| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.13.196 |
|---|---|
| Description: | L-ornithine N(5)-monooxygenase (NAD(P)H). |
| Cath: | 3.50.50.60; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 1.14.13.196 |
| BRENDA Enzyme Link: | BRENDA 1.14.13.196 |
| KEGG Enzyme Link: | KEGG1.14.13.196 |
| BioCyc Enzyme Link: | BioCyc 1.14.13.196 |
| ExPASy Enzyme Link: | ExPASy1.14.13.196 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.13.196 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.13.196 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.13.196 |
| IntEnz Enzyme Link: | IntEnz 1.14.13.196 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.13.196 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:41512 | L-ornithine + NADH + O2 = H2O + N(5)-hydroxy-L-ornithine + NAD(+) |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[NH2;+0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:9]-[NH;+0:10]-[OH;+0:11].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:12] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| sid1, a gene initiating siderophore biosynthesis in Ustilago maydis: molecular characterization, regulation by iron, and role in phytopathogenicity. | Mei B, Budde AD, Leong SA | 1993 Feb 1 | 8430103 |
| Structural insight into the mechanism of oxygen activation and substrate selectivity of flavin-dependent N-hydroxylating monooxygenases. | Franceschini S, Fedkenheuer M, Vogelaar NJ, Robinson HH, Sobrado P, Mattevi A | 2012 Sep 11 | 22928747 |
| Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase. | Mayfield JA, Frederick RE, Streit BR, Wencewicz TA, Ballou DP, DuBois JL | 2010 Oct 1 | 20650894 |
| Aspergillus fumigatus SidA is a highly specific ornithine hydroxylase with bound flavin cofactor. | Chocklett SW, Sobrado P | 2010 Aug 10 | 20614882 |
| dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is indispensable for deferriferrichrysin biosynthesis. | Yamada O, Na Nan S, Akao T, Tominaga M, Watanabe H, Satoh T, Enei H, Akita O | 2003 | 16233371 |
| RHEA:41508 | L-ornithine + NADPH + O2 = H2O + N(5)-hydroxy-L-ornithine + NADP(+) |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[CH;+0:3]=[C;H0;+0:4](-[*:5])-[CH2;+0:6]-[CH;+0:7]=[CH;+0:8]-1.[*:9]-[NH2;+0:10].[O;H0;+0:11]=[O;H0;+0:12]>>[*:9]-[NH;+0:10]-[OH;+0:11].[*:1]-[n+;H0:2]1:[cH;+0:3]:[c;H0;+0:4](-[*:5]):[cH;+0:6]:[cH;+0:7]:[cH;+0:8]:1.[OH2;+0:12] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| sid1, a gene initiating siderophore biosynthesis in Ustilago maydis: molecular characterization, regulation by iron, and role in phytopathogenicity. | Mei B, Budde AD, Leong SA | 1993 Feb 1 | 8430103 |
| Cloning and nucleotide sequence of the pvdA gene encoding the pyoverdin biosynthetic enzyme L-ornithine N5-oxygenase in Pseudomonas aeruginosa. | Visca P, Ciervo A, Orsi N | 1994 Feb | 8106324 |
| Consecutive enzymatic modification of ornithine generates the hydroxamate moieties of the siderophore erythrochelin. | Robbel L, Helmetag V, Knappe TA, Marahiel MA | 2011 Jul 12 | 21650455 |
| Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase. | Mayfield JA, Frederick RE, Streit BR, Wencewicz TA, Ballou DP, DuBois JL | 2010 Oct 1 | 20650894 |
| Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. | Meneely KM, Barr EW, Bollinger JM Jr, Lamb AL | 2009 May 26 | 19368334 |
| Delta-amino group hydroxylation of L-ornithine during coelichelin biosynthesis. | Pohlmann V, Marahiel MA | 2008 May 21 | 18452021 |
| Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism. | Meneely KM, Lamb AL | 2007 Oct 23 | 17900176 |
| Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. | Ge L, Seah SY | 2006 Oct | 17015659 |
| dffA gene from Aspergillus oryzae encodes L-ornithine N5-oxygenase and is indispensable for deferriferrichrysin biosynthesis. | Yamada O, Na Nan S, Akao T, Tominaga M, Watanabe H, Satoh T, Enei H, Akita O | 2003 | 16233371 |