Q9ZHY3
Gene name |
pheA (NGO1510) |
Protein name |
Bifunctional chorismate mutase/prephenate dehydratase |
Names |
Chorismate mutase-prephenate dehydratase, P-protein |
Species |
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) |
KEGG Pathway |
ngo:NGO_1510 |
EC number |
4.2.1.51: Hydro-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 Q9ZHY3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9ZHY3-F1 | Predicted | AlphaFoldDB |
No variants for Q9ZHY3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9ZHY3 | |||||
No associated diseases with Q9ZHY3
6 regional properties for Q9ZHY3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Prephenate dehydratase | 91 - 271 | IPR001086 |
| domain | Chorismate mutase II, prokaryotic-type | 3 - 91 | IPR002701 |
| domain | ACT domain | 281 - 356 | IPR002912 |
| domain | Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain | 9 - 80 | IPR010957 |
| conserved_site | Prephenate dehydratase, conserved site | 245 - 267 | IPR018528-1 |
| conserved_site | Prephenate dehydratase, conserved site | 307 - 314 | IPR018528-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.51 | Hydro-lyases |
| 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 |
|---|---|
| chorismate mutase activity | Catalysis of the reaction: chorismate = prephenate. |
| prephenate dehydratase activity | Catalysis of the reaction: prephenate = phenylpyruvate + H2O + CO2. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| chorismate metabolic process | The chemical reactions and pathways involving chorismate, the anion of (3R-trans)-3-((1-carboxyethenyl)oxy)-4-hydroxy-1,5-cyclohexadiene-1-carboxylic acid. |
| L-phenylalanine biosynthetic process | The chemical reactions and pathways resulting in the formation of L-phenylalanine, the L-enantiomer of 2-amino-3-phenylpropanoic acid, i.e. (2S)-2-amino-3-phenylpropanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSQTIDELLI | PHRNAIDTID | AEILRLLNER | AQHAHAIGEL | KGTGAVYRPE | REVAVLRRIQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLNKGPLPDE | SVARLFREVM | SECLAVERPL | TIAYLGPQGT | FTQQAAIKHF | GHAAHTMACP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TIDDCFKQVE | TRQADYLVAP | VENSTEGSVG | RTLDLLAVTA | LQACGEVVLR | IHHNLLRKNN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GSTEGIAKVF | SHAQALAQCN | DWLGRRLPNA | ERIAVSSNAE | AARLVAESDD | GTVAAIAGRT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AAEIYGLDMV | AECIEDEPNN | TTRFLVMGHH | ETGASGSDKT | SLAVSAPNRA | GAVASLLQPL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TESGISMTKF | ESRPSKSVLW | EYLFFIDIEG | HRRDAQIQTA | LERLGERASF | VKAIGSYPTA |
| VL |