A4G3R1
Gene name |
cbiA |
Protein name |
Cobyrinate a,c-diamide synthase |
Names |
Cobyrinic acid a,c-diamide synthetase |
Species |
Herminiimonas arsenicoxydans |
KEGG Pathway |
har:HEAR0965 |
EC number |
6.3.5.11: Carbon--nitrogen ligases with glutamine as amido-N-donor |
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 A4G3R1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A4G3R1-F1 | Predicted | AlphaFoldDB |
No variants for A4G3R1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A4G3R1 | |||||
No associated diseases with A4G3R1
14 regional properties for A4G3R1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain | 128 - 334 | IPR005479-1 |
| domain | Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain | 686 - 892 | IPR005479-2 |
| domain | Carbamoyl-phosphate synthetase, large subunit oligomerisation domain | 427 - 549 | IPR005480 |
| domain | Carbamoyl-phosphate synthase large subunit, CPSase domain | 19 - 33 | IPR005483-1 |
| domain | Carbamoyl-phosphate synthase large subunit, CPSase domain | 48 - 58 | IPR005483-2 |
| domain | Carbamoyl-phosphate synthase large subunit, CPSase domain | 168 - 180 | IPR005483-3 |
| domain | Carbamoyl-phosphate synthase large subunit, CPSase domain | 204 - 223 | IPR005483-4 |
| domain | Carbamoyl-phosphate synthase large subunit, CPSase domain | 239 - 256 | IPR005483-5 |
| domain | Carbamoyl-phosphate synthase large subunit, CPSase domain | 297 - 326 | IPR005483-6 |
| domain | Carbamoyl-phosphate synthase large subunit, CPSase domain | 380 - 398 | IPR005483-7 |
| domain | Methylglyoxal synthase-like domain | 963 - 1099 | IPR011607 |
| domain | ATP-grasp fold | 133 - 328 | IPR011761-1 |
| domain | ATP-grasp fold | 691 - 887 | IPR011761-2 |
| domain | Carbamoyl-phosphate synthase large chain, methylglyoxal synthase-like domain | 969 - 1069 | IPR033937 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.11 | Carbon--nitrogen ligases with glutamine as amido-N-donor |
| 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 |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| cobyrinic acid a,c-diamide synthase activity | Catalysis of the conversion of cobyrinic acid to cobyrinic acid a,c-diamide via the intermediate formation of cobyrinic acid c-monoamide. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| cobalamin biosynthetic process | The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. |
| glutamine metabolic process | The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVMSSPTNSA | RIILISGIAS | GQGKTTVTAA | LARKLIRQGL | RVRVFKTGPD | YLDPMILQRA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SGAEVYALDL | WMVGLDDCRR | LLARAASEVD | VILIEGVMGL | YDGDPSSADL | ARAFGVPVVV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VLDAAKMAQT | VGAVVLGLQQ | YGPVDLAGVI | VNRLASPSHA | SMVTRGIRNV | PILATLPKQQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QALPERHLGL | VQPDEIAQVD | QVLDQLADQI | EIDMVAWDAI | APVVLDGSLA | AASTQQLLAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KTIAIARDAA | FAFVYHANLE | CLRAAGAQLK | FFSPLNDETI | PAEADAVYIP | GGYPELHCAT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSSAQRWQDS | MRAAHVRNMP | ILAECGGMMV | IADSLIDAQG | KKWPMVGLIP | GEVAMQGKLA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLGMQSLATE | DGELRGHAFH | YSTLSTPVEP | QAQTVKRSNG | AHGEAVYKQG | ALTATYFHAY |
| 430 | |||||
| FSSCPAATAR | IFSPEIKA |