Q9DCL9
Gene name |
Paics |
Protein name |
Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase |
Names |
PAICS |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:67054 |
EC number |
4.1.1.21: Carboxy-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 Q9DCL9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9DCL9-F1 | Predicted | AlphaFoldDB |
23 variants for Q9DCL9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388770538 | 39 | I>F | No | EVA | |
| rs3388764215 | 60 | I>N | No | EVA | |
| rs3395779480 | 63 | C>F | No | EVA | |
| rs3395779494 | 116 | Q>* | No | EVA | |
| rs580452369 | 172 | I>V | No | EVA | |
| rs3388768014 | 177 | E>K | No | EVA | |
| rs3388760906 | 221 | D>A | No | EVA | |
| rs3388739220 | 259 | L>P | No | EVA | |
| rs3388760879 | 261 | K>N | No | EVA | |
| rs3388760885 | 264 | S>N | No | EVA | |
| rs3388774049 | 277 | D>H | No | EVA | |
| rs3388774058 | 293 | I>N | No | EVA | |
| rs3388749504 | 295 | C>* | No | EVA | |
| rs3388767966 | 295 | C>S | No | EVA | |
| rs3388774079 | 344 | A>T | No | EVA | |
| rs3395779500 | 369 | P>PSGKTLKFWAHTALKIFKVLPLGSRRDDHTS*A | No | EVA | |
| rs3395790710 | 393 | L>S | No | EVA | |
| rs3395779474 | 396 | H>D | No | EVA | |
| rs3395779685 | 399 | W>* | No | EVA | |
| rs3395407170 | 399 | W>* | No | EVA | |
| rs3395790678 | 400 | A>P | No | EVA | |
| rs3388765337 | 406 | I>L | No | EVA | |
| rs3388765266 | 412 | S>F | No | EVA |
No associated diseases with Q9DCL9
5 regional properties for Q9DCL9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | PurE domain | 266 - 413 | IPR000031 |
| conserved_site | SAICAR synthetase, conserved site | 93 - 107 | IPR018236-1 |
| conserved_site | SAICAR synthetase, conserved site | 187 - 195 | IPR018236-2 |
| domain | SAICAR synthetase/ADE2, N-terminal | 10 - 258 | IPR028923 |
| domain | Class II PurE | 266 - 421 | IPR033626 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.1.21 | Carboxy-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 5-amino-4-imidazole carboxylate lyase activity | Catalysis of the reaction: 5-aminoimidazole + CO2 = 5-amino-4-imidazole carboxylate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| identical protein binding | Binding to an identical protein or proteins. |
| phosphoribosylaminoimidazole carboxylase activity | Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + 2 H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2). |
| phosphoribosylaminoimidazolesuccinocarboxamide synthase activity | Catalysis of the reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate + ATP = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + 2 H(+) + phosphate. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| 'de novo' AMP biosynthetic process | The chemical reactions and pathways resulting in the formation of adenosine monophosphate (AMP) from inosine 5'-monophosphate (IMP). |
| 'de novo' IMP biosynthetic process | The chemical reactions and pathways resulting in the formation of IMP, inosine monophosphate, by the stepwise assembly of a purine ring on ribose 5-phosphate. |
| 'de novo' XMP biosynthetic process | The chemical reactions and pathways resulting in the formation of XMP, xanthosine monophosphate, from simpler precursors. |
| GMP biosynthetic process | The chemical reactions and pathways resulting in the formation of GMP, guanosine monophosphate. |
| purine nucleobase biosynthetic process | The chemical reactions and pathways resulting in the formation of purine nucleobases, one of the two classes of nitrogen-containing ring compounds found in DNA and RNA, which include adenine and guanine. |
2 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9I7S8 | Paics | Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase | Drosophila melanogaster (Fruit fly) | PR |
| P22234 | PAICS | Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase | Homo sapiens (Human) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATAVVVNIG | KKLYEGKTKE | VYELLDTPGR | VLLQSKDQIT | AGNAARKNHL | EGKAAISNKI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TSCIFQLLQE | AGIKTAFTKK | CGETAFIAPQ | CEMIPIEWVC | RRIATGSFLK | RNPGVQEGYK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FYPPKVEMFF | KDDANNDPQW | SEEQLIAAKF | CFAGLVIGQT | EVDIMSHATQ | AIFEILEKSW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LPQDCTLVDM | KIEFGVDVTT | KEIVLADVID | NDSWRLWPSG | DRSQQKDKQS | YRDLKEVTPE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GLQMVKKNFE | WVADRVELLL | KSDSQCRVVV | LMGSTSDLGH | CEKIKKACGN | FGIPCELRVT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SAHKGPDETL | RIKAEYEGDG | IPTVFVSVAG | RSNGLGPVLS | GNTAYPVISC | PPITPDWGAQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DVWSSLRLPS | GIGCSTILSP | EGSAQFAAQI | FGLNNHLVWA | KLRASILNTW | ISLKQADKKV |
| RQCNL |