Q9PLR2
Gene name |
hemA |
Protein name |
Glutamyl-tRNA reductase |
Names |
GluTR |
Species |
Chlamydia muridarum (strain MoPn / Nigg) |
KEGG Pathway |
cmu:TC_0033 |
EC number |
1.2.1.70: 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 Q9PLR2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9PLR2-F1 | Predicted | AlphaFoldDB |
No variants for Q9PLR2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9PLR2 | |||||
No associated diseases with Q9PLR2
4 regional properties for Q9PLR2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | 171 - 307 | IPR006151 |
| domain | Glutamyl-tRNA reductase, N-terminal | 6 - 156 | IPR015895 |
| domain | Tetrapyrrole biosynthesis, glutamyl-tRNA reductase, dimerisation domain | 321 - 418 | IPR015896 |
| conserved_site | Glutamyl-tRNA reductase, conserved site | 99 - 122 | IPR018214 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.70 | With NAD(+) or NADP(+) as acceptor |
| 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 |
|---|---|
| glutamyl-tRNA reductase activity | Catalysis of the reaction: (S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = L-glutamyl-tRNA(Glu) + 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 |
|---|---|
| protoporphyrinogen IX biosynthetic process | The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MVREGEEHID | EEFSLGVIGV | SYRETALQQR | EQVLQFLQQA | QLSFYPKFPQ | EEGRSVLLST |
| 70 | 80 | 90 | 100 | 110 | 120 |
| CHRVELYGMA | TEAIFSTLEK | EIREMGAIPY | FYRNQDCFSH | LFCVVGGMDS | LVLGETEIQG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QVKRAYLQAI | EEQKLAFALH | FLFQKALKEG | KVFRTKRSSP | STEITIPAFV | QHELQKQKMA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RSASLLFMGY | SEINRSVAYY | LQKQGFSRIT | FCSRQPLSLR | SMDQVLREEV | CFQDPYHVIF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LGSSELRHAF | PRSLWEGVWD | FPGRLVFDFA | VPRALPVQPA | CRDRYIDMEQ | ISDWLRQHQK |
| 310 | 320 | 330 | |||
| EVFPLQLDSL | REVGYRYWES | LNRRLARRRY | ASV |