ID   A0A1Q4FCK8_9SPHI        Unreviewed;       578 AA.
AC   A0A1Q4FCK8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:OJY91083.1};
GN   ORFNames=BGP14_06745 {ECO:0000313|EMBL:OJY91083.1};
OS   Sphingobacteriales bacterium 44-15.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895837 {ECO:0000313|EMBL:OJY91083.1, ECO:0000313|Proteomes:UP000186250};
RN   [1] {ECO:0000313|EMBL:OJY91083.1, ECO:0000313|Proteomes:UP000186250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-15 {ECO:0000313|EMBL:OJY91083.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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:OJY91083.1}.
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DR   EMBL; MKWG01000007; OJY91083.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4FCK8; -.
DR   STRING; 1895837.BGP14_06745; -.
DR   Proteomes; UP000186250; 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; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR   Pfam; PF00890; FAD_binding_2; 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   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          14..47
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          57..325
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          443..564
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   578 AA;  63971 MW;  5427549ACDD4A692 CRC64;
     MGKLQIKKSP TVHDVVVIGS GAGGGMAGYV LAQAGVKVLM LEAGPYFDPR KDSHQLKWPW
     QSPRRGASTV RAFGDFDAAY GGWEIDGEPY TRNNNTEFDW FRSRMLGGKT NHWGRISLRM
     GPDDFQPKDG LTERWPFGYD ELKPYYDKVD RLIGLYGTVE GLENEPDGIF MTPPKPRLPE
     LFIKKAGASV GVKVIAGRGS VMTEALPDNK DRQPCFYCGQ CGRSCKVYGD FSASSCLVIP
     AIKTGNLEVI TNAMVREILT DKNGQATGVS YINKEDMQEY QVSAKTVILG ASACESARIL
     LNSRSSAHPN GLANNSNVVG KYLHDSTGSS LGGFLPQLLD RKRFNEDGTG SIHIYSPWWL
     DNKKLDFPRG YHIEYGGGMR MPSYGFGGGM HRMNGLVPGK DGKTKQAGGF GASLKDDYRR
     FYGTTLGMAG RGTAIARKEN YCEIDPNVVD KYGIPVLRFN YTWSNEEIKQ AKHMQETFQE
     LFHAMGGIVT SSPHGEHDNW GLEAPGRIIH EVGTIRMGDD PKKSALNKWC QAHDCKNLFV
     VDAAPFVQQG DKNATWTILA LSWRTAEYIL EQRKKGNV
//