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PSEAE:PVDA

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Species (Taxon ID) Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1). (208964)
Gene Name(s) pvdA (ECO:0000303 with PMID:8106324[1]) (synonyms: pvd-1)
Protein Name(s) L-ornithine N(5)-monooxygenase (ECO:0000303 with PMID:17900176[2])

L-ornithine N(5)-hydroxylase (ECO:0000303 with PMID:17015659[3]) Ornithine hydroxylase (ECO:0000303 with PMID:17900176[2]) L-ornithine N(5)-oxygenase (ECO:0000303 with PMID:8106324[1]) Pyoverdin biosynthesis protein A (ECO:0000303 with PMID:8106324[1])

External Links
UniProt Q51548
EMBL Z25465
AE004091
PIR A49892
D83346
RefSeq NP_251076.1
WP_003114509.1
PDB 3S5W
3S61
PDBsum 3S5W
3S61
ProteinModelPortal Q51548
SMR Q51548
IntAct Q51548
MINT Q51548
STRING 208964.PA2386
PaxDb Q51548
PRIDE Q51548
EnsemblBacteria AAG05774
GeneID 882167
KEGG pae:PA2386
PATRIC fig|208964.12.peg.2496
PseudoCAP PA2386
eggNOG ENOG4105F1Y
COG3486
HOGENOM HOG000237193
InParanoid Q51548
KO K10531
OMA CEGTHGL
PhylomeDB Q51548
BioCyc MetaCyc:MONOMER-15307
PAER208964:G1FZ6-2424-MONOMER
BRENDA 1.14.13.B10
UniPathway UPA00019
Proteomes UP000002438
GO GO:0005737
GO:0005886
GO:0004497
GO:0034338
GO:0006879
GO:0002049
Gene3D 3.50.50.60
InterPro IPR036188
IPR025700
Pfam PF13434
SUPFAM SSF51905

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0034338

short-chain carboxylesterase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11101
PANTHER:PTN000546472
UniProtKB:P9WK87

F

Seeded From UniProt

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001009003
UniProtKB:G5EB76

P

Seeded From UniProt

part_of

GO:0005737

cytoplasm

PMID:22498339[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

part_of

GO:0005737

cytoplasm

PMID:18757814[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

involved_in

GO:0002049

pyoverdine biosynthetic process

PMID:15317763[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

involved_in

GO:0002049

pyoverdine biosynthetic process

PMID:20650894[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

enables

GO:0004497

monooxygenase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0503

F

Seeded From UniProt

involved_in

GO:0002049

pyoverdine biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00019

P

Seeded From UniProt

enables

GO:0034338

short-chain carboxylesterase activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11101
PANTHER:PTN000546472
UniProtKB:P9WK87

F

Seeded From UniProt

involved_in

GO:0006879

cellular iron ion homeostasis

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001009003
UniProtKB:G5EB76

P

Seeded From UniProt

part_of

GO:0005737

cytoplasm

PMID:22498339[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

part_of

GO:0005737

cytoplasm

PMID:18757814[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

involved_in

GO:0002049

pyoverdine biosynthetic process

PMID:15317763[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

involved_in

GO:0002049

pyoverdine biosynthetic process

PMID:20650894[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0997
UniProtKB-KW:KW-1003
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

part_of

GO:0005886

plasma membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003

C

Seeded From UniProt

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

enables

GO:0004497

monooxygenase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0503

F

Seeded From UniProt

part_of

GO:0005886

plasma membrane

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

involved_in

GO:0002049

pyoverdine biosynthetic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00019

P

Seeded From UniProt

GO:0031172

ornithine N5-monooxygenase activity

PMID:30257953[9]

ECO:0005636

F

Figure 1B & 1C show increased expression and production of pyoverdine in Pseudomonas aeruginosa, the final product of the biosynthetic pathway that pvdA/L-ornithine N(5)-monooxygenase is involved in, when iron levels are low, denoting upregulation of pvdA/L-ornithine N(5)-monooxygenase under iron-deficient conditions.

complete
CACAO 13552

GO:0002049

pyoverdine biosynthetic process

PMID:30257953[9]

ECO:0005636

P

Figure 1B & 1C show increased expression and production of pyoverdine in Pseudomonas aeruginosa, the final product of the biosynthetic pathway that pvdA/L-ornithine N(5)-monooxygenase is involved in, when iron levels are low.

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Visca, P et al. (1994) Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa. J. Bacteriol. 176 1128-40 PubMed GONUTS page
  2. 2.0 2.1 Meneely, KM & Lamb, AL (2007) Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism. Biochemistry 46 11930-7 PubMed GONUTS page
  3. Ge, L & Seah, SY (2006) Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. J. Bacteriol. 188 7205-10 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  5. 5.0 5.1 Guillon, L et al. (2012) High cellular organization of pyoverdine biosynthesis in Pseudomonas aeruginosa: clustering of PvdA at the old cell pole. Environ. Microbiol. 14 1982-94 PubMed GONUTS page
  6. 6.0 6.1 Imperi, F et al. (2008) Membrane-association determinants of the omega-amino acid monooxygenase PvdA, a pyoverdine biosynthetic enzyme from Pseudomonas aeruginosa. Microbiology (Reading, Engl.) 154 2804-13 PubMed GONUTS page
  7. 7.0 7.1 Vandenende, CS et al. (2004) Functional characterization of an aminotransferase required for pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa PAO1. J. Bacteriol. 186 5596-602 PubMed GONUTS page
  8. 8.0 8.1 Mayfield, JA et al. (2010) Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase. J. Biol. Chem. 285 30375-88 PubMed GONUTS page
  9. 9.0 9.1 Goss, CH et al. (2018) Gallium disrupts bacterial iron metabolism and has therapeutic effects in mice and humans with lung infections. Sci Transl Med 10 PubMed GONUTS page