A317XC05_9EURO Unreviewed; 523 AA.
AC A0A317XC05;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:PWY96073.1};
GN ORFNames=BO94DRAFT_483119 {ECO:0000313|EMBL:PWY96073.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY96073.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY96073.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY96073.1,
RC ECO:0000313|Proteomes:UP000246702};
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 -!- 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:PWY96073.1}.
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DR EMBL; MSFK01000002; PWY96073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XC05; -.
DR STRING; 1450535.A0A317XC05; -.
DR OrthoDB; 2249493at2759; -.
DR Proteomes; UP000246702; 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:SF138; DEHYDROGENASE PKFF-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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000246702}.
FT DOMAIN 37..282
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 384..518
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 57356 MW; F4A7678764677CC1 CRC64;
MTGNLSEVPG YTELFDNSKT PPRDEVEHWW EVPGTPETNN RDLNFTGGKM IGGSHAFSYF
GYLHPTVGAM QKWADDVGDQ SWTYPNTKKY FDQSTFYTPP NATTRFANAT PEYDPSLKGN
GPLEITWPRW AHPFSTWIAK AFDALGVSHT LGYVTGELLG SSWILDTINS TDGTRATTWT
AYIKDKPVQK KIDIFTSTLA GKIVFDGTKA TGVDVTRDLP NQETEQFNIN AKHEVVLAGG
GILSPQLLMV SGVGPADQLE ALNIPVVLDH SRIGQNMHDH IVFGVTYKVK VPTSSILLDD
ATRWHHEGLF KENVTGMLVN PGPDYGAIVD IPSDLRNFTQ EVKQDLAALP KDWPELIIVG
FPLGHDWPSD GNYATLMGIP MTAKSTGSIA LKSGSMVDKP KVIPNWLTSQ TDLQVSIASL
KYMRRVFENP AMGEILASDE ISPGIEAVTW DELEDALKGG FRSMHHPAAT LRMGRDGDPD
AVTDSRGKVR GLDNVRVVDP SAFPFLPPGL PLAPACMFSS LHF
//
