ID S2YMT9_9ACTN Unreviewed; 377 AA.
AC S2YMT9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=HMPREF1211_05781 {ECO:0000313|EMBL:EPD58842.1};
OS Streptomyces sp. HGB0020.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD58842.1, ECO:0000313|Proteomes:UP000014410};
RN [1] {ECO:0000313|EMBL:EPD58842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0020 {ECO:0000313|EMBL:EPD58842.1};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptomyces sp. HGB0020.";
RL Submitted (APR-2013) 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:EPD58842.1}.
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DR EMBL; AGER01000023; EPD58842.1; -; Genomic_DNA.
DR RefSeq; WP_016435683.1; NZ_KE150428.1.
DR AlphaFoldDB; S2YMT9; -.
DR STRING; 1078086.HMPREF1211_05781; -.
DR PATRIC; fig|1078086.3.peg.5835; -.
DR HOGENOM; CLU_009665_4_0_11; -.
DR OrthoDB; 3217377at2; -.
DR Proteomes; UP000014410; 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; 2.
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:UP000014410}.
FT DOMAIN 9..174
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 296..331
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 44
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 51
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 108
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
SQ SEQUENCE 377 AA; 40489 MW; 2EFB30DBC5A1407D CRC64;
MNTTHAPRIA IVGAGPGGLT CARILQRHGI TVTVLDRDAG PDARNQGGTL DLHADNGQLA
LREAGLLDAF FRLARPEGQE MRQLDTAGTT LFHHLPEEGE QFKPEIDRGH LRDLLLDSLS
PGTVCWGRTL TKVSGPAEGP RTLHFADGTT VEADLVIGAD GAWSTVRRAV SPATPRYTGV
SFLEARFDDV EKRHPRVAGL VGQGSTAAAD GERALFAQRN SGDHIRVYVI QQVPADWIAG
AGLTPDDTDG IRRVLLERYA HWSPRMRELI ADNDGAYVDR PIFALPVPHT WDRNPTVTLL
GDAAHLMPPL GVGVNLAMLD ACELALAIAH NGTVAEAVRA YERTMVPRST ETARLLDGAT
AGLLSTELPD FAGADRA
//
