P34948
Gene name |
PMI1 (MANA, CAALFM_C209640WA, CaO19.1390) |
Protein name |
Mannose-6-phosphate isomerase |
Names |
Phosphohexomutase, Phosphomannose isomerase, PMI |
Species |
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) |
KEGG Pathway |
cal:CAALFM_C209640WA |
EC number |
5.3.1.8: Interconverting aldoses and ketoses |
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
3 structures for P34948
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1PMI | X-ray | 170 A | A | 2-441 | PDB |
| 5NW7 | X-ray | 185 A | A | 1-441 | PDB |
| AF-P34948-F1 | Predicted | AlphaFoldDB |
No variants for P34948
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P34948 | |||||
No associated diseases with P34948
5 regional properties for P34948
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Phosphomannose isomerase, type I, conserved site | 130 - 138 | IPR018050-1 |
| conserved_site | Phosphomannose isomerase, type I, conserved site | 285 - 310 | IPR018050-2 |
| domain | Phosphomannose isomerase type I, C-terminal domain | 348 - 398 | IPR046456 |
| domain | Phosphomannose isomerase type I, catalytic domain | 6 - 155 | IPR046457 |
| domain | Phosphomannose isomerase type I, helical insertion domain | 171 - 266 | IPR046458 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.3.1.8 | Interconverting aldoses and ketoses |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| mannose-6-phosphate isomerase activity | Catalysis of the reaction: D-mannose 6-phosphate = D-fructose 6-phosphate. |
| zinc ion binding | Binding to a zinc ion (Zn). |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
| cell wall mannoprotein biosynthetic process | The chemical reactions and pathways resulting in the formation of cell wall mannoproteins, any cell wall protein that contains covalently bound mannose residues. |
| fungal-type cell wall organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall. |
| GDP-mannose biosynthetic process | The chemical reactions and pathways resulting in the formation of GDP-mannose, a substance composed of mannose in glycosidic linkage with guanosine diphosphate. |
| protein glycosylation | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSEKLFRIQ | CGYQNYDWGK | IGSSSAVAQF | VHNSDPSITI | DETKPYAELW | MGTHPSVPSK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AIDLNNQTLR | DLVTAKPQEY | LGESIITKFG | SSKELPFLFK | VLSIEKVLSI | QAHPDKKLGA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QLHAADPKNY | PDDNHKPEMA | IAVTDFEGFC | GFKPLDQLAK | TLATVPELNE | IIGQELVDEF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ISGIKLPAEV | GSQDDVNNRK | LLQKVFGKLM | NTDDDVIKQQ | TAKLLERTDR | EPQVFKDIDS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RLPELIQRLN | KQFPNDIGLF | CGCLLLNHVG | LNKGEAMFLQ | AKDPHAYISG | DIIECMAASD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NVVRAGFTPK | FKDVKNLVEM | LTYSYESVEK | QKMPLQEFPR | SKGDAVKSVL | YDPPIAEFSV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LQTIFDKSKG | GKQVIEGLNG | PSIVIATNGK | GTIQITGDDS | TKQKIDTGYV | FFVAPGSSIE |
| 430 | 440 | ||||
| LTADSANQDQ | DFTTYRAFVE | A |