Q8DDP9
Gene name |
ubiE |
Protein name |
Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE |
Names |
2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, Demethylmenaquinone methyltransferase |
Species |
Vibrio vulnificus (strain CMCP6) |
KEGG Pathway |
vvu:VV1_0909 |
EC number |
2.1.1.163: Methyltransferases |
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 Q8DDP9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8DDP9-F1 | Predicted | AlphaFoldDB |
No variants for Q8DDP9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8DDP9 | |||||
No associated diseases with Q8DDP9
2 regional properties for Q8DDP9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | UbiE/COQ5 methyltransferase, conserved site | 45 - 60 | IPR023576-1 |
| conserved_site | UbiE/COQ5 methyltransferase, conserved site | 167 - 181 | IPR023576-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.1.163 | Methyltransferases |
| 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 |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-octaprenyl-6-methoxy-1,4-benzoquinone methylase activity | Catalysis of the reaction: 2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine = 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine. |
| demethylmenaquinone methyltransferase activity | Catalysis of the reaction: 2-demethylmenaquinone + S-adenosyl-L-methionine = menaquinone + S-adenosyl-L-homocysteine. |
| S-adenosylmethionine:2-demethylmenaquinol methyltransferase activity | Catalysis of the reaction: S-adenosyl-L-methionine + a demethylmenaquinol <=> S-adenosyl-L-homocysteine + H+ + a menaquinol. |
| S-adenosylmethionine:2-demethylmenaquinol-7 methyltransferase activity | Catalysis of the reaction: 2-demethylmenaquinol-7 + S-adenosyl-L-methionine = menaquinol-7 + S-adenosyl-L-homocysteine + H+. |
| S-adenosylmethionine:2-demethylquinol-8 methyltransferase activity | Catalysis of the reaction: 2-demethylmenaquinol-8 + S-adenosyl-L-methionine <=> menaquinol-8 + H+ + S-adenosyl-L-homocysteine. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| aerobic respiration | The enzymatic release of energy from inorganic and organic compounds (especially carbohydrates and fats) which requires oxygen as the terminal electron acceptor. |
| menaquinone biosynthetic process | The chemical reactions and pathways resulting in the formation of any of the menaquinones. Structurally, menaquinones consist of a methylated naphthoquinone ring structure and side chains composed of a variable number of unsaturated isoprenoid residues. Menaquinones that have vitamin K activity and are known as vitamin K2. |
| methylation | The process in which a methyl group is covalently attached to a molecule. |
| ubiquinone biosynthetic process | The chemical reactions and pathways resulting in the formation of ubiquinone, a lipid-soluble electron-transporting coenzyme. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDISVQSNT | ALESSETTHF | GFTTVAKEEK | VAKVAQVFHS | VAAKYDIMND | LMSGGIHRLW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KRFTIDCSGA | RPGQRVLDLG | GGTGDLTAKF | SRIVGEKGHV | ILADINNSML | NVGRDKLRDS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GIVGNVHYVQ | ANAEELPFPD | DYFDIITISF | CLRNVTDKDK | ALRSMFRVLK | PGGRLLVLEF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SKPVFDPLSK | VYDAYSFHLL | PKMGELVAND | ADSYRYLAES | IRMHPDQETL | KGMMQEAGFE |
| 250 | |||||
| NTSYYNLTGG | IVALHRGYKF |