ID   D3HIZ8_LEGLN            Unreviewed;       454 AA.
AC   D3HIZ8;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Putative kynurenine 3-monooxygenase {ECO:0000313|EMBL:CBJ12379.1};
GN   OrderedLocusNames=LLO_1994 {ECO:0000313|EMBL:CBJ12379.1};
OS   Legionella longbeachae serogroup 1 (strain NSW150).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ12379.1, ECO:0000313|Proteomes:UP000001060};
RN   [1] {ECO:0000313|EMBL:CBJ12379.1, ECO:0000313|Proteomes:UP000001060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSW150 {ECO:0000313|EMBL:CBJ12379.1,
RC   ECO:0000313|Proteomes:UP000001060};
RX   PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA   Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA   Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA   Etienne J., Hartland E., Buchrieser C.;
RT   "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT   unique strategies to cause Legionnaires' disease.";
RL   PLoS Genet. 6:E1000851-E1000851(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FN650140; CBJ12379.1; -; Genomic_DNA.
DR   RefSeq; WP_003636779.1; NC_013861.1.
DR   AlphaFoldDB; D3HIZ8; -.
DR   STRING; 661367.LLO_1994; -.
DR   KEGG; llo:LLO_1994; -.
DR   eggNOG; COG0654; Bacteria.
DR   HOGENOM; CLU_023210_0_1_6; -.
DR   OrthoDB; 9782160at2; -.
DR   Proteomes; UP000001060; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR46028; KYNURENINE 3-MONOOXYGENASE; 1.
DR   PANTHER; PTHR46028:SF2; KYNURENINE 3-MONOOXYGENASE; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:CBJ12379.1};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023033,
KW   ECO:0000313|EMBL:CBJ12379.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001060}.
FT   DOMAIN          3..176
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   454 AA;  52811 MW;  EB30E7A97DEACEB4 CRC64;
     MRIAIIGAGL TGLLLSLYLA RRGYEVDIYE QRSDPRITTH PYDKGRKMSI DLSSRGLLSL
     AEMGLAEKIL SKSVPMRDRV IHLPNGEIIS LAYGKCANDC IHTVSRSQLH FDLLQETESV
     PSIVVHFNRS FVDMDTTSGE FILFDNHLNK HFNIKPFFLF GCDGANSMVR KCIEKQKDVT
     FQYSYFPYQY KELTIPYLEN KTLQLEAMHM WPRENSMLVA QPNYDHSFTC AFLLPSTGDY
     SFEKLTKSYS PQQMLNYFKD QYSDIYPFIS NLENDLYNNP IGSLITINEG HWNIDKVALM
     GDSTHAMVPF LGQGLNCCFE DCYLFNQFLD KYNDDWQTAI PAFEEFRKKD TNAITIMSLE
     NYPELFDSDL QKSILLREIE NYLMVNFKDT FATYHNLTCF SSHSYSYINS IRLIQKEMIL
     DISQTINNIK EINKDKIELF LEDYHKKICK VRIQ
//