ID A0A0W1A3S5_9GAMM Unreviewed; 443 AA.
AC A0A0W1A3S5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Flavin containing monooxygenae {ECO:0000313|EMBL:KTD75956.1};
GN ORFNames=Lwor_2522 {ECO:0000313|EMBL:KTD75956.1};
OS Legionella worsleiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45076 {ECO:0000313|EMBL:KTD75956.1, ECO:0000313|Proteomes:UP000054662};
RN [1] {ECO:0000313|EMBL:KTD75956.1, ECO:0000313|Proteomes:UP000054662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49508 {ECO:0000313|EMBL:KTD75956.1,
RC ECO:0000313|Proteomes:UP000054662};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD75956.1}.
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DR EMBL; LNZC01000031; KTD75956.1; -; Genomic_DNA.
DR RefSeq; WP_058494265.1; NZ_UGPA01000001.1.
DR AlphaFoldDB; A0A0W1A3S5; -.
DR STRING; 45076.Lwor_2522; -.
DR PATRIC; fig|45076.6.peg.2770; -.
DR Proteomes; UP000054662; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054662}.
SQ SEQUENCE 443 AA; 51547 MW; 07AD820A74E97E0B CRC64;
MEIERTHKKS SSPRICVIGA GPSGIAAIKN LQEHGLTNIT AFEKNNQIGG NWVYDEQNNH
SSVYETTHII SSKRWSEFDD FPMPADYSDY PSHTQLLDYF HSYAQKFNLH QYIRFNTTVI
KATRTEDDLW HILYEDAQGQ HEEHYDYLLV ANGHHWDPYM PEYQGEFSGE VLHSHQYKKA
SVFKNKRVLV IGGGNSACDV AVEISRVSPK TCISMRRGYH IFPKFIFGKP TDDAVAKIQW
MPGWLRQKFI SLVVRGLQGR YGKYKLMKPD CGPLEIHPTI NSELLYFIRH GKITPRPGLS
HFSDRVVHFT DGSQDEFDTV IFATGYKISF PFFDKECLDF SNVTQVPLYR KMMHPDYDNL
YFIGLCQPQG CIWPLADYQA KIVARIIAGT LERPKQLHQK IEKEMKRPHY RFKSNRRHAL
EVDYHVFRRE LLDMLEKNKV VGT
//
