A2RJM8
Gene name |
proA |
Protein name |
Gamma-glutamyl phosphate reductase |
Names |
GPR, Glutamate-5-semialdehyde dehydrogenase, Glutamyl-gamma-semialdehyde dehydrogenase, GSA dehydrogenase |
Species |
Lactococcus lactis subsp cremoris (strain MG1363) |
KEGG Pathway |
llm:llmg_0886 |
EC number |
1.2.1.41: With NAD(+) or NADP(+) as acceptor |
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 A2RJM8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2RJM8-F1 | Predicted | AlphaFoldDB |
No variants for A2RJM8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A2RJM8 | |||||
No associated diseases with A2RJM8
4 regional properties for A2RJM8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GPR domain | 1 - 413 | IPR000965 |
| domain | Aldehyde dehydrogenase domain | 10 - 280 | IPR015590-1 |
| domain | Aldehyde dehydrogenase domain | 314 - 376 | IPR015590-2 |
| conserved_site | Gamma-glutamyl phosphate reductase GPR, conserved site | 320 - 341 | IPR020593 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.41 | With NAD(+) or NADP(+) as acceptor |
| 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| glutamate-5-semialdehyde dehydrogenase activity | Catalysis of the reaction: L-glutamate 5-semialdehyde + NADP(+) + phosphate = L-glutamyl 5-phosphate + H(+) + NADPH. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| L-proline biosynthetic process | The chemical reactions and pathways resulting in the formation of L-proline, an L-enantiomer of a chiral, cyclic, nonessential alpha-amino acid found in peptide linkage in proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MIEELGLKVK | TASKEAAKLS | TAEKNTFLQK | LADSLVENTD | RIISENAKDL | AKAKGHGISE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IMVDRLRLTA | QRISDMATGL | RQVAELPDPI | GQVLQGFTNL | DGLKIVQKRV | PLGTVGMIFE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SRPNVTIDAF | SLCFKTGNSV | LLRGGSDAIY | SNMVLVEIIK | ENLLSAKITD | GVVELLSDTS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HAEAEKMMQA | DKFLDVLIPR | GSARLINRVK | EKATVPVIET | GVGNCTIFVD | ESADLDMATR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IVINAKTQRP | SVCNAAESLV | VHAKIADEFL | PKLQNEINKV | HEVEFRADER | SLKALSAGIP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ATDEDFGMEF | LDYILSVKTV | DNLDEAIEHI | NTYSSRHSES | IVTHDYFNAQ | KFQDEIDAAA |
| 370 | 380 | 390 | 400 | 410 | |
| VYVNASTRFT | DGFVFGLGAE | IGISTQKLHA | RGPMGLEALT | STKYLIDGCG | QIR |