H8EVV4
Gene name |
icl1 (ERDMAN_0512, Q643_00485) |
Protein name |
Isocitrate lyase 1 |
Names |
ICL1, Isocitrase, Isocitratase, Methylisocitrate lyase, MICA |
Species |
Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman) |
KEGG Pathway |
mtn:ERDMAN_0512 |
EC number |
4.1.3.1: Oxo-acid-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 H8EVV4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-H8EVV4-F1 | Predicted | AlphaFoldDB |
No variants for H8EVV4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for H8EVV4 | |||||
No associated diseases with H8EVV4
1 regional properties for H8EVV4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Isocitrate lyase/phosphorylmutase, conserved site | 189 - 194 | IPR018523 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.3.1 | Oxo-acid-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 |
|---|---|
| isocitrate lyase activity | Catalysis of the reaction: isocitrate = glyoxylate + succinate. |
| metal ion binding | Binding to a metal ion. |
| methylisocitrate lyase activity | Catalysis of the reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glyoxylate cycle | A modification of the TCA cycle occurring in some plants and microorganisms, in which isocitrate is cleaved to glyoxylate and succinate. Glyoxylate can then react with acetyl-CoA to form malate. |
| 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 |
| MSVVGTPKSA | EQIQQEWDTN | PRWKDVTRTY | SAEDVVALQG | SVVEEHTLAR | RGAEVLWEQL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| HDLEWVNALG | ALTGNMAVQQ | VRAGLKAIYL | SGWQVAGDAN | LSGHTYPDQS | LYPANSVPQV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VRRINNALQR | ADQIAKIEGD | TSVENWLAPI | VADGEAGFGG | ALNVYELQKA | LIAAGVAGSH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| WEDQLASEKK | CGHLGGKVLI | PTQQHIRTLT | SARLAADVAD | VPTVVIARTD | AEAATLITSD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VDERDQPFIT | GERTREGFYR | TKNGIEPCIA | RAKAYAPFAD | LIWMETGTPD | LEAARQFSEA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VKAEYPDQML | AYNCSPSFNW | KKHLDDATIA | KFQKELAAMG | FKFQFITLAG | FHALNYSMFD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LAYGYAQNQM | SAYVELQERE | FAAEERGYTA | TKHQREVGAG | YFDRIATTVD | PNSSTTALTG |
| STEEGQFH |