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Database: UniProt
Entry: A0A1I2F080_9BURK
LinkDB: A0A1I2F080_9BURK
Original site: A0A1I2F080_9BURK 
ID   A0A1I2F080_9BURK        Unreviewed;       449 AA.
AC   A0A1I2F080;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=L-ornithine N5-oxygenase {ECO:0000313|EMBL:SFE98429.1};
GN   ORFNames=SAMN04489711_1098 {ECO:0000313|EMBL:SFE98429.1};
OS   Paracidovorax wautersii.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=1177982 {ECO:0000313|EMBL:SFE98429.1, ECO:0000313|Proteomes:UP000199119};
RN   [1] {ECO:0000313|EMBL:SFE98429.1, ECO:0000313|Proteomes:UP000199119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27981 {ECO:0000313|EMBL:SFE98429.1,
RC   ECO:0000313|Proteomes:UP000199119};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FONX01000009; SFE98429.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2F080; -.
DR   STRING; 1177982.SAMN04489711_1098; -.
DR   OrthoDB; 7527071at2; -.
DR   Proteomes; UP000199119; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase 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;
FT   REGION          430..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  49683 MW;  86914E1C62FF6B23 CRC64;
     MQPIHDLIGI GFGPSNVALA IALEEQRDAH GRAVAPFFIE RQPAFAWHPH MLLAQSHMQI
     SFLKDLVTLR HPRSRFTFLN YLHEQGRLPD FINLKSFYPS RQEFNDYLRW AAGHFEDRCA
     YGEDVFEVLP ETAEDGSVQA LRVRSRDVAG AVHERLARNL IVGVGGSARI PEVFRGLRGD
     PRVFHSSTYL RDMAACGDAR RIAVVGAGQS AAEIFMDLQG RPQAPEVDWV MRARAIRPAD
     DSPFVNEVFN AQFTDYMFGC SCAQREALLR EYAHTNYAVA DLDLIQQVFK VFYEQRVAAS
     ERLRMLRQHE VTAAQADASG IHFTLRDGAS GQQRVERYDA AVLATGYERV AHRQVLAPLA
     RYLGDFTVDR HYRIQATPGF KPGIFLQGAC EDSHGLSDTL LSVTAVRSGE IGGVIAASLL
     GAEGPRHAAA GRRSGAGGAS ESEETALYA
//
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