B2J9G3
Gene name |
guaA |
Protein name |
GMP synthase [glutamine-hydrolyzing] |
Names |
GMP synthetase, Glutamine amidotransferase |
Species |
Nostoc punctiforme (strain ATCC 29133 / PCC 73102) |
KEGG Pathway |
npu:Npun_R0710 |
EC number |
6.3.5.2: 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 B2J9G3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B2J9G3-F1 | Predicted | AlphaFoldDB |
No variants for B2J9G3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B2J9G3 | |||||
No associated diseases with B2J9G3
5 regional properties for B2J9G3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GMP synthase, C-terminal | 222 - 540 | IPR001674 |
| domain | GMP synthase, glutamine amidotransferase | 27 - 214 | IPR004739 |
| domain | Glutamine amidotransferase | 29 - 209 | IPR017926 |
| domain | NAD/GMP synthase | 225 - 299 | IPR022310 |
| domain | GMP synthetase ATP pyrophosphatase domain | 217 - 415 | IPR025777 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.5.2 | 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 |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| GMP synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: ATP + XMP + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate + 2H(+). |
| pyrophosphatase activity | Catalysis of the hydrolysis of a pyrophosphate bond (diphosphate bond) between two phosphate groups. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glutamine metabolic process | The chemical reactions and pathways involving glutamine, 2-amino-4-carbamoylbutanoic acid. |
| tRNA modification | The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNTVVTLPTE | QAPQTLENVG | RFDRPLIIIL | DFGSQYSELI | ARRIRETQVY | SEVLSYRTTS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EQLRQLNPKG | IILSGGPSSV | YGDNAPHCDP | EIWNLGIPVL | GVCYGMQLMV | NQLGGEVAKA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DRGEYGKASL | YIDDPTDLLT | NVEDGTTMWM | SHGDSVTQMP | SGFELLAHTE | NTPCAAIADH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ERKLYGVQFH | PEVVHSIGGI | ALIRNFVYHI | CDCEPTWTTA | AFVEEAIREI | RTRVGEKRVL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LALSGGVDSS | TLAFLLYKAI | GEQLTCVFID | QGFMRKYEPE | RLVKLFQEQF | HIPVEYVNAR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DRFLAKVAGV | TDPEEKRRRI | GHEFINVFEE | TSKRLGHFDY | LAQGTLYPDV | IESADTNADP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QTGERVAVKI | KSHHNVGGLP | KDLRFKLVEP | LRKLFKDEVR | KVGRSIGLPE | EIVQRQPFPG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PGLAIRILGE | VTSERLNILR | DADLIVRQEI | NQRGMYHDFW | QAFAVLLPIR | SVGVMGDQRT |
| 490 | 500 | 510 | 520 | 530 | |
| YAYPIVLRIV | TSEDGMTADW | ARVPYDVLEV | ISTRIVNEVK | GVNRVVYDIT | SKPPGTIEWE |