A1SBA6
Gene name |
menD |
Protein name |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase |
Names |
SEPHCHC synthase, Menaquinone biosynthesis protein MenD |
Species |
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B) |
KEGG Pathway |
saz:Sama_3460 |
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 A1SBA6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1SBA6-F1 | Predicted | AlphaFoldDB |
No variants for A1SBA6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1SBA6 | |||||
No associated diseases with A1SBA6
3 regional properties for A1SBA6
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 |
| MDHLHSSTAE | LNLLWGSLIL | EELTRHGVMH | LCMAPGSRST | PLTLAAAAQD | KLTRHLHFDE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RGLGFLALGL | AKASQAPVAI | ITTSGTAVAN | LYPAIVEASL | THVPLIILSG | DRPWELIGCG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ANQAIEQLGI | FGGYARQLNL | PTPDLRIGPE | VLLSALDEQL | ANLDRPLHIN | CMYPEPLYPS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EHRFDQFDSY | LSRLGQWQDT | QVPYLSVANA | SLSAFPPRDA | MMRFVHGKGV | IVAGTLTEAE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TPTELITLSQ | KLGWPLLTDA | QSQLRQHPGA | IGHIDQLLLN | PRARALLDQA | ERVLVFGGRL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSKRLISYLA | EKDWHSYWQV | LPHQERLDPS | HSNKQLWLGR | AGDVCALEWP | RSSEANWAAS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LISLNQSVEQ | DFIHHIDGGE | FGEAQVIRAI | AASHTAEQQL | FIGNSLPVRL | YDMFAPIGCC |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AASTYTNRGA | SGIDGLIATA | CGVARHSGRP | TTLILGDLSA | LHDLNSLALA | RDCQSPLVIV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VLNNDGGNIF | NLLPVPTEEL | RSDFYRLSHG | LEFGYGAAMF | GLPYDRAEDM | EAFIDAYQAA |
| 550 | 560 | 570 | |||
| LEHPGASVIE | VTVAQDQASN | QIRRMAEWIR | SR |