ID A0A0M9XAQ1_9ACTN Unreviewed; 381 AA.
AC A0A0M9XAQ1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ADK41_02700 {ECO:0000313|EMBL:KOT45453.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT45453.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT45453.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT45453.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-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:KOT45453.1}.
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DR EMBL; LGCN01000017; KOT45453.1; -; Genomic_DNA.
DR RefSeq; WP_030823310.1; NZ_LGCN01000017.1.
DR AlphaFoldDB; A0A0M9XAQ1; -.
DR PATRIC; fig|36816.3.peg.574; -.
DR OrthoDB; 3217377at2; -.
DR Proteomes; UP000037773; 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:UP000037773}.
FT DOMAIN 11..205
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 298..353
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 46
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 110
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 304
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
SQ SEQUENCE 381 AA; 41182 MW; 2CCD1C358C098F7E CRC64;
MNSPEPARAR ISVIGAGPGG LTCARILQQH GMAVTVYDRD RGPDARNQGG TLDLHADNGQ
IALREAGLLD EFFKLARPEG QEMRQMDPTG TITSHEVPAP DELFKPEIDR GQLRNLLLDS
LQPGTVRWGR AIDTISGPDD GPRQLHFTDG TTVQTDLVIG ADGASSRVRP AVSPAVPEYT
GVSFLEAWFS DVENRHPDLA ELVGQGSAHA ADGERGLFAQ RNSGNHIRVY IIQRVPVDWI
STSGLTAEDT DGIRSLLLGE YAHWSPRIRR MITENDGPYV DRPIFALPVP HTWEHNPTVT
LLGDAAHLMP PLGVGVNLAM LDASEIALAL ANATTVADAI RTYEKTMLPR STETAKALEG
GAEHLLSTDA PDFGSDNDAR H
//
