ID A0A1Q3WA46_9BACT Unreviewed; 581 AA.
AC A0A1Q3WA46;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:OJW70919.1};
GN ORFNames=BGO59_32360 {ECO:0000313|EMBL:OJW70919.1};
OS Spirosoma sp. 48-14.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1895854 {ECO:0000313|EMBL:OJW70919.1, ECO:0000313|Proteomes:UP000186057};
RN [1] {ECO:0000313|EMBL:OJW70919.1, ECO:0000313|Proteomes:UP000186057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=48-14 {ECO:0000313|EMBL:OJW70919.1};
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 -!- 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:OJW70919.1}.
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DR EMBL; MKUD01000081; OJW70919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3WA46; -.
DR STRING; 1895854.BGO59_32360; -.
DR Proteomes; UP000186057; 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; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-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 104..306
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 445..567
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 581 AA; 63861 MW; 80A651C704E8A888 CRC64;
MSCSLNGKEL AMYDVIIIGS GAGGGMAAYQ LTKAGANVCL LEAGGYFDPA DPKYITQLKW
PYESPRRGAS TVRAFGDFDA AWGGWQIDGE PYSAETGTEF HWFRSQMLGG RTNHWGRISL
RFGPDDFRRY SLSGIGADWP IGYDDMKPYY DRVDKLIGVF GTNVGLPNEP DGFFLPPPKP
RLHEMLITKA ARSIGVPVFP SRLAVLTKPI NQERGTCFYC AQCGRACSAY ADFSSSSALV
IPALKTGKLT LINNAMAREV LTDPQSGLCT GVSYVDKNSL QERTVKGKMV ILAASTCQSA
RLLLNSKSSR FQRGLANGSG VVGKYLNDST GASMSGFIPA LMNRKRYNED GAQSCHIYTP
WWLDNKKLDF PRGYHIEYGG GMRMPDAGFM GGIEAYNGRM ADASGKKKEA GGYGASLKED
YLRYYGAFVS MAGRGEPVPM ESNYCEIDPN RVDQYGIPTL RFNYKWSDYE IKQARHMQQT
FDEILHAMGG QRVSPAPGAD RNYGLEAPGR IIHEAGTIRM GNDPKTSALN AFQQAHEVKN
LFVVDAAAFP SQGDKNLTWT ILASSMRTSD YIIDQIKKKA L
//
