A6SUQ1
Gene name |
purH |
Protein name |
Bifunctional purine biosynthesis protein PurH |
Names |
|
Species |
Janthinobacterium sp (strain Marseille) (Minibacterium massiliensis) |
KEGG Pathway |
mms:mma_0308 |
EC number |
2.1.2.3: Hydroxymethyl-, formyl- and related transferases |
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 A6SUQ1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A6SUQ1-F1 | Predicted | AlphaFoldDB |
No variants for A6SUQ1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A6SUQ1 | |||||
No associated diseases with A6SUQ1
1 regional properties for A6SUQ1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Methylglyoxal synthase-like domain | 1 - 145 | IPR011607 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.2.3 | Hydroxymethyl-, formyl- and related transferases |
| 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 |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| IMP cyclohydrolase activity | Catalysis of the reaction: IMP + H2O = 5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide. |
| phosphoribosylaminoimidazolecarboxamide formyltransferase activity | Catalysis of the reaction: 10-formyltetrahydrofolate + 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide = tetrahydrofolate + 5'-phosphoribosyl-5-formamido-4-imidazolecarboxamide. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' IMP biosynthetic process | The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIKQALISVS | DKTGVLEFAR | ALSGMGVNIL | STGGTAKLLA | ENGISVTEVA | DYTGFPEMLD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GRVKTLHPKV | HGGILARRDF | AEHVSALEKH | NIPTIDMVVV | NLYPFQQTVA | REHCSLEDAI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ENIDIGGPAM | LRSSAKNHKD | VIVICDPTDY | SQVLGELSAN | QGEVSYETKF | TLAKKVFAHT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AQYDGAITNY | FTSLGADKQH | ATRSSYPATL | NLHFEKVQEM | RYGENPHQSA | AFYRESNPQV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GALANYTQLQ | GKELSYNNIA | DADAAWECVK | TFDESACVII | KHANPCGVAV | GASPLEAYSK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ALQTDPTSAF | GGIIAFNREL | DGNAAEAVAK | QFVEVLIAPS | FSEKAKQIFA | GKQNVRLLEI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PLGNAVNAHD | FKRVGGGLLV | QSPDAKNVVL | AELKVVSKKQ | PTPQQLQDLM | FAWRVAKFVK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SNAIVFCANG | MTMGVGAGQM | SRIDSARIAS | IKAQNAGLSL | VGTAVASDAF | FPFRDGLDVV |
| 490 | 500 | 510 | 520 | ||
| VAAGATSVIH | PGGSMRDQEV | IDAADEQGVV | MLMTGTRHFR | H |