A1AUE9
Gene name |
hemA |
Protein name |
Glutamyl-tRNA reductase |
Names |
GluTR |
Species |
Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1) |
KEGG Pathway |
ppd:Ppro_3377 |
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 A1AUE9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1AUE9-F1 | Predicted | AlphaFoldDB |
No variants for A1AUE9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1AUE9 | |||||
No associated diseases with A1AUE9
4 regional properties for A1AUE9
| 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 |
| MNIIVVGLSH | KTAPVEVRER | VAFSPNLIER | PLRELVSLDD | ISEGVIVSTC | NRVEIYATTH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DIAGGTARIK | RFLADHHRIP | LESLEQYLYS | YHSEAAIRHV | FRVASSLDSM | VVGEPQILGQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IKTAYGYAAE | YRTSGTILNR | FLHKAFSVAK | RVRTETRIAS | SAVSVAFAAV | ELARKILGDL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SGKTVMLIGA | GEMCELAAKH | FLTSGARGLL | VANRTFAKGE | RLAAEFGGEA | IPFEELFQEL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HRADIVLSST | GAPHTIIAPR | DVEAVVKRRK | FKPMFFIDIA | VPRDIDPRVN | DLESAYLFTV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DDLQEIVEAN | MAQRNQEASK | GEEIVEQEIG | QFHCWLSSLE | STPTIVALRA | RFEEIRRAEL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EKTLCGWKDL | SPEAEKRLEI | MTLSIMNKLL | HTPTAVLKRA | GQGGRTDLYT | DALRQLFDLQ |
| 430 | |||||
| TSRQDDDELE | LELEEE |