P28037
Gene name |
Aldh1l1 |
Protein name |
Cytosolic 10-formyltetrahydrofolate dehydrogenase |
Names |
10-FTHFDH, FDH, Aldehyde dehydrogenase family 1 member L1, FBP-CI |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:64392 |
EC number |
1.5.1.6: With NAD(+) or NADP(+) as acceptor |
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
17 structures for P28037
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1S3I | X-ray | 230 A | A | 1-310 | PDB |
| 2O2P | X-ray | 170 A | A/B/C/D | 397-902 | PDB |
| 2O2Q | X-ray | 200 A | A/B/C/D | 397-902 | PDB |
| 2O2R | X-ray | 220 A | A/B/C/D | 397-902 | PDB |
| 3RHJ | X-ray | 189 A | A/B/C/D | 397-902 | PDB |
| 3RHL | X-ray | 200 A | A/B/C/D | 397-902 | PDB |
| 3RHM | X-ray | 238 A | A/B/C/D | 397-902 | PDB |
| 3RHO | X-ray | 226 A | A/B/C/D | 397-902 | PDB |
| 3RHP | X-ray | 250 A | A/B/C/D | 397-902 | PDB |
| 3RHQ | X-ray | 210 A | A/B/C/D | 397-902 | PDB |
| 3RHR | X-ray | 230 A | A/B/C/D | 397-902 | PDB |
| 4GNZ | X-ray | 230 A | A/B/C/D | 397-902 | PDB |
| 4GO0 | X-ray | 338 A | A/B/C/D | 397-902 | PDB |
| 4GO2 | X-ray | 228 A | A/B/C/D | 397-902 | PDB |
| 7RLT | EM | 370 A | A/B/C/D | 1-902 | PDB |
| 7RLU | EM | 290 A | A/B/C/D | 1-902 | PDB |
| AF-P28037-F1 | Predicted | AlphaFoldDB |
5 variants for P28037
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3320253589 | 386 | G>E | No | EVA | |
| rs3320191876 | 431 | V>M | No | EVA | |
| rs3320306368 | 488 | L>P | No | EVA | |
| rs3320320862 | 488 | L>V | No | EVA | |
| rs8162596 | 852 | K>N | No | EVA |
No associated diseases with P28037
7 regional properties for P28037
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Phosphoribosylglycinamide formyltransferase, active site | 131 - 154 | IPR001555 |
| domain | Formyl transferase, N-terminal | 1 - 180 | IPR002376 |
| domain | Formyl transferase, C-terminal | 205 - 309 | IPR005793 |
| domain | Phosphopantetheine binding ACP domain | 318 - 395 | IPR009081 |
| domain | Aldehyde dehydrogenase domain | 430 - 898 | IPR015590 |
| conserved_site | Aldehyde dehydrogenase, cysteine active site | 700 - 711 | IPR016160 |
| conserved_site | Aldehyde dehydrogenase, glutamic acid active site | 672 - 679 | IPR029510 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.5.1.6 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 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. |
| protein-containing complex | A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| aldehyde dehydrogenase (NAD+) activity | Catalysis of the reaction: an aldehyde + NAD+ + H2O = an acid + NADH + H+. |
| aldehyde dehydrogenase (NADP+) activity | Catalysis of the reaction: an aldehyde + NADP+ + H2O = an acid + NADPH + H+. |
| aldehyde dehydrogenase [NAD(P)+] activity | Catalysis of the reaction: an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+. |
| formyltetrahydrofolate dehydrogenase activity | Catalysis of the reaction: 10-formyltetrahydrofolate + H(2)O + NADP(+) = (6S)-5,6,7,8-tetrahydrofolate + CO(2) + H(+) + NADPH. |
| hydroxymethyl-, formyl- and related transferase activity | Catalysis of the transfer of a hydroxymethyl- or formyl group from one compound (donor) to another (acceptor). |
| protein-containing complex binding | Binding to a macromolecular complex. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| 10-formyltetrahydrofolate catabolic process | The chemical reactions and pathways resulting in the breakdown of 10-formyltetrahydrofolate, the formylated derivative of tetrahydrofolate. |
| bile acid signaling pathway | The series of molecular signals initiated by bile acid binding to its receptor, and ending with the regulation of a downstream cellular process, e.g. transcription. |
| folic acid metabolic process | The chemical reactions and pathways involving folic acid, pteroylglutamic acid. Folic acid is widely distributed as a member of the vitamin B complex and is essential for the synthesis of purine and pyrimidines. |
| NADPH regeneration | A metabolic process that generates a pool of NADPH by the reduction of NADP+. |
| one-carbon metabolic process | The chemical reactions and pathways involving the transfer of one-carbon units in various oxidation states. |
| tetrahydrofolate biosynthetic process | The chemical reactions and pathways resulting in the formation of tetrahydrofolate, 5,6,7,8-tetrahydrofolic acid, a folate derivative bearing additional hydrogens on the pterin group. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q8R0Y6 | Aldh1l1 | Cytosolic 10-formyltetrahydrofolate dehydrogenase | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKIAVIGQSL | FGQEVYCQLR | KEGHEVVGVF | TIPDKDGKAD | PLGLEAEKDG | VPVFKFPRWR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ARGQALPEVV | AKYQALGAEL | NVLPFCSQFI | PMEVINAPRH | GSIIYHPSLL | PRHRGASAIN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WTLIHGDKKG | GFTIFWADDG | LDTGDLLLQK | ECEVLPDDTV | STLYNRFLFP | EGIKGMVQAV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLIAEGTAPR | CPQSEEGATY | EGIQKKETAK | INWDQPAEAI | HNWIRGNDKV | PGAWTEACGQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KLTFFNSTLN | TSGLSTQGEA | LPIPGAHRPG | VVTKAGLILF | GNDDRMLLVK | NIQLEDGKMM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PASQFFKGSA | SSDLELTEAE | LATAEAVRSS | WMRILPNVPE | VEDSTDFFKS | GAASVDVVRL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VEEVKELCDG | LELENEDVYM | ATTFRGFIQL | LVRKLRGEDD | ESECVINYVE | KAVNKLTLQM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PYQLFIGGEF | VDAEGSKTYN | TINPTDGSVI | CQVSLAQVSD | VDKAVAAAKE | AFENGLWGKI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NARDRGRLLY | RLADVMEQHQ | EELATIEALD | AGAVYTLALK | THVGMSIQTF | RYFAGWCDKI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QGATIPINQA | RPNRNLTLTK | KEPVGVCGIV | IPWNYPLMML | SWKTAACLAA | GNTVVIKPAQ |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VTPLTALKFA | ELTLKAGIPK | GVVNILPGSG | SLVGQRLSDH | PDVRKIGFTG | STEVGKHIMK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SCALSNVKKV | SLELGGKSPL | IIFADCDLNK | AVQMGMSSVF | FNKGENCIAA | GRLFVEESIH |
| 730 | 740 | 750 | 760 | 770 | 780 |
| NQFVQKVVEE | VEKMKIGNPL | ERDTNHGPQN | HEAHLRKLVE | YCQRGVKEGA | TLVCGGNQVP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| RPGFFFQPTV | FTDVEDHMYI | AKEESFGPIM | IISRFADGDV | DAVLSRANAT | EFGLASGVFT |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RDINKALYVS | DKLQAGTVFI | NTYNKTDVAA | PFGGFKQSGF | GKDLGEAALN | EYLRIKTVTF |
| EY |