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Database: UniProt
Entry: A0A0M9GEP9_9PSED
LinkDB: A0A0M9GEP9_9PSED
Original site: A0A0M9GEP9_9PSED 
ID   A0A0M9GEP9_9PSED        Unreviewed;       438 AA.
AC   A0A0M9GEP9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Lysine/ornithine N-monooxygenase {ECO:0000313|EMBL:KPA89293.1};
GN   ORFNames=PF66_04144 {ECO:0000313|EMBL:KPA89293.1};
OS   Pseudomonas fuscovaginae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA89293.1, ECO:0000313|Proteomes:UP000037931};
RN   [1] {ECO:0000313|EMBL:KPA89293.1, ECO:0000313|Proteomes:UP000037931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA89293.1,
RC   ECO:0000313|Proteomes:UP000037931};
RX   PubMed=26422147;
RA   Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA   Cruz C.V., Oliva R.;
RT   "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT   Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL   PLoS ONE 10:E0139256-E0139256(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC       oxygenase family. {ECO:0000256|ARBA:ARBA00007588}.
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:KPA89293.1}.
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DR   EMBL; JSYZ01000016; KPA89293.1; -; Genomic_DNA.
DR   RefSeq; WP_054063659.1; NZ_JSYZ01000016.1.
DR   AlphaFoldDB; A0A0M9GEP9; -.
DR   STRING; 50340.PF66_04144; -.
DR   PATRIC; fig|50340.43.peg.1447; -.
DR   OrthoDB; 7527071at2; -.
DR   Proteomes; UP000037931; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR025700; Lys/Orn_oxygenase.
DR   PANTHER; PTHR42802:SF1; L-ORNITHINE N(5)-MONOOXYGENASE; 1.
DR   PANTHER; PTHR42802; MONOOXYGENASE; 1.
DR   Pfam; PF13434; Lys_Orn_oxgnase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   Monooxygenase {ECO:0000313|EMBL:KPA89293.1};
KW   Oxidoreductase {ECO:0000313|EMBL:KPA89293.1}.
SQ   SEQUENCE   438 AA;  48688 MW;  8328B5B476AA2B95 CRC64;
     MKTYDLIGIG IGPFNLSLAA LAEPTGLDTL FLDKRDAFAW HPGMLVSNGQ LQVSPLKDCV
     TLAAPTSRYS FLNYLAEHRR LYSFINKGGA CTSRKEFADY YGWVARQLSN LRFAQEVLDV
     VECNDGYTVV TAEQSYHARA VAIGVGISPR VPECARPWLG DAIYHVADFL HREALRPGEQ
     VLVVGGGQSG AETVEQLLGT PALGGFTWVT SRSNLFAMDD NAFVNEAFCP AYNQRFQNLP
     MAQRSHAVQQ ERLTSDGISA DLCNRLYEQL YERRVGQEPR PPIDILQAAV LDGLEPDGRR
     WRARLRSLSS GSQRTLVVDR VILATGFQPC PQPYVDALLA KARRDSGLPL IDANYCVQFA
     TPMPGPVYLQ NRSLVQHGLQ SVNLSMVAYR NSRILNDLLG YEYFQAEPDT PMFSHLDALP
     EAPARHLEPR HALSLVQY
//
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