ID A0A127VA89_9SPHI Unreviewed; 395 AA.
AC A0A127VA89;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=AY601_1154 {ECO:0000313|EMBL:AMP98081.1};
OS Pedobacter cryoconitis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=188932 {ECO:0000313|EMBL:AMP98081.1, ECO:0000313|Proteomes:UP000071561};
RN [1] {ECO:0000313|EMBL:AMP98081.1, ECO:0000313|Proteomes:UP000071561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 27485 {ECO:0000313|EMBL:AMP98081.1,
RC ECO:0000313|Proteomes:UP000071561};
RA Lee J., Kim O.-S.;
RT "Complete genome sequence of Pedobacter cryoconitis PAMC 27485.";
RL Submitted (MAR-2016) 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}.
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DR EMBL; CP014504; AMP98081.1; -; Genomic_DNA.
DR RefSeq; WP_068397721.1; NZ_CP014504.1.
DR AlphaFoldDB; A0A127VA89; -.
DR KEGG; pcm:AY601_1154; -.
DR PATRIC; fig|188932.3.peg.1191; -.
DR OrthoDB; 9782160at2; -.
DR Proteomes; UP000071561; Chromosome.
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:UP000071561}.
FT DOMAIN 11..79
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 303..337
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 47
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
SQ SEQUENCE 395 AA; 43771 MW; 8EAFEDB83FEA5A12 CRC64;
METINLLQDK KIAIVGGGPG GLTLARLLQL KGANVKVYER DFNNEARVQG AIVDLHFESG
LKVMEDAGLM EAFKANYMPG ADKFRLVDKN AKILADEHEQ SSDESFGDEH FRPEIDRGAL
RNILIAGLLP DTVVWDSQFE HMVQVNNIWE LQFKNGTTAT ADLVIGAEGY RSKIRPYVTD
IKALYSGATI IQGEIDDPEK ECPEIYALVN KGNLIAMGSG KTIAAQPRGD GGLTYYASSL
YPEDWIKTSG IDFNDSEKVY TYLVNYYEGW DPIFFTLFKA CSHFVPRPLN YFPLDQHWEA
KPNLTLIGDA AHLMPPSGEG VNTAMLDALD LSECLTSGGF QNIEAAIAAY ENQMQLRAKL
LGQEALEEIK DFASPSEESI KKLIKQFTPI GLSKE
//
