Q9IAJ6
Gene name |
gatm |
Protein name |
Glycine amidinotransferase, mitochondrial |
Names |
L-arginine:glycine amidinotransferase, Transamidinase |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:379386 |
EC number |
2.1.4.1: Amidinotransferases |
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 Q9IAJ6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9IAJ6-F1 | Predicted | AlphaFoldDB |
No variants for Q9IAJ6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9IAJ6 | |||||
No associated diseases with Q9IAJ6
No regional properties for Q9IAJ6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q9IAJ6 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.4.1 | Amidinotransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| glycine amidinotransferase activity | Catalysis of the reaction: L-arginine + glycine = L-ornithine + guanidinoacetate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| creatine biosynthetic process | The chemical reactions and pathways resulting in the formation of creatine, N-[amino(imino)methyl]-N-methylglycine. Creatine is formed by a process beginning with amidino group transfer from L-arginine to glycine to form guanidinoacetate, followed by methyl group transfer from S-adenosyl-L-methionine to guanidinoacetate; it is then is phosphorylated to form a pool that stores high energy phosphate for the replenishment of ATP during periods of high, or fluctuating energy demand. In animals, most creatine is transported to and used in muscle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLRVRCLRGG | SRGAEAVHYI | GSMLRKSFVG | WVQRSFQSTQ | AAAVSEKPCA | ADEKVRDTAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QECPVCSYNE | WDPLEEVIVG | RPENANVPPF | SVEVKANTYE | KYWPFYQKHG | GQSFPVDHVK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KAIEEIEEMC | KVLKHEGVIV | QRPEVIDWSV | KYKTPDFEST | GMYAAMPRDI | LLVVGNEIIE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| APMAWRARFF | EYRAYRPLIK | DYFRRGAKWT | TAPKPTMADE | LYDQDYPIRT | VEDRHKLAAM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GKFVTTEFEP | CFDAADFMRA | GRDIFAQRSQ | VTNYLGIEWM | RRHLAPDYKV | HIISFKDPNP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| MHIDATFNII | GPGLVLSNPD | RPCHQIELFK | KAGWTVVTPP | TPLIPDNHPL | WMSSKWLSMN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VLMLDEKRVM | VDANETSIHK | MFEKLGISTI | KVNIRHANSL | GGGFHCWTCD | IRRRGTLQSY |
| FR |