Q6MHQ6
Gene name |
menD |
Protein name |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase |
Names |
SEPHCHC synthase, Menaquinone biosynthesis protein MenD |
Species |
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100) |
KEGG Pathway |
bba:Bd3484 |
EC number |
2.2.1.9: Transketolases and transaldolases |
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 Q6MHQ6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6MHQ6-F1 | Predicted | AlphaFoldDB |
No variants for Q6MHQ6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6MHQ6 | |||||
No associated diseases with Q6MHQ6
1 regional properties for Q6MHQ6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain | 4 - 125 | IPR012001 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.2.1.9 | Transketolases and transaldolases |
| 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase activity | Catalysis of the reaction: 2-oxoglutarate + H(+) + isochorismate = 5-enolpyruvoyl-6-hydroxy-2-succinyl-cyclohex-3-ene-1-carboxylate + CO(2). |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| manganese ion binding | Binding to a manganese ion (Mn). |
| thiamine pyrophosphate binding | Binding to thiamine pyrophosphate, the diphosphoric ester of thiamine. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTNMELAAKV | IQELVHTGVR | EFILCAGARN | SPMVHILDEC | KNLKVYSFFE | ERAAGFFALG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RIASTRRPVA | VITTSGTAVA | ELLPAAVEGT | YSSLPLIMVT | ADRPKHYRGS | GAPQTIEQVG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IFSYYNEVAL | DLDSENSHLS | FKSLSWKKPI | HVNVSFEEPL | IDGPVPQIHI | PSVSERTKLP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VQIPLGTLKE | METFVNTHKP | LVMVGILPEK | AYGTVLDFLK | QYKAPVYCEG | ISSLRGHPDL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KDVEIRSGEK | MIHRVLEMGV | CDSILRIGGI | PTARVWRDLE | DKYKELPVFS | VSFNHFTGLS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RPVQHCNSLD | LLSQVEFSYP | HHENVKVNIE | DAARATQIRQ | LLDKYPDSEQ | GMIYAISKRM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KGSSVYLGNS | LPIREWDSSS | SHDFPPARVA | ANRGANGIDG | QISTFLGWAH | PELENWCLVG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DLTALYDLSS | LWVTSQLDAK | KFRVVVINNG | GGQIFHRMFK | KEIFINKHQI | SFESWAKMWN |
| 490 | 500 | 510 | 520 | ||
| WSYDKWHTIP | EDNKELNLAD | HQIIELSPNW | EHTQEFWKEY | DLLWKE |