Q9PMG8
Gene name |
carA |
Protein name |
Carbamoyl-phosphate synthase small chain |
Names |
Carbamoyl-phosphate synthetase glutamine chain |
Species |
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) |
KEGG Pathway |
cje:Cj1494c |
EC number |
6.3.5.5: 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 Q9PMG8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9PMG8-F1 | Predicted | AlphaFoldDB |
No variants for Q9PMG8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9PMG8 | |||||
No associated diseases with Q9PMG8
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.5 | 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. |
| carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: 2 ATP + L-glutamine + CO2 + H2O = 2 ADP + phosphate + glutamate + carbamoyl phosphate. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' pyrimidine nucleobase biosynthetic process | The chemical reactions and pathways resulting in the formation of pyrimidine nucleobases, 1,3-diazine, organic nitrogenous bases, beginning with the synthesis of a pyrimidine ring from simpler precursors. |
| 'de novo' UMP biosynthetic process | The chemical reactions and pathways resulting in the formation of UMP, uridine monophosphate, starting with the synthesis of (S)-dihydroorotate from bicarbonate; UMP biosynthesis may either occur via reduction by quinone, NAD(+) or oxygen. |
| arginine biosynthetic process | The chemical reactions and pathways resulting in the formation of arginine, 2-amino-5-(carbamimidamido)pentanoic acid. |
| 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 |
| MKAYIYLEND | IFLSAKAFGK | SGTFFGELVF | NTSLTGYQEI | ISDPSYAGQF | IVFSMPEIGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VGTNENDNES | KEIFASGVLM | RELSSSFSNF | RAKESLQDYL | EKHGKIGIYE | LDTRYLVKMI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RNNGNLRAVI | STEISNKEDL | KIALEKSAKI | DEVNFVKEVS | TKKNYSHKQG | VWNASFQKFN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DAKRSEKKVA | VIDYGVKTNI | LNELVEVGFE | VEVYPYNVKA | DELITLYKKG | EIQGVFLSNG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PGEPRILKQE | IAEIKKLAEA | KIPMLGICLG | HQLLSNAFGY | ETYKMKFGQH | GANHPVINLD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TKTVEITAQN | HNYNVPEELA | QVAHITHRNL | FGDNVEGVRY | KDYPIISVQH | HPESSSGPHE |
| 370 | |||||
| SKYIFKEFMN | LM |