C7C436
Gene name |
mcsA |
Protein name |
2-methylcitrate synthase, mitochondrial |
Names |
Methylcitrate synthase, (2S,3S)-2-methylcitrate synthase, Citrate synthase 2 |
Species |
Gibberella moniliformis (Maize ear and stalk rot fungus) (Fusarium verticillioides) |
KEGG Pathway |
|
EC number |
2.3.3.5: 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 C7C436
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C7C436-F1 | Predicted | AlphaFoldDB |
No variants for C7C436
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C7C436 | |||||
No associated diseases with C7C436
1 regional properties for C7C436
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| active_site | Citrate synthase active site | 350 - 362 | IPR019810 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.3.5 | Acyl groups converted into alkyl groups on transfer |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 2-methylcitrate synthase activity | Catalysis of the reaction: H(2)O + oxaloacetate + propanoyl-CoA = (2R,3S)-2-methylcitrate + CoA + H(+). |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MALNLTSSRR | ALGSLKPLTR | AAFSGVRGYA | TAEPDLKATL | REAIPAKREL | LKKVKAHSNK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VLGEVKVENT | LGGMRGLKAM | VWEGSVLDAN | EGIRFHGRTI | KDCQKELPKG | KTGTEMLPEA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MFWLLLTGQV | PSVNQVRTFS | RELAEKAQIP | EFISKMLDNF | PKDLHPMTQF | AMAVSALNYE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SKFAKAYEQG | LNKADYWEPT | FDDCISLLAK | LPTIAAKIYQ | NAYRGGGALP | AEVDLEQDWS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YNFAAMLGKG | GKENENFQDL | LRLYLALHGD | HEGGNVSAHA | THLVGSALSD | PFLSYSAGLQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GLAGPLHGLA | AQEVLRWIIQ | MKEAIPANYT | EQDVNDYLWS | TLNSGRVVPG | YGHAVLRKPD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PRFEALMDYA | AARPEIANDP | VFQLVEKNSR | IAPEVLKKHG | KTKNPYPNVD | SSSGVLFHHY |
| 430 | 440 | 450 | 460 | 470 | |
| GFHETLYYTA | TFGVSRGLGP | LAQLIWDRAL | GLPIERPKSI | NLEGILKQVE | GQ |