ID A0A085YZI4_9FLAO Unreviewed; 386 AA.
AC A0A085YZI4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=IX38_20210 {ECO:0000313|EMBL:KFE97597.1};
OS Chryseobacterium luteum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=421531 {ECO:0000313|EMBL:KFE97597.1, ECO:0000313|Proteomes:UP000028703};
RN [1] {ECO:0000313|EMBL:KFE97597.1, ECO:0000313|Proteomes:UP000028703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18605 {ECO:0000313|EMBL:KFE97597.1,
RC ECO:0000313|Proteomes:UP000028703};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Chryseobacterium luteum DSM 18605.";
RL Submitted (JUL-2014) 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:KFE97597.1}.
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DR EMBL; JPRO01000024; KFE97597.1; -; Genomic_DNA.
DR RefSeq; WP_034707572.1; NZ_JPRO01000024.1.
DR AlphaFoldDB; A0A085YZI4; -.
DR STRING; 421531.IX38_20210; -.
DR eggNOG; COG0654; Bacteria.
DR OrthoDB; 9782160at2; -.
DR Proteomes; UP000028703; 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}.
FT DOMAIN 8..172
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 300..361
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 43
FT /ligand="NADPH"
FT /ligand_id="ChEBI:CHEBI:57783"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
FT BINDING 306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00845"
SQ SEQUENCE 386 AA; 43575 MW; 953A54C5612CBD4A CRC64;
MLIENKSIAI VGGGPGGLTL ARLLQLKNAQ VKVYERDLNK NARVQGSPLD MHEGSGMDAL
RNADLLDEFK KNYRPGADKM LIVNEHAEIL FTDHETKRDE DFGNEDFRPE IDRGPLRNML
LDSLKPETVV WDRHFISMEA QNEGWLLHFK NGLSAYADLV IAADGANSRI RPYLTDLKPV
YSGILMLEGN VYHAEKTAPH IKALIKDGKI MAFGNNKNLL LGQKGNGDLG FYASFRANEN
WAAESGLDFS DQKEMLKWFK KEYAEWGSIW YELFENASVP FIPRPIYSMP LDQSWETKPN
LILLGDAAHV MPPFAGEGAN MAMLDALELS ECLTSDRFTT LKEAISHYEI QMRKRAAEAT
KESLENGDKM HSEKALDNML EFFTSH
//
