Q9JSX6
Gene name |
nadA |
Protein name |
Quinolinate synthase |
Names |
|
Species |
Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) |
KEGG Pathway |
nma:NMA2090 |
EC number |
2.5.1.72: Transferring alkyl or aryl groups, other than methyl groups |
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 Q9JSX6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9JSX6-F1 | Predicted | AlphaFoldDB |
No variants for Q9JSX6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9JSX6 | |||||
No associated diseases with Q9JSX6
No regional properties for Q9JSX6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9JSX6 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.5.1.72 | Transferring alkyl or aryl groups, other than methyl groups |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| metal ion binding | Binding to a metal ion. |
| quinolinate synthetase A activity | Catalysis of the reaction: iminoaspartate + dihydroxy-acetone-phosphate = quinolinate + 2 H2O + phosphate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| NAD biosynthetic process | The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide, a coenzyme present in most living cells and derived from the B vitamin nicotinic acid; biosynthesis may be of either the oxidized form, NAD, or the reduced form, NADH. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQTAARRSFD | YDMPLIQTPT | SACQIRQAWA | KVADTPDRET | ADRLKDEIKA | LLKETNAVLV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AHYYVDPLIQ | DLALETGGCV | GDSLEMARFG | AEHEAGTLVV | AGVRFMGESA | KILCPEKTVL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MPDLEAECSL | DLGCPEEAFS | AFCDQHPDRT | VVVYANTSAA | VKARADWVVT | SSVALEIVSY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKSRGEKLIW | GPDRHLGDYI | CRETGADMLL | WQGSCIVHNE | FKGQELAALK | AEHPDAVVLV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HPESPQSVIE | LSDVVGSTSK | LLKAAVSRPE | KKFIVATDLG | ILHEMQKQAP | DKQFIAAPTA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GNGGSCKSCA | FCPWMAMNSL | GGIKYALTSG | RNEILLDRKL | GEAAKLPLQR | MLDFAAGLKR |
| GDVFNGMGPA |