ID   PVDA_BURCE              Reviewed;         444 AA.
AC   O51940;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000250|UniProtKB:Q51548};
DE            EC=1.14.13.195 {ECO:0000250|UniProtKB:Q51548};
DE   AltName: Full=L-ornithine N(5)-hydroxylase {ECO:0000250|UniProtKB:Q51548};
DE            Short=Ornithine hydroxylase {ECO:0000250|UniProtKB:Q51548};
DE   AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:10456885};
GN   Name=pvdA {ECO:0000303|PubMed:10456885};
OS   Burkholderia cepacia (Pseudomonas cepacia).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=K56-2;
RX   PubMed=10456885; DOI=10.1128/iai.67.9.4443-4455.1999;
RA   Sokol P.A., Darling P., Woods D.E., Mahenthiralingam E., Kooi C.;
RT   "Role of ornibactin biosynthesis in the virulence of Burkholderia cepacia:
RT   characterization of pvdA, the gene encoding L-ornithine N(5)-oxygenase.";
RL   Infect. Immun. 67:4443-4455(1999).
CC   -!- FUNCTION: Catalyzes the conversion of L-ornithine to N(5)-
CC       hydroxyornithine, the first step in the biosynthesis of all
CC       hydroxamate-containing siderophores, such as ornibactin.
CC       {ECO:0000269|PubMed:10456885}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine +
CC         NADP(+); Xref=Rhea:RHEA:41508, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78275; EC=1.14.13.195;
CC         Evidence={ECO:0000250|UniProtKB:Q51548};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q51548};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q51548};
CC   -!- PATHWAY: Siderophore biosynthesis; ornibactin biosynthesis.
CC       {ECO:0000269|PubMed:10456885}.
CC   -!- DISRUPTION PHENOTYPE: Less virulent than wild-type in chronic and acute
CC       models of respiratory infection. {ECO:0000269|PubMed:10456885}.
CC   -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC       oxygenase family. {ECO:0000305}.
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DR   EMBL; AF013993; AAB94515.1; -; Genomic_DNA.
DR   AlphaFoldDB; O51940; -.
DR   SMR; O51940; -.
DR   STRING; 292.DM42_51; -.
DR   eggNOG; COG3486; Bacteria.
DR   UniPathway; UPA00018; -.
DR   GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
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; -; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR025700; Lys/Orn_oxygenase.
DR   PANTHER; PTHR42802; PTHR42802; 1.
DR   Pfam; PF13434; K_oxygenase; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Monooxygenase; NADP; Oxidoreductase.
FT   CHAIN           1..444
FT                   /note="L-ornithine N(5)-monooxygenase"
FT                   /id="PRO_0000204030"
FT   REGION          420..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         40..48
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         59
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         125
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         211..214
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         236
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         250..253
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         280..282
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
FT   BINDING         408..410
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q51548"
SQ   SEQUENCE   444 AA;  50011 MW;  4A30C953E32582D6 CRC64;
     MQRETVFDLI GVGFGPSNLA LAVRLAERSG AHTLAHCFVE RQPAFGWHRG MLLDDCRMQI
     SFLKDLVTMR DPKSRYTFIN YLFERGRLNE FVNLKNFYPT RVEFHDYLSW VADAFDDRVH
     YSETVLGIEP VRGDGARIDA LRVLSRDAAG HERQRVTRAL SVGVGGTPAI PDAFAALGRD
     RVIHSSSYLT DIDRLVASPD GERRRVAVIG AGQSAAEVFI DLARRFPHVD ANLVMRAGAL
     KPADDSPFVN EIFSPEFTDV VYAQPQDARR ALLERYRDTN YAVVDRPLIE QIYEMLYLQR
     IDGTPRHALL ANSAIEAAVR TADGRIELTL RDRMSGATRI ERFDALVLAT GYRRDTHSAL
     LEGLAPHLGD ALTRGDVTRD YLLATPEHFA PRIYLQGCCE DSHGRPTRCC RSWRAVRTKS
     ARRSKTGSRP RTMKAWPGPR TKND