P9WKK7
Gene name |
icl (Rv0467, MTV038.11) |
Protein name |
Isocitrate lyase |
Names |
ICL, Isocitrase, Isocitratase |
Species |
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
KEGG Pathway |
mtu:Rv0467 |
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
12 structures for P9WKK7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1F61 | X-ray | 200 A | A/B | 2-428 | PDB |
| 1F8I | X-ray | 225 A | A/B/C/D | 2-428 | PDB |
| 1F8M | X-ray | 180 A | A/B/C/D | 2-428 | PDB |
| 5DQL | X-ray | 178 A | A/B/C/D | 1-428 | PDB |
| 6C4A | X-ray | 180 A | A/B/C/D/E/F/G/H | 1-428 | PDB |
| 6C4C | X-ray | 220 A | A/B/C/D/E/F/G/H | 1-428 | PDB |
| 6VB9 | X-ray | 188 A | A/B/C/D | 1-428 | PDB |
| 6WSI | X-ray | 175 A | A/B/C/D | 1-428 | PDB |
| 6XPP | X-ray | 155 A | A/B/C/D | 1-428 | PDB |
| 7CP1 | X-ray | 258 A | A/B | 1-428 | PDB |
| 7RB1 | X-ray | 190 A | A/B/C/D | 1-428 | PDB |
| AF-P9WKK7-F1 | Predicted | AlphaFoldDB |
No variants for P9WKK7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P9WKK7 | |||||
No associated diseases with P9WKK7
1 regional properties for P9WKK7
| 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 | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| extracellular region | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
4 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. |
| zymogen binding | Binding to a zymogen, an enzymatically inactive precursor of an enzyme that is often convertible to an active enzyme by proteolysis. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to hypoxia | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level. |
| 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. |
| isocitrate metabolic process | The chemical reactions and pathways involving isocitrate, the anion of isocitric acid, 1-hydroxy-1,2,3-propanetricarboxylic acid. Isocitrate is an important intermediate in the TCA cycle and the glycoxylate cycle. |
| response to host immune response | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detecting the immune response of the host organism. The host is defined as the larger of the organisms involved in a symbiotic interaction. |
| 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 |