A9ITA7
Gene name |
folE2 |
Protein name |
GTP cyclohydrolase FolE2 |
Names |
|
Species |
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) |
KEGG Pathway |
bpt:Bpet3059 |
EC number |
3.5.4.16: In cyclic amidines |
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 A9ITA7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A9ITA7-F1 | Predicted | AlphaFoldDB |
No variants for A9ITA7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A9ITA7 | |||||
No associated diseases with A9ITA7
No regional properties for A9ITA7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A9ITA7 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 3.5.4.16 | In cyclic amidines |
| 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 |
|---|---|
| GTP cyclohydrolase I activity | Catalysis of the reaction: GTP + H2O = formate + 7,8-dihydroneopterin 3'-triphosphate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 7,8-dihydroneopterin 3'-triphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of 7,8-dihydroneopterin 3'-triphosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNSPIDPALV | MPDVQSSADT | RHIPIQRVGI | RGVRHPMLVA | GADGAPQPTV | ANWTLTVALP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AEEKGTHMSR | FVALLEKYRS | VPMTPALFAA | MARDMLPLLH | AERGDITAAF | PYFINKSAPV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SGVQSLLDYE | VQWIARAAGD | QVEFELVVQV | PVTSLCPCSK | AISEYGAHNQ | RSHVTVSVVL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NGDLAMDRII | RLVEDEGSCE | LWGLLKRPDE | KFVTERAYDN | PKFVEDLVRD | VAARLAAHPG |
| 250 | 260 | ||||
| VARYRVEAEN | FESIHNHSAY | AVVEG |