C1CXR4
Gene name |
carB |
Protein name |
Carbamoyl-phosphate synthase large chain |
Names |
Carbamoyl-phosphate synthetase ammonia chain |
Species |
Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115) |
KEGG Pathway |
ddr:Deide_00700 |
EC number |
6.3.4.16: Other carbon--nitrogen ligases |
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 C1CXR4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C1CXR4-F1 | Predicted | AlphaFoldDB |
No variants for C1CXR4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C1CXR4 | |||||
No associated diseases with C1CXR4
13 regional properties for C1CXR4
| 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 | 666 - 869 | IPR005479-2 |
| domain | Carbamoyl-phosphate synthetase, large subunit oligomerisation domain | 417 - 540 | 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 | 379 - 397 | IPR005483-7 |
| domain | Methylglyoxal synthase-like domain | 930 - 1028 | IPR011607 |
| domain | ATP-grasp fold | 133 - 328 | IPR011761-1 |
| domain | ATP-grasp fold | 671 - 863 | IPR011761-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.4.16 | Other carbon--nitrogen ligases |
| 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 |
|---|---|
| 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. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| '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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPKRTDLQTI | LILGSGPIQI | GQAAEFDYSG | TQALKALRGE | GYRVVLVNSN | PATIMTDPDL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ADATYLEPLT | PEFVEKIIAL | EKPDAILPTL | GGQTALNLAM | ELHERGTLEK | YGVELIGAGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EAIKKGEDRE | LFQAAMKKIG | VETARGKMVH | SMEEAVEYQK | EIGLPIVIRP | SFTLGGTGGG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IAHTYEEFLA | ITEGGLRDSP | VTSVLLEESI | LGWKEYELEV | MRDTADTVII | ITSIENFDPM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GVHTGDSITV | APAQTLSDVE | YQRLRNQSLA | IIREIGVATG | GSNIQFAVNP | DNGRVIVIEM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NPRVSRSSAL | ASKATGFPIA | KIAALLAVGY | HLDELPNDIT | RVTPASFEPS | IDYVVTKIPR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FAFEKFPGTS | DHLGTQMRSV | GEVMAIGRTF | KESLQKALRS | TESDIRGVYA | EMDEAGLRAL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LYPNPRRIEA | VIELLRRGES | IDALFDATKI | DRWFLEQIKE | IIDAEHELLE | LGPISEWKYE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YWREVKRLGF | SDARIGEIVG | LSELQVRQLR | KAARATPVYK | TVDTCAAEFE | AYTPYHYSTY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EWEDEVTGTD | KPKVVILGSG | PNRIGQGVEF | DYATVHAVWA | LQEAGYETIM | VNSNPETVST |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DYDTADRLYF | EPLTFEDVMN | IVDHEKPVGV | IVQLGGQTPL | KLAKKLADAG | APIIGTSPET |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IHEAEDRASF | NALCERLGLS | QPRGKVAETP | EQARQLAAEL | GFPLMARPSY | VLGGRAMRTV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| RSMEELVTYL | DEVYAAVEGQ | PSILLDQFLE | GALELDVDTL | CDGERAVVAG | IMEHVEAAGV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| HSGDSACVLP | PVNLSAELLA | RVKADTERLA | LELGVRGLMN | VQWAVKDGTA | YILEANPRAS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RTVPFVSKAV | NHPLAKSAAR | IAVGHTLEQI | GLTETPEAAM | YSVKEVHLPF | LKFKGVSPIL |
| 910 | 920 | 930 | 940 | 950 | 960 |
| GPEMKSTGES | MGIDADPYLA | FYRAQLGAKS | YLPLSGTALL | LGDGLDEVAS | TLQGAGLNVI |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| REQDGNTLPD | LLIDVTGSPL | LRTALERGVP | IVSTREAAVW | TSKAIAAAQG | SELRVRSLQD |
| WQTQEAVAG |