PVDA_PSEAE
ID PVDA_PSEAE Reviewed; 443 AA.
AC Q51548;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=L-ornithine N(5)-monooxygenase {ECO:0000303|PubMed:17900176};
DE EC=1.14.13.195 {ECO:0000269|PubMed:17015659, ECO:0000269|PubMed:17900176};
DE AltName: Full=L-ornithine N(5)-hydroxylase {ECO:0000303|PubMed:17015659};
DE Short=Ornithine hydroxylase {ECO:0000303|PubMed:17900176};
DE AltName: Full=L-ornithine N(5)-oxygenase {ECO:0000303|PubMed:8106324};
DE AltName: Full=Pyoverdin biosynthesis protein A {ECO:0000303|PubMed:8106324};
GN Name=pvdA {ECO:0000303|PubMed:8106324}; Synonyms=pvd-1;
GN OrderedLocusNames=PA2386;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8106324; DOI=10.1128/jb.176.4.1128-1140.1994;
RA Visca P., Ciervo A., Orsi N.;
RT "Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin
RT biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa.";
RL J. Bacteriol. 176:1128-1140(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=17015659; DOI=10.1128/jb.00949-06;
RA Ge L., Seah S.Y.;
RT "Heterologous expression, purification, and characterization of an l-
RT ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis
RT in Pseudomonas aeruginosa.";
RL J. Bacteriol. 188:7205-7210(2006).
RN [4]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17900176; DOI=10.1021/bi700932q;
RA Meneely K.M., Lamb A.L.;
RT "Biochemical characterization of a flavin adenine dinucleotide-dependent
RT monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests
RT a novel reaction mechanism.";
RL Biochemistry 46:11930-11937(2007).
RN [5]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLY-215.
RX PubMed=18757814; DOI=10.1099/mic.0.2008/018804-0;
RA Imperi F., Putignani L., Tiburzi F., Ambrosi C., Cipollone R., Ascenzi P.,
RA Visca P.;
RT "Membrane-association determinants of the omega-amino acid monooxygenase
RT PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa.";
RL Microbiology 154:2804-2813(2008).
RN [6]
RP FUNCTION.
RX PubMed=19368334; DOI=10.1021/bi900442z;
RA Meneely K.M., Barr E.W., Bollinger J.M. Jr., Lamb A.L.;
RT "Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas
RT aeruginosa: substrate triggering of O2 addition but not flavin reduction.";
RL Biochemistry 48:4371-4376(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD; NADP;
RP L-ORNITHINE AND N(5)-HYDROXY-L-ORNITHINE, AND COFACTOR.
RX PubMed=21757711; DOI=10.1074/jbc.m111.265876;
RA Olucha J., Meneely K.M., Chilton A.S., Lamb A.L.;
RT "Two structures of an N-hydroxylating flavoprotein monooxygenase: ornithine
RT hydroxylase from Pseudomonas aeruginosa.";
RL J. Biol. Chem. 286:31789-31798(2011).
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 pyoverdin. Pyoverdin is a
CC hydroxamate siderophore composed of a 6,7-dihydroxyquinoline-containing
CC fluorescent chromophore joined to the N-terminus of a partly cyclic
CC octapeptide (D-Ser-L-Arg-D-Ser-L-N(5)-OH-Orn-L-Lys-L-N(5)-OH-Orn-L-Thr-
CC L-Thr in strain PAO1). Specific for NADPH, which plays a role in
CC stabilization of the C4a-hydroperoxyflavin intermediate.
CC {ECO:0000269|PubMed:17015659, ECO:0000269|PubMed:19368334,
CC ECO:0000269|PubMed:8106324}.
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:0000269|PubMed:17015659, ECO:0000269|PubMed:17900176};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:21757711};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:21757711};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.58 mM for L-ornithine {ECO:0000269|PubMed:17015659};
CC KM=0.6 mM for L-ornithine {ECO:0000269|PubMed:17900176};
CC KM=160 uM for NADPH {ECO:0000269|PubMed:17015659};
CC KM=21.9 uM for FAD(+) {ECO:0000269|PubMed:17015659};
CC Vmax=1.34 umol/min/mg enzyme {ECO:0000269|PubMed:17015659};
CC Vmax=479 nmol/min/mg enzyme {ECO:0000269|PubMed:17015659};
CC pH dependence:
CC Optimum pH is 8.0-8.5. {ECO:0000269|PubMed:17015659,
CC ECO:0000269|PubMed:17900176};
CC -!- PATHWAY: Siderophore biosynthesis; pyoverdin biosynthesis.
