Q1QVV9
Gene name |
folD |
Protein name |
Bifunctional protein FolD |
Names |
|
Species |
Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11) |
KEGG Pathway |
csa:Csal_2048 |
EC number |
1.5.1.5: 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
1 structures for Q1QVV9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1QVV9-F1 | Predicted | AlphaFoldDB |
No variants for Q1QVV9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1QVV9 | |||||
No associated diseases with Q1QVV9
3 regional properties for Q1QVV9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain | 6 - 121 | IPR020630 |
| domain | Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain | 116 - 281 | IPR020631 |
| conserved_site | Tetrahydrofolate dehydrogenase/cyclohydrolase, conserved site | 260 - 268 | IPR020867 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.5.1.5 | With NAD(+) or NADP(+) as acceptor |
| 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 |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| methenyltetrahydrofolate cyclohydrolase activity | Catalysis of the reaction: 5,10-methenyltetrahydrofolate + H2O = 10-formyltetrahydrofolate. |
| methylenetetrahydrofolate dehydrogenase (NADP+) activity | Catalysis of the reaction: 5,10-methylenetetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| histidine biosynthetic process | The chemical reactions and pathways resulting in the formation of histidine, 2-amino-3-(1H-imidazol-4-yl)propanoic acid. |
| methionine biosynthetic process | The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. |
| purine nucleotide biosynthetic process | The chemical reactions and pathways resulting in the formation of a purine nucleotide, a compound consisting of nucleoside (a purine base linked to a deoxyribose or ribose sugar) esterified with a phosphate group at either the 3' or 5'-hydroxyl group of the sugar. |
| tetrahydrofolate interconversion | The chemical reactions and pathways by which one-carbon (C1) units are transferred between tetrahydrofolate molecules, to synthesise other tetrahydrofolate molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTAQLIDGKA | IAANVREQVS | RQVQARRQEG | KRAPGLAVVL | VGEDPASEVY | VRNKHRACDK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AGVHSVQHKL | PADTTQADLE | ALIDSLNADC | SIDGILVQLP | LPDHLDARPI | LERIRPDKDV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DGFHPYNLGR | LAQRLPVLRP | CTPKGIMTLL | QESGIHARGL | DAVIVGASNI | VGRPMALELM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LAGSTTTVCH | RFTRDLESHV | RRADLLVVAV | GRPGLVKGEW | VKEGAVVIDV | GINRQDDGKL |
| 250 | 260 | 270 | 280 | ||
| AGDVEFAPAA | ARASYITPVP | GGVGPMTVAS | LLENTLFAAE | LHDGMHA |