ID   A0A0X3W6V9_9ACTN        Unreviewed;       637 AA.
AC   A0A0X3W6V9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KUL52548.1};
GN   ORFNames=ADL30_23435 {ECO:0000313|EMBL:KUL52548.1};
OS   Streptomyces sp. NRRL S-1521.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL52548.1, ECO:0000313|Proteomes:UP000053420};
RN   [1] {ECO:0000313|EMBL:KUL52548.1, ECO:0000313|Proteomes:UP000053420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL52548.1,
RC   ECO:0000313|Proteomes:UP000053420};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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:KUL52548.1}.
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DR   EMBL; LLZK01000216; KUL52548.1; -; Genomic_DNA.
DR   RefSeq; WP_062778550.1; NZ_LLZK01000216.1.
DR   AlphaFoldDB; A0A0X3W6V9; -.
DR   Proteomes; UP000053420; 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; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000053420}.
FT   DOMAIN          31..389
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          484..617
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          90..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   637 AA;  69864 MW;  DDE3E70E9D479E5B CRC64;
     MTSYDDADTA IFPAGAATQT SATEAARGEW DAVVVGGGMA GSIVADQLSQ AGYEVLILEA
     GPGKDLDLAE YESYLSRFYG AVVKDNQSPY PFNPNARMPR STDTMPVRPD TPRDDFYLVQ
     EDKYCTDTTF TRVLGGTSMH WEGKALRMLP EDFNLKTKYG QGLNWPLSYD DLEPYYRQAE
     AELGVAAEVE DQAYLGMHFP QGYVFPMHRM PPSFLDQTVA RGVDGMRVNL ADDDYTLQVR
     SFPQARNGVP NAAYDGGKGF VPVGAVSTSQ VEEGERCQGN TNCVPICPVQ AKYHAGKTLA
     KALRKGNVKI VTQAVASKVE IDEQDRRVTG ITVKNYQSLA SDSYETYTVK GTVYILCAHA
     IENARLMLAS DMQRMSRSKL IGRNLMDHAY LLSWGLLPEP AGTMRGTSCT SGITDLRGGR
     FRGTQAGFGV DIHNDGWGWA TGSPYTDLVE LVDEQGLRGA ELRRTLGNQI SRQLLLAFMI
     DLLPDRSNTV TVDDRYKDAI GNVKPVVSLK IPPYTMRGAA FARKLATDIF DKLGAEDRTT
     YDKDRYSAVE HDGQWYNIVG GNHLAGTHIM GTDPVNSVVD HTQQSWDHDN LYLVGPGSLP
     SIGTSNISLT MAALAFRSST HIVRYLRAAK APATIRS
//