Q97YJ8
Gene name |
thiC1 |
Protein name |
Phosphomethylpyrimidine synthase 1 |
Names |
Hydroxymethylpyrimidine phosphate synthase 1, HMP-P synthase 1, HMP-phosphate synthase 1, HMPP synthase 1, Thiamine biosynthesis protein ThiC 1 |
Species |
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) |
KEGG Pathway |
sso:SSO1324 |
EC number |
4.1.99.17: Other carbon-carbon 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 Q97YJ8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q97YJ8-F1 | Predicted | AlphaFoldDB |
No variants for Q97YJ8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q97YJ8 | |||||
No associated diseases with Q97YJ8
No regional properties for Q97YJ8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q97YJ8 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.99.17 | Other carbon-carbon 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 |
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. |
| lyase activity | Catalysis of the cleavage of C-C, C-O, C-N and other bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. They differ from other enzymes in that two substrates are involved in one reaction direction, but only one in the other direction. When acting on the single substrate, a molecule is eliminated and this generates either a new double bond or a new ring. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| thiamine biosynthetic process | The chemical reactions and pathways resulting in the formation of thiamine (vitamin B1), a water soluble vitamin present in fresh vegetables and meats, especially liver. |
| thiamine diphosphate biosynthetic process | The chemical reactions and pathways resulting in the formation of thiamine diphosphate, a derivative of thiamine (vitamin B1) which acts as a coenzyme in a range of processes including the Krebs cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAIIEEARSG | QITDEMKEIS | KLEGIPVEKV | RNRISECKII | LIRNAKYPSK | KLVPIGKGLT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TKVNINIGTS | DEVVNLQMEL | EKVKVANRWG | DTLMDLSTGG | DLDDIRREII | RASELPVGTV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PVYQVFIESF | KKKSGGAYFT | EDELLSTVEK | HLKDGVAFMT | IHAGITKELA | IRALKSNRII |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PIVSRGGDMI | AGWMIHNNSE | NPYRKHWGYL | LEMFKEYDAV | ISLGDALRPG | ATGDAHDEFQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VGELLETARL | VKSALKEGVQ | VMVEGPGHVP | LNEIAWDVKL | MKKLTGGVPY | YVLGPLPIDV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GAPYDHIASA | IGAAISSAAG | ADLLCYLTPA | EHLGLPTVKQ | VEEGAIAYRI | AAHAGDVVKL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GRRVRKWDDE | VSYYRGKLEW | DNMISRLIDP | QRAYQVYTQF | GIPKVKACTM | CGGYCPMMWA |
| 430 | |||||
| MDQVRKIGSS | SSL |