CC {ECO:0000269|PubMed:8106324}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17015659}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:18757814}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18757814}; Cytoplasmic side
CC {ECO:0000269|PubMed:18757814}.
CC -!- SIMILARITY: Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-
CC oxygenase family. {ECO:0000305}.
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DR EMBL; Z25465; CAA80959.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05774.1; -; Genomic_DNA.
DR PIR; A49892; A49892.
DR PIR; D83346; D83346.
DR RefSeq; NP_251076.1; NC_002516.2.
DR RefSeq; WP_003114509.1; NZ_QZGE01000021.1.
DR PDB; 3S5W; X-ray; 1.90 A; A/B=1-443.
DR PDB; 3S61; X-ray; 3.03 A; A/B=1-443.
DR PDBsum; 3S5W; -.
DR PDBsum; 3S61; -.
DR AlphaFoldDB; Q51548; -.
DR SMR; Q51548; -.
DR IntAct; Q51548; 3.
DR MINT; Q51548; -.
DR STRING; 208964.PA2386; -.
DR PaxDb; Q51548; -.
DR PRIDE; Q51548; -.
DR EnsemblBacteria; AAG05774; AAG05774; PA2386.
DR GeneID; 882167; -.
DR KEGG; pae:PA2386; -.
DR PATRIC; fig|208964.12.peg.2496; -.
DR PseudoCAP; PA2386; -.
DR HOGENOM; CLU_020931_2_0_6; -.
DR InParanoid; Q51548; -.
DR OMA; YHGNTNY; -.
DR PhylomeDB; Q51548; -.
DR BioCyc; MetaCyc:MON-15307; -.
DR BioCyc; PAER208964:G1FZ6-2424-MON; -.
DR BRENDA; 1.14.13.195; 5087.
DR UniPathway; UPA00019; -.
DR PHI-base; PHI:6937; -.
DR PHI-base; PHI:7942; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:PseudoCAP.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031172; F:ornithine N5-monooxygenase activity; IEA:RHEA.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0002049; P:pyoverdine biosynthetic process; IDA:PseudoCAP.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; FAD; Flavoprotein;
KW Membrane; Monooxygenase; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..443
FT /note="L-ornithine N(5)-monooxygenase"
FT /id="PRO_0000204029"
FT BINDING 45..53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 130
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 215..218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 240
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 254..257
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 284..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 407..409
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:21757711"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:21757711"
FT MUTAGEN 215
FT /note="G->D: Loss of function."
FT /evidence="ECO:0000269|PubMed:18757814"
FT CONFLICT 384..443
FT /note="TDERCKVAIYAQGFSQASHGLSDTLLSVLPVRAEEISGSLYQHLKPGTAARA
FT LHEHALAS -> PTSAARWRSTRRASARPAMASATPCCRCCRCVPRKSPAPCTST (in
FT Ref. 1; CAA80959)"
FT /evidence="ECO:0000305"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 20..36
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3S5W"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3S61"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 124..138
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 141..151
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:3S61"
FT HELIX 290..306
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 317..325
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:3S5W"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 341..351
FT /evidence="ECO:0007829|PDB:3S5W"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:3S5W"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:3S5W"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:3S5W"
FT HELIX 412..427
FT /evidence="ECO:0007829|PDB:3S5W"
SQ SEQUENCE 443 AA; 49478 MW; 3971A2B223802ACA CRC64;
MTQATATAVV HDLIGVGFGP SNIALAIALQ ERAQAQGALE VLFLDKQGDY RWHGNTLVSQ
SELQISFLKD LVSLRNPTSP YSFVNYLHKH DRLVDFINLG TFYPCRMEFN DYLRWVASHF
QEQSRYGEEV LRIEPMLSAG QVEALRVISR NADGEELVRT TRALVVSPGG TPRIPQVFRA
LKGDGRVFHH SQYLEHMAKQ PCSSGKPMKI AIIGGGQSAA EAFIDLNDSY PSVQADMILR
ASALKPADDS PFVNEVFAPK FTDLIYSREH AERERLLREY HNTNYSVVDT DLIERIYGVF
YRQKVSGIPR HAFRCMTTVE RATATAQGIE LALRDAGSGE LSVETYDAVI LATGYERQLH
RQLLEPLAEY LGDHEIGRDY RLQTDERCKV AIYAQGFSQA SHGLSDTLLS VLPVRAEEIS
GSLYQHLKPG TAARALHEHA LAS
