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Database: UniProt
Entry: B1VU68_STRGG
LinkDB: B1VU68_STRGG
Original site: B1VU68_STRGG 
ID   B1VU68_STRGG            Unreviewed;       537 AA.
AC   B1VU68;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Putative GMC-family oxidoreductase {ECO:0000313|EMBL:BAG17912.1};
GN   OrderedLocusNames=SGR_1083 {ECO:0000313|EMBL:BAG17912.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17912.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17912.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism Streptomyces
RT   griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; AP009493; BAG17912.1; -; Genomic_DNA.
DR   RefSeq; WP_012378288.1; NC_010572.1.
DR   AlphaFoldDB; B1VU68; -.
DR   GeneID; 6210765; -.
DR   KEGG; sgr:SGR_1083; -.
DR   PATRIC; fig|455632.4.peg.1081; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_11; -.
DR   Proteomes; UP000001685; Chromosome.
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; 3.30.410.40; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF152; OXIDASE (CODA), PUTATIVE (AFU_ORTHOLOGUE AFUA_8G04090)-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   DOMAIN          261..275
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         96
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   537 AA;  58507 MW;  8FA4EAD456E90F51 CRC64;
     MPSTPRSTAV PDPEGPVADY VIVGGGTAGS VIASRLTEDP DVTVTVIEGG PTDIDRDDVL
     TLRRWLGLLG GDLDYDYPTT EQPRGNSHIR HSRARVLGGC SSHNTLISFK PLPGDWDEWA
     EAGAEGWDAA AMDPYFAKLR NNIVPVDEKD RNAIARDFVD AARAAAGVPR VDSFNSKPFH
     EGVGFFDLAY HPENNKRSSA SVAYLHPHIE AGDRPNLRIM LETWAYRLEF EGARATGVHV
     RTKDGEEILL RAAREVVVCA GAVDTPRLLL HSGIGPREDL AALGIDVRHD LPGVGENLLD
     HPESVIVWET DGPIPENSAM DSDAGLFVRR DPGSRGPDLM FHFYQIPFTD NPERLGYQKP
     EHGVSMTPNI PKPRSRGRLY LTSADPEVKP ALDFRYFTDE DDHDGRTLVD GIKLARRIAA
     TEPLAHWLKR EVCPGPEVTS DEDISAYARK VAHTVYHPAG TCKIGAADDQ EAVVDPQLRI
     RGLEGIRIAD ASVFPTMPAV NPMIGVLMVG EKCAELLADR TRDTAPVTGP STGGDAR
//
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