B1IV85
Gene name |
rutA |
Protein name |
Pyrimidine monooxygenase RutA |
Names |
|
Species |
Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks) |
KEGG Pathway |
ecl:EcolC_2583 |
EC number |
1.14.99.46: Miscellaneous |
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 B1IV85
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B1IV85-F1 | Predicted | AlphaFoldDB |
No variants for B1IV85
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B1IV85 | |||||
No associated diseases with B1IV85
1 regional properties for B1IV85
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Luciferase-like domain | 1 - 320 | IPR011251 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.99.46 | Miscellaneous |
| 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 |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| monooxygenase activity | Catalysis of the incorporation of one atom from molecular oxygen into a compound and the reduction of the other atom of oxygen to water. |
| oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from each of two donors, and molecular oxygen is reduced or incorporated into a donor. |
| uracil oxygenase activity | Catalysis of the reaction: uracil + NADH + O2 + H+ = ureidoacrylate peracid + NAD+. Ureidoacrylate peracid is spontaneously reduced by NADH to form ureidoacrylate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| nitrogen utilization | A series of processes that forms an integrated mechanism by which a cell or an organism detects the depletion of primary nitrogen source, usually ammonia, and then activates genes to scavenge the last traces of the primary nitrogen source and to transport and metabolize alternative nitrogen sources. The utilization process begins when the cell or organism detects nitrogen levels, includes the activation of genes whose products detect, transport or metabolize nitrogen-containing substances, and ends when nitrogen is incorporated into the cell or organism's metabolism. |
| uracil catabolic process | The chemical reactions and pathways resulting in the breakdown of uracil, 2,4-dioxopyrimidine, one of the pyrimidine bases occurring in RNA, but not in DNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKIGVFVPIG | NNGWLISTHA | PQYMPTFELN | KAIVQKAEHY | HFDFALSMIK | LRGFGGKTEF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WDHNLESFTL | MAGLAAVTSR | IQIYATAATL | TLPPAIVARM | AATIDSISGG | RFGVNLVTGW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QKPEYEQMGI | WPGDDYFSRR | YDYLTEYVQV | LRDLWGTGKS | DFKGDFFTMN | DCRVSPQPSV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PMKVICAGQS | DAGMAFSAQY | ADFNFCFGKG | VNTPTAFAPT | AARMKQAAEQ | TGRDVGSYVL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FMVIADETDD | AARAKWEHYK | AGADEEALSW | LTEQSQKDTR | SGTDTNVRQM | ADPTSAVNIN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MGTLVGSYAS | VARMLDEVAS | VPGAEGVLLT | FDDFLSGIET | FGERIQPLMQ | CRAHLPVLTQ |
| EVA |