B5XML5
Gene name |
proA |
Protein name |
Gamma-glutamyl phosphate reductase |
Names |
GPR, Glutamate-5-semialdehyde dehydrogenase, Glutamyl-gamma-semialdehyde dehydrogenase, GSA dehydrogenase |
Species |
Streptococcus pyogenes serotype M49 (strain NZ131) |
KEGG Pathway |
soz:Spy49_1295c |
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 B5XML5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B5XML5-F1 | Predicted | AlphaFoldDB |
No variants for B5XML5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B5XML5 | |||||
No associated diseases with B5XML5
4 regional properties for B5XML5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | GPR domain | 3 - 415 | IPR000965 |
| domain | Aldehyde dehydrogenase domain | 36 - 283 | IPR015590-1 |
| domain | Aldehyde dehydrogenase domain | 301 - 378 | IPR015590-2 |
| conserved_site | Gamma-glutamyl phosphate reductase GPR, conserved site | 322 - 344 | 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 |
| MTDMRRLGQR | AKQASLLIAP | LSTQIKNRFL | STLAKALVDD | TQTLLAANQK | DLANAKEHGI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SDIMMDRLRL | TSERIKAMAQ | GVQQVADLAD | PIGQVIKGYT | NLDGLKILQK | RVPLGVIAMI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FESRPNVSVD | AFSLAFKTNN | AIILRGGKDA | LHSNKALVKL | IRQSLEKSGI | TPDAVQLVED |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PSHAVAEELM | QATDYVDVLI | PRGGAKLIQT | VKEKAKVPVI | ETGVGNVHIY | VDAQADLDMA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TKIVINAKTK | RPSVCNAAEG | LVIHEAVAAR | FIPMLEKAIN | QVQPVEWRAD | DKALPLFEQA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VPAKAEDFET | EFLDYIMSVK | VVSSLEEAIF | WINQHTSHHS | EAIITRDIKV | AETFQDLVDA |
| 370 | 380 | 390 | 400 | 410 | |
| AAVYVNASTR | FTDGFVFGLG | AEIGISTQKM | HARGPMGLEA | LTSTKFYING | DGHIRE |