A1WZS9
Gene name |
glmU |
Protein name |
Bifunctional protein GlmU |
Names |
|
Species |
Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira halophila (strain DSM 244 / SL1)) |
KEGG Pathway |
hha:Hhal_2428 |
EC number |
2.3.1.157: Transferring groups other than amino-acyl groups |
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 A1WZS9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1WZS9-F1 | Predicted | AlphaFoldDB |
No variants for A1WZS9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1WZS9 | |||||
No associated diseases with A1WZS9
6 regional properties for A1WZS9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ACT domain | 679 - 760 | IPR002912-1 |
| domain | ACT domain | 788 - 861 | IPR002912-2 |
| domain | HD/PDEase domain | 436 - 590 | IPR003607 |
| domain | Protein-PII uridylyltransferase, N-terminal | 23 - 100 | IPR005105 |
| domain | HD domain | 440 - 569 | IPR006674 |
| domain | PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase | 166 - 304 | IPR013546 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.1.157 | Transferring groups other than amino-acyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| glucosamine-1-phosphate N-acetyltransferase activity | Catalysis of the reaction: alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+). |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| UDP-N-acetylglucosamine diphosphorylase activity | Catalysis of the reaction: N-acetyl-alpha-D-glucosamine 1-phosphate + UTP = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| cell morphogenesis | The developmental process in which the size or shape of a cell is generated and organized. |
| cell wall organization | A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. |
| lipid A biosynthetic process | The chemical reactions and pathways resulting in the formation of lipid A, the glycolipid group of bacterial lipopolysaccharides, consisting of four to six fatty acyl chains linked to two glucosamine residues. Further modifications of the backbone are common. |
| peptidoglycan biosynthetic process | The chemical reactions and pathways resulting in the formation of peptidoglycans, any of a class of glycoconjugates found in bacterial cell walls. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
| UDP-N-acetylglucosamine biosynthetic process | The chemical reactions and pathways resulting in the formation of UDP-N-acetylglucosamine, a substance composed of N-acetylglucosamine, a common structural unit of oligosaccharides, in glycosidic linkage with uridine diphosphate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRAPVAVVIL | AAGKGTRMRS | AQPKVLQPLA | GRPLLAHVLD | TALALGPEQV | HVVYGHGGDQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VAAAHADYPV | YWVEQPRQLG | TGHAVACALP | QIPDDHRVLV | LYGDVPLVTP | ETLKPLLAGD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GLELLAARVP | DPTGYGRIIR | DDDGAVVAIV | EEKDADPEQR | RVDEVNTGLL | AASAGDLRRW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| MAALSADNAQ | GEYYLTDAVA | AARADGTPVR | ARFTSEAGEA | SGINDLVQLA | EVEEAFQRRW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ARRLLQGGLR | LVAPHRFTLR | GAVRHGTDCA | VDADCTLEGE | VQLGHGVQVG | QGVILRDCVI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EDGAQVGPYT | VVEQAHIGAG | CRVGPFAHLR | PGTVLEEGAR | VGNFVETKAA | RLGPGAKANH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LTYVGDAEVG | ARANLGAGTI | TCNYDGAEKH | RTQIGEDAFI | GSGSQLVAPV | QVGARATIGA |
| 430 | 440 | 450 | 460 | 470 | |
| GTTLTSDAPA | DALTVGRSRA | RTIPGWQHPG | LTGRRGPPDD | NDATPASGGA | KEE |