Q553V1
Gene name |
cs (DDB_G0275311) |
Protein name |
Citrate synthase, mitochondrial |
Names |
|
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0275311 |
EC number |
2.3.3.16: Acyl groups converted into alkyl groups on transfer |
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 Q553V1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q553V1-F1 | Predicted | AlphaFoldDB |
No variants for Q553V1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q553V1 | |||||
No associated diseases with Q553V1
4 regional properties for Q553V1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Actinin-type actin-binding domain, conserved site | 10 - 19 | IPR001589 |
| domain | Calponin homology domain | 8 - 115 | IPR001715-1 |
| domain | Calponin homology domain | 124 - 229 | IPR001715-2 |
| domain | Cortexillin, coiled coil | 231 - 337 | IPR015383 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.3.16 | Acyl groups converted into alkyl groups on transfer |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| phagocytic vesicle | A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| citrate (Si)-synthase activity | Catalysis of the reaction: acetyl-CoA + H2O + oxaloacetate = citrate + CoA, where the acetyl group is added to the si-face of oxaloacetate; acetyl-CoA thus provides the two carbon atoms of the pro-S carboxymethyl group. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| carbohydrate metabolic process | The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y. |
| citrate metabolic process | The chemical reactions and pathways involving citrate, 2-hydroxy-1,2,3-propanetricarboyxlate. Citrate is widely distributed in nature and is an important intermediate in the TCA cycle and the glyoxylate 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 |
| MFARLARANY | LKNSGRYFST | EPTLKERLVQ | IIPGKIEQVK | QLKTEHGDKI | IGTCTVAQAY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GGMRSVKSLV | TETSSLDPEE | GIRFRGLTIP | ECQEKLPKAP | GGAEPLPEGI | LWLLLTGEVP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TESQVKTLSK | DLAKRAGLPK | HVTSMIKAFP | EQMHPMSQLA | AAILALQGES | KFVKAYNDGV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KKDKYWESTL | EDSLDVIAKL | PEVAALIYQN | TYKKSDITHK | IDENLDWSAN | FNRMLGYTSK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DFDELMRLYL | TIHTDHEGGN | VSAHTTHLVG | SALSDSYLSL | SAGMCGLAGP | LHGLANQEVL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SWTMKLQEKL | GNKEVSNEVL | SEAIWEGLNA | GRVVPGFGHA | VLRKTDPRYT | CQREFALKHL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PQDPLFKLVS | QIYEVVPDIL | TKHGKTKNPY | PNVDAHSGCL | LQYYGLKEHN | FYTVLFGVSR |
| 430 | 440 | 450 | |||
| AIGVLSSLVW | DRILGHPIER | PKSVTTEWIS | SYVNSDQSKK |