ID A0A101SWI9_9ACTN Unreviewed; 379 AA.
AC A0A101SWI9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Flavin-dependent monooxygenase {ECO:0000256|HAMAP-Rule:MF_00845};
DE AltName: Full=TetX monooxygenase {ECO:0000256|HAMAP-Rule:MF_00845};
DE Short=TetX {ECO:0000256|HAMAP-Rule:MF_00845};
DE EC=1.14.13.- {ECO:0000256|HAMAP-Rule:MF_00845};
GN ORFNames=AQJ66_24060 {ECO:0000313|EMBL:KUN81477.1};
OS Streptomyces bungoensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285568 {ECO:0000313|EMBL:KUN81477.1, ECO:0000313|Proteomes:UP000053024};
RN [1] {ECO:0000313|EMBL:KUN81477.1, ECO:0000313|Proteomes:UP000053024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41781 {ECO:0000313|EMBL:KUN81477.1,
RC ECO:0000313|Proteomes:UP000053024};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces bungoensis DSM 41781, type strain
RT for the species Streptomyces bungoensis.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: An FAD-requiring monooxygenase active on some tetracycline
CC antibiotic derivatives, which leads to their inactivation. Hydroxylates
CC carbon 11a of tetracycline and some analogs. {ECO:0000256|HAMAP-
CC Rule:MF_00845}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a tetracycline + H(+) + NADPH + O2 = an 11a-
CC hydroxytetracycline + H2O + NADP(+); Xref=Rhea:RHEA:61444,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:144644,
CC ChEBI:CHEBI:144645; Evidence={ECO:0000256|HAMAP-Rule:MF_00845};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00845};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00845}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00845}.
CC -!- DOMAIN: Consists of an N-terminal FAD-binding domain with a Rossman
CC fold and a C-terminal substrate-binding domain. {ECO:0000256|HAMAP-
CC Rule:MF_00845}.
CC -!- SIMILARITY: Belongs to the aromatic-ring hydroxylase family. TetX
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00845}.
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:KUN81477.1}.
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DR EMBL; LMWX01000041; KUN81477.1; -; Genomic_DNA.
DR RefSeq; WP_061926138.1; NZ_KQ948863.1.
DR AlphaFoldDB; A0A101SWI9; -.
DR STRING; 285568.AQJ66_24060; -.
DR OrthoDB; 3217377at2; -.
DR Proteomes; UP000053024; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR HAMAP; MF_00845; TetX_monooxygenase; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR043683; TetX_monooxygenase.
DR PANTHER; PTHR46972; MONOOXYGENASE ASQM-RELATED; 1.
DR PANTHER; PTHR46972:SF1; RHODANESE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00845};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00845};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_00845};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000256|HAMAP-
KW Rule:MF_00845}; NADP {ECO:0000256|HAMAP-Rule:MF_00845};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00845};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00845}; Reference proteome {ECO:0000313|Proteomes:UP000053024}.
FT DOMAIN 6..344
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 42
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
SQ SEQUENCE 379 AA; 39737 MW; AE6425B62D2772A4 CRC64;
MSTHHPIAII GGGLGGLTAA RVLHVNGIQA ALFELEASAG ARTQGGMLDI HEDSGQKALH
AAGLHDGFLK IVHEGGQAMR LVGPDATVHV SETDDGTGGR PEVDRADLRD LLLDSLPEGT
VRWGRKATGV QALGDGRHEV TFADGSAITT DLLIGADGAW SRVRPLLSDA TPAYTGISFA
ETDLYDADAR HPRSAAVVGD GFFISLGDRC GFLAHRETDG SLHVYAALKA GEGWLDTIDF
TDLAAAKAAV LTRFDGWHED LRALIADADT ITPRRIHALP VGHRWERGAG VTLLGDAAHV
MSPFAGEGAN LAMLDGAELA EAIAAHRGDT EAALTAYEKA LFPRSEASAA ESAASLERMF
SDQGLERMIE FFTSGPAAG
//
