Q44697
Gene name |
trpE |
Protein name |
Anthranilate synthase component 1 |
Names |
AS, ASI |
Species |
Buchnera aphidicola subsp Diuraphis noxia |
KEGG Pathway |
|
EC number |
4.1.3.27: Oxo-acid-lyases |
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 Q44697
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q44697-F1 | Predicted | AlphaFoldDB |
No variants for Q44697
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q44697 | |||||
No associated diseases with Q44697
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.3.27 | Oxo-acid-lyases |
| 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 |
|---|---|
| anthranilate synthase activity | Catalysis of the reaction: chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tryptophan biosynthetic process | The chemical reactions and pathways resulting in the formation of tryptophan, the chiral amino acid 2-amino-3-(1H-indol-3-yl)propanoic acid; tryptophan is synthesized from chorismate via anthranilate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEKKPYEIKI | IQKKAKYHPD | PTIVFNHICG | SQKQTLLLET | AEINKKNDLE | SIMIIDAALR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ISSERNHSVQ | LTALSKNGEN | ILSILKSNLK | QKVQMFIQDT | SIRLEFPHFQ | KNLDEDKKIF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLSIFDTFRF | IMKFFKNRNK | VQKAMFFGGL | FSYDLISNFE | LLPKLKKTQK | CPHFCFYLAE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TLLIVDHQKK | TCLIQNSLFT | KNSHEQMRVE | KRGREIQKKL | EASLNSIPVR | QEVKNSMLTA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NMSDEQYCSI | IKKLQILIRK | GEIFQVVPSR | KFFLPCSNPL | SAYQKLKKSN | PSPYMFFMQD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KDFTLFGASP | ESSLKYDDTT | RQVELYPIAG | TRPRGRNMDG | TLNLDLDSRI | ELEMRTNHKE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LAEHLMLVDL | ARNDLARICE | PGSRYVSDLV | RVDKYPHVMH | LVSRVVGTLK | PELDALHAYA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ACMNMGTLTG | APKIRAMELI | AEYEMEQRGS | YGGAIGYFTD | LGNLDTCITI | RSAYVEDNIA |
| 490 | 500 | 510 | |||
| TIQSGSGIVY | NSIPEDEVKE | GINKAKRVIN | AIQHAHHLV |