ID   A0A258WUG5_9SPHI        Unreviewed;       567 AA.
AC   A0A258WUG5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:OYZ31833.1};
GN   ORFNames=B7Y24_08365 {ECO:0000313|EMBL:OYZ31833.1};
OS   Sphingobacteriales bacterium 16-39-50.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1970581 {ECO:0000313|EMBL:OYZ31833.1, ECO:0000313|Proteomes:UP000216983};
RN   [1] {ECO:0000313|EMBL:OYZ31833.1, ECO:0000313|Proteomes:UP000216983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16-39-50 {ECO:0000313|EMBL:OYZ31833.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-2017) 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:OYZ31833.1}.
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; NCHA01000005; OYZ31833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A258WUG5; -.
DR   Proteomes; UP000216983; 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;
FT   DOMAIN          104..339
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          441..554
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   567 AA;  64159 MW;  8D80E1E14AD82FAC CRC64;
     MNINIKAEKQ NTYDAIVVGS GISGGWAAKE LTEKGLKVLM LERGRNVEHV KDYDTALMKP
     WEFKHRGRIT PEERSRHLVQ TRAGQYSEFN AKFWVDDVDC PYTEVKRFDW YRGYHVGGRS
     LTWGRGCLRL SEMDFSANAK DGYGVDWPVR YKDISPWYDY VERFAGISGQ NEGLAQLPDG
     IFLPPFEMNC VEKAVKERIE KHYNKERMMT VYRMANLTVP HNGRGTCQNR NLCSRGCPFG
     AYFSTQSATL PAAMATGNLT LRPYSIVSEV LYDKETRKAK GVMVIDSETN EHIEYSAKVI
     FMNASTLGTT QILLNSTSDT FPDGLGNSSG HLGHNLMDHH FQIGASGRAE GFDDKYYYGR
     RPIGIYIPRY RNLGDKPERD YLRGFHYGGS ASRTGWQRAI PEMGFGQDFK EDMTEPGPWV
     MGLGSFGEHL PEFKNRAFLD RTKKDKWGLP LLAVDCEFGE NERKMRIDMK NDAAEILEAA
     GMKDIQAFDR PAIPGMAIHE MGTARMGHDP KTSVLNKWNQ MHDVKNVFVT DGAFMTSNAC
     QNPSLTYMAF TARACDHAVS ELKKGNL
//