ID   N1USX5_LEPIR            Unreviewed;       455 AA.
AC   N1USX5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Flavin-binding monooxygenase-like protein {ECO:0000313|EMBL:EMY26774.1};
GN   ORFNames=LEP1GSC115_4457 {ECO:0000313|EMBL:EMY26774.1};
OS   Leptospira interrogans serovar Australis str. 200703203.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1085541 {ECO:0000313|EMBL:EMY26774.1, ECO:0000313|Proteomes:UP000012220};
RN   [1] {ECO:0000313|EMBL:EMY26774.1, ECO:0000313|Proteomes:UP000012220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200703203 {ECO:0000313|EMBL:EMY26774.1,
RC   ECO:0000313|Proteomes:UP000012220};
RA   Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA   Sanka R., DePew J., Purushe J., Picardeau M., Werts C., Goarant C.,
RA   Vinetz J.M., Sutton G.G., Nierman W.C., Fouts D.E.;
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:EMY26774.1}.
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DR   EMBL; AHNY02000077; EMY26774.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1USX5; -.
DR   BioCyc; LINT1085541:G11IQ-442-MONOMER; -.
DR   Proteomes; UP000012220; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:EMY26774.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ   SEQUENCE   455 AA;  52250 MW;  1A3814BFC71159B6 CRC64;
     MKSNARVCVV GAGPSGIAAG KNCVEYGLDV VIFEKNDKVG GNWVFNAKTG HSSVYENTHI
     ISSKVWSEYE DFPMPEDYPE YPNHKQLQAY FESYAKHFGV YKKIRFHHTI QKITKTPNEE
     WKVEYTNASK KKKVEFFDVL MVANGHHWDP KYPEYEGKFT GKFLHSHDFK GVTNEWKGKD
     ILVIGAGNSA CDVAVESARV ANSVKLSMRS PQWFFPKFLF GMPSDVFAAK TPNWIPSIIK
     QFALSKLIYI LQGSYKNYGL PENKNLALSH HPTLNSDLLD FIRHGRINPR PAIKKLHGKE
     VEFIDGTKER FDIICACTGF WTTFPFFDKS FIDFQHVEKI PLFRKMIHND FQNLYFIGLF
     QPVGCIWPMA DYQAKLACLE ILGKYKRPQN LKAAIQYEID HPHFTFERGQ RHAVEVDYHS
     FRKELRLELL KAGVDIGKPP GGNKSLYKNF PKAAS
//