G5EB76
Gene name |
sidA |
Protein name |
L-ornithine N(5)-monooxygenase |
Names |
OMO, L-ornithine N(5)-oxygenase, Siderophore biosynthesis protein A |
Species |
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
KEGG Pathway |
ani:AN5823.2 |
EC number |
1.14.13.196: With NADH or NADPH as one donor, and incorporation of one atom of oxygen |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for G5EB76
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-G5EB76-F1 | Predicted | AlphaFoldDB |
No variants for G5EB76
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for G5EB76 | |||||
No associated diseases with G5EB76
9 regional properties for G5EB76
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | RNA polymerase sigma-70 | 114 - 127 | IPR000943-1 |
| domain | RNA polymerase sigma-70 | 138 - 146 | IPR000943-2 |
| domain | RNA polymerase sigma-70 | 262 - 274 | IPR000943-3 |
| domain | RNA polymerase sigma-70 | 283 - 309 | IPR000943-4 |
| domain | RNA polymerase sigma-70 region 3 | 169 - 245 | IPR007624 |
| domain | RNA polymerase sigma-70 region 2 | 90 - 159 | IPR007627 |
| domain | RNA polymerase sigma-70 region 4 | 258 - 311 | IPR007630 |
| domain | RNA polymerase sigma-70 region 1.2 | 25 - 58 | IPR009042 |
| domain | RNA polymerase sigma-70 like domain | 86 - 311 | IPR014284 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.13.196 | With NADH or NADPH as one donor, and incorporation of one atom of oxygen |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| ornithine N5-monooxygenase activity | Catalysis of the reaction: L-ornithine + O2 + H+ = N5-hydroxy-L-ornithine + H2O. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular iron ion homeostasis | Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell. |
| cellular response to iron ion starvation | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of iron ions. |
| cellular response to oxidative stress | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
| ferrichrome biosynthetic process | The chemical reactions and pathways resulting in the formation of a ferrichrome. Ferrichromes are any of a group of growth-promoting Fe(III) chelates formed by various genera of microfungi. They are homodetic cyclic hexapeptides made up of a tripeptide of glycine (or other small neutral amino acids) and a tripeptide of an N'acyl-N4-hydroxy-L-ornithine. |
| siderophore biosynthetic process | The chemical reactions and pathways resulting in the formation of siderophores, low molecular weight Fe(III)-chelating substances made by aerobic or facultatively anaerobic bacteria, especially when growing under iron deficient conditions. The complexes of Fe(3+)-siderophores have very high stability constants and are taken up by specific transport systems by microorganisms; the subsequent release of iron requires enzymatic action. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEPLQRKSEL | DFQSYRKMPL | AQQRTQRLKP | TSPEELHDLI | CVGFGPASLA | IAIALHDALD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PCLNKCAPTS | GWQPKVAFLE | RQKQFAWHSG | MLVPGSRMQI | SFIKDLATLR | DPRSSFTFLN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| YLHQKDRLIH | FTNLSTFLPA | RMEFEDYMRW | CANQFSDVVT | YGEEVIEVLP | GKSSPDSPVV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DYFTVLSRNV | ETGEISSRSA | RKVVLALGGT | AKLPAELPQD | PRIMHSSKYC | TALPNLLKDN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NEPYNIAVLG | SGQSAAEIFH | DLQKRYPNSR | TSLIMRDTAM | RPSDDSPFVN | EVFNPERTDK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FYNLSAAERE | RSLKADKATN | YSVVRLELIE | EIYHDMYLQR | VKNPDETQWQ | HRILPSRKIT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RVEHYGPNKR | MRVHVRAVKD | GKDSLIGDGK | EVLEVDALMV | ATGYNRNAHE | QLLSKVQYLR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PATQDRWTPS | RDYRVDLDRS | KVSAGAGIWL | QGSNEQTHGL | SDSLLSVLAT | RGGEMVESIF |
| 490 | |||||
| GEQLESAAVP | DTRFRAML |