P97275
Gene name |
AGPS |
Protein name |
Alkyldihydroxyacetonephosphate synthase, peroxisomal |
Names |
Alkyl-DHAP synthase, Alkylglycerone-phosphate synthase |
Species |
Cavia porcellus (Guinea pig) |
KEGG Pathway |
cpoc:100734021 |
EC number |
2.5.1.26: Transferring alkyl or aryl groups, other than methyl groups |
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
10 structures for P97275
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4BBY | X-ray | 190 A | A/B/C/D | 1-658 | PDB |
| 4BC7 | X-ray | 240 A | A/B/C/D | 1-658 | PDB |
| 4BC9 | X-ray | 241 A | A/B/C/D | 1-658 | PDB |
| 4BCA | X-ray | 240 A | A/B/C/D | 1-658 | PDB |
| 5ADZ | X-ray | 220 A | A/B/C/D | 1-658 | PDB |
| 5AE1 | X-ray | 210 A | A/B/C/D | 1-658 | PDB |
| 5AE2 | X-ray | 200 A | A/B/C/D | 1-658 | PDB |
| 5AE3 | X-ray | 218 A | A/B/C/D | 1-658 | PDB |
| 6GOU | X-ray | 290 A | A/B/C/D | 1-658 | PDB |
| AF-P97275-F1 | Predicted | AlphaFoldDB |
No variants for P97275
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P97275 | |||||
No associated diseases with P97275
No regional properties for P97275
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P97275 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.5.1.26 | Transferring alkyl or aryl groups, other than methyl groups |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| peroxisomal membrane | The lipid bilayer surrounding a peroxisome. |
| peroxisome | A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| alkylglycerone-phosphate synthase activity | Catalysis of the reaction: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone 3-phosphate + a long-chain acid anion. |
| FAD binding | Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| ether lipid biosynthetic process | The chemical reactions and pathways resulting in the formation of ether lipids, lipids that contain (normally) one lipid alcohol in ether linkage to one of the carbon atoms (normally C-1) of glycerol. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAEAAAAAAA | AAAAGETSAS | SGSAAERDPD | QDRAGRRLRV | LSGHLLGRPQ | EALSTNECKA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RRAASAATAA | PTATPAAPES | GIIPKKRQEL | MKWNGWGYND | SKFFLNKKGQ | LELTGKRYPL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SGVALPTFKD | WIQNTFGINL | DHKTTSKASL | NPSDTPPSIV | NEDFLHELKK | TNISYSQEAD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DRVFRAHGHC | LHEIFLLREG | MFERIPDIVL | WPTCHDDVVK | IVNLACKYNL | CIIPIGGGTS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VSYGLMCPAD | ETRTIISLDT | SQMNRILWVD | ENNLTAHVEA | GITGQELERQ | LKESGYCTGH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EPDSLEFSTV | GGWISTRASG | MKKNIYGNIE | DLVVHMKVVT | PRGVIEKSCQ | GPRMSTGPDI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HHFIMGSEGT | LGVITEATIK | IRPTPEYQKY | GSVAFPNFEQ | GVACLREIAK | QRCAPASIRL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MDNQQFQFGH | ALKPQVSSIF | TSFLDGLKKF | YITKFKGFDP | NQLSVATLLF | EGDREKVLQH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EKQVYDIAAK | FGGLAAGEDN | GQRGYLLTYV | IAYMRDLGLE | YYIIGESFET | SAPWDRVVDL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| CRNVKERIRR | ECKEKGVQFP | PLSTCRVTQT | YDAGACIYFY | FAFNYRGISD | PLAVFEQTEA |
| 610 | 620 | 630 | 640 | 650 | |
| AAREEILANG | GSLSHHHGVG | KLRKQWLKES | ISDVGFGMLK | SVKDYVDPTN | IFGNRNLL |