A3CU83
Gene name |
purD |
Protein name |
Phosphoribosylamine--glycine ligase |
Names |
GARS, Glycinamide ribonucleotide synthetase, Phosphoribosylglycinamide synthetase |
Species |
Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) |
KEGG Pathway |
mem:Memar_1000 |
EC number |
6.3.4.13: Other carbon--nitrogen ligases |
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 A3CU83
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A3CU83-F1 | Predicted | AlphaFoldDB |
No variants for A3CU83
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A3CU83 | |||||
No associated diseases with A3CU83
5 regional properties for A3CU83
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | ATP-grasp fold | 111 - 315 | IPR011761 |
| conserved_site | Phosphoribosylglycinamide synthetase, conserved site | 289 - 296 | IPR020559 |
| domain | Phosphoribosylglycinamide synthetase, C-domain | 329 - 418 | IPR020560 |
| domain | Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain | 105 - 295 | IPR020561 |
| domain | Phosphoribosylglycinamide synthetase, N-terminal | 3 - 104 | IPR020562 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.4.13 | Other carbon--nitrogen ligases |
| 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 |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| phosphoribosylamine-glycine ligase activity | Catalysis of the reaction: 5-phospho-D-ribosylamine + ATP + glycine = N(1)-(5-phospho-D-ribosyl)glycinamide + ADP + 2 H(+) + phosphate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| '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. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDMKVLVVGG | GGREHAITRA | LSCNSDTKIF | SVMARKNPGI | ARLSERVLLE | KETNIEKVIP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FATNCGVDAA | VIGPEAPLEA | GIVDRLEAAG | IPSLGPTRAA | ARIETDKAFC | RRLMERHGIA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GCPEYRVCRD | PEEARRFIES | YDGDLAVKPI | GLTGGKGVRI | MGEHVDVAGA | VEYAREIGGS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VVLEERLVGE | EFTLQAFVDG | EHLIPMPLVQ | DHKRAYEGDV | GPNTGGMGSY | SLADHMLPFV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SRRDYEKALR | IMTDTVAAMR | AEGTPYRGIL | YGQFMNTREG | PKVIEFNARF | GDPEAMNVLS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLESDFAGIV | GHIIEGDLAP | SHVRFAKKAT | VCKYLVPEGY | PDAPRANEPL | TLGDYGDALL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YYASVEERDG | TLHTLTSRTL | AFVGRGETLE | EAEAIAEKAA | SSVSGSVFHR | RDIGTPEILE |
| KRCQHMREIL |