O85347
Gene name |
pyrG |
Protein name |
CTP synthase |
Names |
Cytidine 5'-triphosphate synthase, Cytidine triphosphate synthetase, CTP synthetase, CTPS, UTP--ammonia ligase |
Species |
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298) |
KEGG Pathway |
neu:NE1045 |
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 O85347
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O85347-F1 | Predicted | AlphaFoldDB |
No variants for O85347
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O85347 | |||||
No associated diseases with O85347
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 |
| MTKFVFVTGG | VVSSLGKGIA | AASLAALLET | RGIRVTILKL | DPYINVDPGT | MNPFQHGEVF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VTDDGAETDL | DLGHYERFIS | TKMTRQNNFT | TGQIYESVIR | KERRGDYLGG | TVQVIPHITD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EIKLFIRNGV | SDAQVAIVEI | GGTVGDIESL | PFLEAIRQMS | VQLPHHDTCF | IHLTLLPYIS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SAGELKTKPT | QHSVKELREI | GIQPDVLLCR | SDRPLPLEER | RKIALFTNVR | EESVISAIDV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DNIYKIPALL | HEQMLDEIVC | HRLDILARPA | NLTVWKKLVH | ALEHPEHEVS | IALVGKYVDL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TESYKSLSEA | LIHAGIHTRC | KINIHYIDSE | NIEQHGTGCL | TNMDAILVPG | GFGKRGVEGK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IMAISYARNH | RIPYLGICLG | MQLAVIEFSR | NRLQLENAHS | TEFDPDTPYP | VLGLITEWRD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RCGRVEKRSA | QTDLGGTMRL | GGQECLLKPH | TLAHKIYGAD | KVIERHRHRY | EVNAEFIPQL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EQAGMHISGL | SAEGDLCEMI | ELPQSEHPWF | VACQFHPEFT | STPRNGHPLF | KSYIQAAISF |
| 550 | 560 | ||||
| AGQSDRTKLH | SRNVQESVTT | DSSN |