ID   A0A3E1NFT4_9BACT        Unreviewed;       571 AA.
AC   A0A3E1NFT4;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:RFM26835.1};
GN   ORFNames=DXN05_17760 {ECO:0000313|EMBL:RFM26835.1};
OS   Deminuibacter soli.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Deminuibacter.
OX   NCBI_TaxID=2291815 {ECO:0000313|EMBL:RFM26835.1, ECO:0000313|Proteomes:UP000261284};
RN   [1] {ECO:0000313|EMBL:RFM26835.1, ECO:0000313|Proteomes:UP000261284}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K23C18032701 {ECO:0000313|EMBL:RFM26835.1,
RC   ECO:0000313|Proteomes:UP000261284};
RA   Wang C.;
RT   "Chitinophagaceae sp. K23C18032701, a novel bacterium isolated from forest
RT   soil.";
RL   Submitted (AUG-2018) 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:RFM26835.1}.
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DR   EMBL; QTJU01000007; RFM26835.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E1NFT4; -.
DR   OrthoDB; 9787779at2; -.
DR   Proteomes; UP000261284; 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; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR   PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 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   Reference proteome {ECO:0000313|Proteomes:UP000261284}.
FT   DOMAIN          110..344
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          435..558
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   571 AA;  63430 MW;  E4C6D352578A8EB4 CRC64;
     MNDSAFINRN AQDTAGNTFD AIVIGSGISG GWAAKELCEK GLKTLVLERG RNVEHIKDYP
     TATMAPWEFP HRGKLSAKLF NDNPIAARCY AFREETQHFF VKDHEHPYIQ TQPFDWIRGY
     QVGGKSLLWG RWTQRWSDLD FEANAKDGIA TDWPIRYKDI APWYSYVEKF AGISGNRDGL
     PQVPDGEFLP PMEMTVVEKH LKASIEHNFP GRNLIISRTA NLSKALNGRG PCQYRDLCFR
     GCPFGGYFSS NATTLPAAMA TGNLTIRPFS VAHSIIYDEQ TQKAKGVRVI DAGTLKTTEY
     FAKVIFVNAG TLNSTLLLLN STSSRFPNGM GNDSGALGHY LMDHNYRGRI FGEHAGFKDT
     YYYGRRPTGV YIPRFRNLTD KKEVDFLRGY AFACSSHRPQ GNASGSPQIG KAFKDSLTEP
     GPWQMNMTGM GECLPEAGNK VSLSQDKKDQ WGMPLLNIDC SFRSNEIVML RDILQTGAEM
     LDRAGFKNIT QLDSQQAPGL GIHEMGTARM GRDPKTSVLN GHNQVWGAPN VFVTDGACMT
     SGGCQNPSLT YMALTARAVD YAVEALKKRN L
//