C1DSU8
Gene name |
glnD |
Protein name |
Bifunctional uridylyltransferase/uridylyl-removing enzyme |
Names |
UTase/UR, Bifunctional [protein-PII] modification enzyme, Bifunctional nitrogen sensor protein |
Species |
Azotobacter vinelandii (strain DJ / ATCC BAA-1303) |
KEGG Pathway |
avn:Avin_39010 |
EC number |
2.7.7.59: Nucleotidyltransferases |
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 C1DSU8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C1DSU8-F1 | Predicted | AlphaFoldDB |
No variants for C1DSU8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C1DSU8 | |||||
No associated diseases with C1DSU8
6 regional properties for C1DSU8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ACT domain | 692 - 774 | IPR002912-1 |
| domain | ACT domain | 798 - 869 | IPR002912-2 |
| domain | Polymerase, nucleotidyl transferase domain | 73 - 120 | IPR002934 |
| domain | HD/PDEase domain | 446 - 600 | IPR003607 |
| domain | HD domain | 450 - 572 | IPR006674 |
| domain | PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase | 178 - 316 | IPR013546 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.59 | Nucleotidyltransferases |
| 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 |
|---|---|
| [protein-PII] uridylyltransferase activity | Catalysis of the reaction: UTP + (protein-PII) = diphosphate + uridylyl-(protein-PII). |
| phosphoric diester hydrolase activity | Catalysis of the hydrolysis of a phosphodiester to give a phosphomonoester and a free hydroxyl group. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| nitrogen fixation | The process in which nitrogen is taken from its relatively inert molecular form (N2) in the atmosphere and converted into nitrogen compounds useful for other chemical processes, such as ammonia, nitrate and nitrogen dioxide. |
| regulation of nitrogen utilization | Any process that modulates the frequency, rate or extent of nitrogen utilization. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPQVDPDLFD | PGQFQAELAL | KSSPIPAYKK | ALRCAREVLD | ARFQEGRDIR | RLIEDRAWFV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DQILALAWNR | FDWSEDADIA | LIAVGGYGRG | ELHPYSDIDL | LILMDGADHE | VFREPIEGFL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TLLWDIGLEV | GQSVRSLAEC | AEEAQADLTV | ITNLMESRTI | AGPEHLRQRM | QEVTSAQRMW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PSRAFFLAKR | DEQKTRHARY | NDTEYNLEPN | VKGSPGGLRD | IQTLLWIARR | QFGTINLHAM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VGQGFLLESE | YTLLASSQEF | LWKVRYALHM | LAGRAEDRLL | FDLQRQIAGL | LGYEDSDAKL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AVERFMQKYY | RVVLGIAELT | ELVFQHFEEV | ILPGDAAGRV | EPLNERFQVR | DGYLEVTHAG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VFQETPSALL | EIFVLLARRP | EIRGVRADTI | RLLRDHRYLI | DDAFRRDPHN | TGLFIELFKS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RQGIHRNLRR | MNRYGILGRY | LPEFGHIVGQ | MQHDLFHIYT | VDAHTLNLIK | NLRKLFWPEL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AEKYPLASKL | IEKLPKPELI | YLAGLYHDIG | KGRGGDHSEL | GAADALAFCQ | RHDLPAMDTQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LIVWLVRNHL | LMSTTAQRKD | LSDPQVIFDF | AQKVRDQTYL | DYLYVLTVAD | INATNPTLWN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| SWRASLLRQL | YTETKHALRR | GLEQPVGREE | QIRQTQKAAL | DILVRSGTDP | DDAEHLWTQL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| GDDYFLRHTS | SDIAWHTEAI | LQHPSSGGPL | VLIKETTQRE | FEGATQIFIY | APDQHDFFAV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| TVAAMDQLNL | SIHDARVITS | TSQFTLDTYI | VLDADGGSIG | NNPARIQEIR | QGLVEALRNP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ADYPTIIQRR | VPRQLKHFAF | APQVTIQNDA | LRPVTILEII | APDRPGLLAR | IGKIFLDFDL |
| 850 | 860 | 870 | 880 | 890 | |
| SLQNAKIATL | GERVEDVFFV | TDAHNQPLSD | PELCARLQLA | IAEQLADGDS | YIQPSRISI |