P43902
Gene name |
tyrA (HI_1290) |
Protein name |
T-protein |
Names |
|
Species |
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
KEGG Pathway |
hin:HI_1290 |
EC number |
1.3.1.12: 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
2 structures for P43902
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 2PV7 | X-ray | 200 A | A/B | 81-377 | PDB |
| AF-P43902-F1 | Predicted | AlphaFoldDB |
No variants for P43902
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P43902 | |||||
No associated diseases with P43902
5 regional properties for P43902
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Chorismate mutase II, prokaryotic-type | 1 - 92 | IPR002701 |
| domain | Prephenate dehydrogenase | 101 - 364 | IPR003099 |
| domain | Chorismate mutase, T-protein | 7 - 89 | IPR011277 |
| domain | Prephenate dehydrogenase, dimerization domain | 245 - 346 | IPR046825 |
| domain | Prephenate dehydrogenase, nucleotide-binding domain | 141 - 206 | IPR046826 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.1.12 | 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| chorismate mutase activity | Catalysis of the reaction: chorismate = prephenate. |
| NAD+ binding | Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. |
| prephenate dehydrogenase (NAD+) activity | Catalysis of the reaction: NAD(+) + prephenate = (4-hydroxyphenyl)pyruvate + CO(2) + NADH. |
| prephenate dehydrogenase (NADP+) activity | Catalysis of the reaction: NADP(+) + prephenate = (4-hydroxyphenyl)pyruvate + CO(2) + NADPH. |
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. |
| tyrosine biosynthetic process | The chemical reactions and pathways resulting in the formation of tyrosine, an aromatic amino acid, 2-amino-3-(4-hydroxyphenyl)propanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSFMEALKDL | RSEIDSLDRE | LIQLFAKRLE | LVSQVGKVKH | QHGLPIYAPE | REIAMLQARR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LEAEKAGISA | DLIEDVLRRF | MRESYANENQ | FGFKTINSDI | HKIVIVGGYG | KLGGLFARYL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RASGYPISIL | DREDWAVAES | ILANADVVIV | SVPINLTLET | IERLKPYLTE | NMLLADLTSV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KREPLAKMLE | VHTGAVLGLH | PMFGADIASM | AKQVVVRCDG | RFPERYEWLL | EQIQIWGAKI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YQTNATEHDH | NMTYIQALRH | FSTFANGLHL | SKQPINLANL | LALSSPIYRL | ELAMIGRLFA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QDAELYADII | MDKSENLAVI | ETLKQTYDEA | LTFFENNDRQ | GFIDAFHKVR | DWFGDYSEQF |
| 370 | |||||
| LKESRQLLQQ | ANDLKQG |