Q3AFT7
Gene name |
pyrG |
Protein name |
CTP synthase |
Names |
Cytidine 5'-triphosphate synthase, Cytidine triphosphate synthetase, CTP synthetase, CTPS, UTP--ammonia ligase |
Species |
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901) |
KEGG Pathway |
chy:CHY_0125 |
EC number |
6.3.4.2: 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 Q3AFT7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3AFT7-F1 | Predicted | AlphaFoldDB |
No variants for Q3AFT7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3AFT7 | |||||
No associated diseases with Q3AFT7
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.4.2 | 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| CTP synthase activity | Catalysis of the reaction: ATP + UTP + glutamine + H20= ADP + phosphate + CTP + glutamate. |
| glutaminase activity | Catalysis of the reaction: L-glutamine + H2O = L-glutamate + NH3. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' CTP biosynthetic process | The chemical reactions and pathways resulting in the formation of cytidine 5'-triphosphate (CTP) from simpler components. |
| 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 |
| MTKFIFVTGG | VVSSLGKGIT | AASLGRLLKS | RGLKVAIQKF | DPYINVDPGT | MSPYQHGEVF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VTDDGAETDL | DLGHYERFID | INLTKNSNVT | TGKVYWAVIS | KERRGDYLGG | TVQVIPHITN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EIKERILRVA | KESNPDVVIT | EIGGTVGDIE | SLPFLEAIRQ | LKNDVGKDNV | LYIHVTLVPT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LRVTGELKTK | PTQHSVKELR | SIGIQPDIIV | ARSEQPLSRE | ITEKIALFCD | IDKNAVIQAV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DASNIYEVPL | KLKEEGLDDI | VIKKLGLTCG | EPDLSEWEQI | VERYKNPKFE | VTIGIVGKYV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SLPDAYLSVA | EALRHAGIYH | ETRVNIRWID | SEMLEKEPVE | KYLSNLDGIL | VPGGFGDRGV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EGKIKAIQYA | RENKVPYLGL | CLGMQTAVIE | FARNVAGLKD | ANSSEFKPDG | PHSVIDLLPE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QKEVEQLGGT | MRLGLYPCKL | VPGTKAHAAY | GEEIIYERHR | HRYEFNNEYR | ELLTGLGLVI |
| 490 | 500 | 510 | 520 | 530 | |
| SGTSPDGRLV | EIIELSDHPW | FVATQFHPEF | KSRPNRPHPL | FREFIGASLK | TNKLF |