Q8ZZC0
Gene name |
thiC |
Protein name |
Phosphomethylpyrimidine synthase |
Names |
Hydroxymethylpyrimidine phosphate synthase, HMP-P synthase, HMP-phosphate synthase, HMPP synthase, Thiamine biosynthesis protein ThiC |
Species |
Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2) |
KEGG Pathway |
pai:PAE0333 |
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 Q8ZZC0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8ZZC0-F1 | Predicted | AlphaFoldDB |
No variants for Q8ZZC0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8ZZC0 | |||||
No associated diseases with Q8ZZC0
No regional properties for Q8ZZC0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8ZZC0 | |||
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 |
| MDNTIIRRAR | EGRIDDEMRK | IAEAEGVSPE | KLRDRIAKGQ | VVYIRNVKWP | SEKVVAIGKG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSTKINVNLG | TSTEVVDLDS | ELKKVEVANK | WGDTLMDLSV | GGDLDAIRRA | VISKSKLPVG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TVPVYQAFIE | AFNKRSGGAY | FTIDDLFNTI | ERQLKDGVAF | MTIHAAVTKE | AAIRVLKSDR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VIPVVSRGGD | MIIGWMLHND | AENPYLTHWD | YLLELFAQYD | AVISIGDALR | PGAVADAHDE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FHVGELVEAA | RLAKRAIKAG | VQVMIEGPGH | VPLNDVIWTI | KLEKRLTGGV | PYYVLGPLPT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DVAAPYDHIA | SAVGAALAAA | AGADLLCYIT | PAEHLSLPTV | EQVEQGAIAY | RIAAHIGDVV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KLGRKARRWD | DEVSYYRGRL | MWDEMIKRLV | DPERAYKVYT | QYGPPKVKGC | TMCGGYCPMN |
| MVIQQARRLK |