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BACTU:IDO
Contents
| Species (Taxon ID) | Bacillus thuringiensis. (1428) | |
| Gene Name(s) | ido (ECO:0000303 with PMID:20665018[1]) | |
| Protein Name(s) | L-isoleucine-4-hydroxylase (ECO:0000303 with PMID:20665018[1])
L-isoleucine dioxygenase (ECO:0000303 with PMID:19850012[2]) IDO (ECO:0000303 with PMID:19850012[2]) | |
| External Links | ||
| UniProt | E2GIN1 | |
| EMBL | HM358019 | |
| BioCyc | MetaCyc:MONOMER-17595 | |
| GO | GO:0051213 GO:0008198 GO:0031418 | |
| InterPro | IPR018724 | |
| Pfam | PF10014 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
| GO:0051213 |
dioxygenase activity |
ECO:0000314 |
F |
Table 1, Fig 2, Table 2 |
complete | |||||
|
enables |
GO:0008198 |
ferrous iron binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051213 |
dioxygenase activity |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0051213 |
dioxygenase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0031418 |
L-ascorbic acid binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0055114 |
oxidation-reduction process |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0016491 |
oxidoreductase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Smirnov, SV et al. (2010) Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-hydroxyisoleucine. Appl. Microbiol. Biotechnol. 88 719-26 PubMed GONUTS page
- ↑ 2.0 2.1 2.2 Kodera, T et al. (2009) A novel l-isoleucine hydroxylating enzyme, l-isoleucine dioxygenase from Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine. Biochem. Biophys. Res. Commun. 390 506-10 PubMed GONUTS page
- ↑ 3.0 3.1 Smirnov, SV et al. (2012) A novel family of bacterial dioxygenases that catalyse the hydroxylation of free L-amino acids. FEMS Microbiol. Lett. 331 97-104 PubMed GONUTS page
