ID Q70IY0_STRSD Unreviewed; 508 AA.
AC Q70IY0; Q2MF19;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE SubName: Full=Putative aminoglycoside 6'-dehydrogenase, TobQ {ECO:0000313|EMBL:CAH18553.1};
GN Name=tobQ {ECO:0000313|EMBL:CAH18553.1};
OS Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 /
OS CBS 697.72 / NBRC 16175 / NCIMB 11028 / NRRL B-12390 / A12253. 1)
OS (Streptomyces tenebrarius).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Streptoalloteichus.
OX NCBI_TaxID=1933 {ECO:0000313|EMBL:CAE22474.1};
RN [1] {ECO:0000313|EMBL:CAE22474.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 17920 {ECO:0000313|EMBL:CAE22474.1};
RX PubMed=14757238; DOI=10.1016/S0378-1097(03)00881-4;
RA Kharel M.K., Basnet D.B., Lee H.C., Liou K., Woo J.S., Kim B.-G.,
RA Sohng J.K.;
RT "Isolation and characterization of the tobramycin biosynthetic gene cluster
RT from Streptomyces tenebrarius.";
RL FEMS Microbiol. Lett. 230:185-190(2004).
RN [2] {ECO:0000313|EMBL:CAH18553.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain: DSM 40477 {ECO:0000313|EMBL:CAH18553.1};
RA Aboshanab K., Schmidt-Beissner H., Wehmeier U., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Comparison of the gene clusters for the biosynthesis of the aminoglycoside
RT antibiotics tobramycin-apramycin (Streptomyces tenebrarius DSM 40477), and
RT hygromycin B (Streptomyces hygroscopicus subsp. hygroscopicus DSM 40578).";
RL Submitted (AUG-2004) 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}.
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DR EMBL; AJ579650; CAE22474.1; -; Genomic_RNA.
DR EMBL; AJ810851; CAH18553.1; -; Genomic_DNA.
DR AlphaFoldDB; Q70IY0; -.
DR KEGG; ag:CAE22474; -.
DR BioCyc; MetaCyc:MONOMER-17234; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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 Pfam; PF13450; NAD_binding_8; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:CAH18553.1};
KW Helicase {ECO:0000313|EMBL:CAH18553.1};
KW Hydrolase {ECO:0000313|EMBL:CAH18553.1};
KW Nucleotide-binding {ECO:0000313|EMBL:CAH18553.1}.
FT DOMAIN 202..286
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 382..503
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 508 AA; 54715 MW; 454F694A6A65C7CE CRC64;
MLLISADEAA RRTYDACVVG SGASGSVAAA VLAERGLSVL VVEQGGPIPP GADVEDHEDP
DGWAFARRHG RWTRDGFPWT AMALGGGTVF YAGMSYRYQD SDLAPPSSLL GEADYDHWQV
GLADLEPHYE WIEYQLAVAG PSRKRVGDYV FPVYHRPSLP PTPPGLALAE GARALNLTPL
PTPVAISGIR DRFGPGCAQA TPCTSFSCPT GAKADVVSRV LAPAEGDVSV LVHTRVDRLV
ASGSHRVDAA EVVDRGTGTR RTLRARRFLV AANAIQSAAL LLRSTSRLEP DGLGNGNGLV
GRHLAMKNSV YVRGVVPRRL PGYTPLRHRY SSVCVLDYLT GEEFPDGVGG LIHEANPWEP
AAEREAERGT VLQVECLLGD RPQARNRVRL SRTRDRDGFP RIVLDYEPHP ADLTRLAVLS
ERATDILTKA GAIDVREVDT AYELGSAHLH GTLRSGRDPR TSVTDPFGRL HGYDNVWAVD
GATFPFAGNP NPTLTIQANA HRIASAID
//
