Q10306
Gene name |
cit1 (SPAC6C3.04) |
Protein name |
Probable citrate synthase, mitochondrial |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC6C3.04 |
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 Q10306
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q10306-F1 | Predicted | AlphaFoldDB |
2 variants for Q10306
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_2328838_C_A | 65 | A>E | No | Jeffares_SNPs | |
| I_2329746_G_A | 368 | V>I | No | Jeffares_SNPs |
No associated diseases with Q10306
1 regional properties for Q10306
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Citrate synthase active site | 363 - 375 | IPR019810 |
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. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
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 |
| MMIILNAPRF | MTNTRLASTR | RLASSLLSQA | SLRSRQLNPL | FTSSYSTRSS | SLKDRLAELI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PEKQAEIKKF | RAEHGQDVIG | EVTINQMYGG | ARGVRSLIWE | GSVLDPNEGI | RFRGYTIPEC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QKLLPSSPNG | KQPLPESLFW | LLVTGEIPTL | SQVQALSADW | AARSQLPKFV | EELIDRCPPT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LHPMAQFSLA | VTALEHDSAF | AKAYERGMNK | HDYWKYEYED | CMDLIAKTVP | IAGRIYRNLY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RDGVVAPIQM | DKDHSYNFAN | VLGFANNEEF | VELMRLYLTI | HADHEGGNVS | AHTGHLVGSA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSSPFLSMAA | SLNGLAGPLH | GLANQEVLNF | LITMKKEIGD | DLSEETIKSY | LWKLLNSGRV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VPGYGHAVLR | KTDPRYTAQR | EFALEHLPKD | PMFQLVSRLY | EIVPGVLTEH | GKTKNPYPNV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DSHSGVLLQY | YGLKEQSFYT | VLFGVSRTLG | VASQLIWDRA | LGLPIERPKS | FSTEALKKMV |
| ETK |