Q9A6Q5
Gene name |
thiC (CC_2029) |
Protein name |
Phosphomethylpyrimidine synthase |
Names |
Hydroxymethylpyrimidine phosphate synthase, HMP-P synthase, HMP-phosphate synthase, HMPP synthase, Thiamine biosynthesis protein ThiC |
Species |
Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus) |
KEGG Pathway |
ccr:CC_2029 |
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
5 structures for Q9A6Q5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3EPM | X-ray | 279 A | A/B | 1-612 | PDB |
| 3EPN | X-ray | 211 A | A/B | 1-612 | PDB |
| 3EPO | X-ray | 210 A | A/B | 1-612 | PDB |
| 4S2A | X-ray | 293 A | A | 1-612 | PDB |
| AF-Q9A6Q5-F1 | Predicted | AlphaFoldDB |
No variants for Q9A6Q5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9A6Q5 | |||||
No associated diseases with Q9A6Q5
1 regional properties for Q9A6Q5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ThiC-associated domain | 17 - 72 | IPR025747 |
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 |
4 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. |
| 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase activity | Catalysis of the reaction: 5-aminoimidazole ribonucleotide + S-adenosylmethionine = 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate + 5'deoxyadenosine. |
| carbon-carbon lyase activity | Catalysis of the cleavage of C-C bonds by other means than by hydrolysis or oxidation, or conversely adding a group to a double bond. |
| zinc ion binding | Binding to a zinc ion (Zn). |
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 |
| MNIQSTIKAV | AETISTGPIP | GSRKVYQAGE | LFPELRVPFR | EVAVHPSANE | PPVTIYDPSG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PYSDPAIQID | IEKGLPRTRE | ALVVARGDVE | EVADPRQVKP | EDNGFAQGKH | LAPEFPDTGR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KIYRAKPGKL | VTQLEYARAG | IITAEMEYVA | IRENLRREQD | RPCVRDGEDF | GASIPDFVTP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EFVRQEIARG | RAIIPANINH | GELEPMAIGR | NFLVKINANI | GNSAVLSTVA | DEVDKLVWAT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RWGADTVMDL | STGRNIHNIR | DWIIRNSSVP | IGTVPIYQAL | EKVNGVAEDL | NWEVFRDTLI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EQCEQGVDYF | TIHAGVRLPF | IPMTAKRVTG | IVSRGGSIMA | KWCLAHHKEN | FLYERFDEIC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EIMRAYDVSF | SLGDGLRPGS | TADANDEAQF | SELRTLGELT | KVAWKHGVQV | MIEGPGHVAM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HKIKANMDEQ | LKHCHEAPFY | TLGPLTTDIA | PGYDHITSAI | GAAMIGWFGT | AMLCYVTPKE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HLGLPDRDDV | KTGVITYKLA | AHAADLAKGH | PGAAMWDDAI | SRARFEFRWE | DQFNLGLDPE |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TARKFHDETL | PKEAHKTAHF | CSMCGPKFCS | MKISQEVRDF | AAGKAPNSAE | LGMAEMSEKF |
| 610 | |||||
| REQGSEIYLK | TE |