ID   A0A1M3B6U6_9ACTN        Unreviewed;       542 AA.
AC   A0A1M3B6U6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Glucose dehydrogenase {ECO:0000313|EMBL:OJU79778.1};
GN   ORFNames=BGO11_02980 {ECO:0000313|EMBL:OJU79778.1};
OS   Solirubrobacterales bacterium 70-9.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales.
OX   NCBI_TaxID=1895833 {ECO:0000313|EMBL:OJU79778.1, ECO:0000313|Proteomes:UP000184118};
RN   [1] {ECO:0000313|EMBL:OJU79778.1, ECO:0000313|Proteomes:UP000184118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=70-9 {ECO:0000313|EMBL:OJU79778.1};
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:OJU79778.1}.
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DR   EMBL; MKSH01000275; OJU79778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3B6U6; -.
DR   Proteomes; UP000184118; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD 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; IPR002938; FAD-bd.
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; PF01494; FAD_binding_3; 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          6..39
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          89..310
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          402..523
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   542 AA;  58278 MW;  C097ACC85B3099C6 CRC64;
     MGERLEADVV VIGSGPSGSI VTHTLATAGV DVVCLEQGDW INPSDFGTNE PEWELSIQQR
     WAHDPNVRMA PADYPVEVSD SDMWPVMLNA VGGTSLFYGA EWVRLMASDF RLRSSEGICD
     DWPISYAELK PFHDEVDAFL GVAGVGGDPA YPEGLDYPMP PHPIGKVGMK AAEGVNKLGW
     HWWPGVNAIA VNRHKTLERC LRHGVCEWGC PAGAKASFDL IYLPQAIAAG ARLLTGARVS
     RIESGPDGLA TGAHFVDREG EENFVAAKAV VVCANGIGTP RLLLLSDGPA HPDGLANSSG
     LVGKNLMLHP NCTVTGYYDE DLESWKGPVG ESIHSMEFYE TRPEHDFVRG GKMNVLPTPG
     PLAAVEAHRD QPFDQVWGPA FADVAARHRS GILWATNTED LPEETNRVTL DPTLTDGDGV
     PAPKVSYRIS DNTRRILDFH VERMTELHEA SGASEMIAVD VWLDQPGHLL GTARMGDDPE
     RSVVDSYGRA HDVPNLFVAD GSIFVTGGAA NPTSTITALA LRIAKHIVAT AAERPTAGGV
     AR
//