Q8NSL3
Gene name |
prpD2 (Cgl0657, cg0759) |
Protein name |
2-methylcitrate dehydratase 2 |
Names |
2-MC dehydratase, Aconitate hydratase, ACN, Aconitase |
Species |
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) |
KEGG Pathway |
cgl:Cgl0657 |
EC number |
4.2.1.3: Hydro-lyases |
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 Q8NSL3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8NSL3-F1 | Predicted | AlphaFoldDB |
No variants for Q8NSL3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8NSL3 | |||||
No associated diseases with Q8NSL3
No regional properties for Q8NSL3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q8NSL3 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.3 | Hydro-lyases |
| 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 |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-methylcitrate dehydratase activity | Catalysis of the reaction: (2S,3S)-2-methylcitrate = cis-2-methylaconitate + H(2)O. |
| aconitate hydratase activity | Catalysis of the reaction: citrate = isocitrate. The reaction occurs in two steps: (1) citrate = cis-aconitate + H2O, (2) cis-aconitate + H2O = isocitrate. This reaction is the interconversion of citrate and isocitrate via the labile, enzyme-bound intermediate cis-aconitate. Water is removed from one part of the citrate molecule and added back to a different atom to form isocitrate. |
| citrate dehydratase activity | Catalysis of the reaction: citrate = cis-aconitate + H2O. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| propionate metabolic process, methylcitrate cycle | The chemical reactions and pathways involving propionate that occur in the methylcitrate cycle. |
| tricarboxylic acid cycle | A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MINHEVRTHR | SAEEFPYEEH | LAHKIARVAA | DPVEVAADTQ | EMIINRIIDN | ASVQAASVLR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RPVSSARAMA | QVRPVTDGRG | ASVFGLPGRY | AAEWAALANG | TAVRELDFHD | TFLAAEYSHP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GDNIPPILAA | AQQAGKGGKD | LIRGIATGYE | IQVNLVRGMC | LHEHKIDHVA | HLGPSAAAGI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GTLLDLDVDT | IYQAIGQALH | TTTATRQSRK | GAISSWKAFA | PAFAGKMSIE | AVDRAMRGEG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| APSPIWEGED | GVIAWLLSGL | DHIYTIPLPA | EGEAKRAILD | TYTKEHSAEY | QSQAPIDLAR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SMGEKLAAQG | LDLRDVDSIV | LHTSHHTHYV | IGTGSNDPQK | FDPDASRETL | DHSIMYIFAV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ALEDRAWHHE | RSYAPERAHR | RETIELWNKI | STVEDPEWTR | RYHSVDPAEK | AFGARAVITF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KDGTVVEDEL | AVADAHPLGA | RPFAREQYIQ | KFRTLAEGVV | SEKEQDRFLD | AAQRTHELED |
| 490 | 500 | ||||
| LSELNIELDA | DILAKAPVIP | EGLF |