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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