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Database: UniProt
Entry: A0A0F8TXF9_9EURO
LinkDB: A0A0F8TXF9_9EURO
Original site: A0A0F8TXF9_9EURO 
ID   A0A0F8TXF9_9EURO        Unreviewed;       593 AA.
AC   A0A0F8TXF9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Glucose-methanol-choline (Gmc) oxidoreductase {ECO:0000313|EMBL:KKK12053.1};
GN   ORFNames=ARAM_000996 {ECO:0000313|EMBL:KKK12053.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK12053.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK12053.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK12053.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KKK12053.1}.
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DR   EMBL; JZBS01004128; KKK12053.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8TXF9; -.
DR   STRING; 308745.A0A0F8TXF9; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000034291; 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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291}.
FT   DOMAIN          10..312
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          430..567
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   593 AA;  65412 MW;  956CD8EBF2031448 CRC64;
     MAQVSNGSQY DFIVVGGGTA GNTIAGRLAE NPNVRVLVVE AGIAKPYEVE DITTPSKAFG
     LRGSQYDWAY KTTMIKREDY ERVEKPNTRG KALGGSSCAN YFTWIPGSKA TFDDWEEFGG
     HEWKWDGCVD YLRKCATYHD DEKLYPAELS KIGTGGPLQI SHAELVPEMQ PFRDALTQAW
     VSKGQLLSED IYSGEMHGLT HCVDTIYKGQ RQGSYLYVKD KPNVTILSGV QSRKLIIDKS
     TRICSGVVTV NPVTGEEISV YAKREVIVSQ GVFETPKLLM LSGIGPAKEL AKHGIDVVLD
     SPHVGQHLLD HPIVPFVLQI QDGYGLDDHL LRAGPLNEAA VSAYRRDKTG PVGSGLLELV
     GFPRIDERLE RYPAYREAKA ANGGLDPFGP AGQPHFELDF VGMFSSAFQW HYPVPSQGNY
     MTVIVDLLRP LSEGEVTLNS NNALVQPNIN LNFFGSDLDI LAMREGVRWT YDVLTNGAGF
     KDIVVAEYPW TMPLNSDEAM NKAVLERSQT GFHPCGTARL SKSINQGVVD SKLRVHGIQN
     LRIADASVIP VIPDCRIQNS VYMIGEKGAD IIKSQHKDLY EAQNIPYFVP SKL
//
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