P50244
Gene name |
|
Protein name |
S-adenosylmethionine decarboxylase proenzyme |
Names |
AdoMetDC , SAMDC , EC 4.1.1.50 [Cleaved into: S-adenosylmethionine decarboxylase alpha chain; S-adenosylmethionine decarboxylase beta chain] |
Species |
Trypanosoma brucei brucei |
KEGG Pathway |
|
EC number |
4.1.1.50: Carboxy-lyases |
Protein Class |
S-ADENOSYLMETHIONINE DECARBOXYLASE (PTHR11570) |
Descriptions
S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) is a protein that catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine. Autoinhibition of AdoMetDC is mediated by the N-terminal sequence which blocks the active site, preventing the enzyme's catalytic activity. The relief of this autoinhibition involves heterodimerization with a catalytically dead paralog (proenzyme), resulting in conformational changes that displace the inhibitory N-terminal sequence from the active site, thereby activating the enzyme.
Autoinhibitory domains (AIDs)
Target domain |
86-370 (S-adenosylmethionine decarboxylase alpha chain, specifically, 202-247 active site helices/strands) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P50244
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P50244-F1 | Predicted | AlphaFoldDB |
No variants for P50244
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P50244 | |||||
No associated diseases with P50244
1 regional properties for P50244
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | S-adenosylmethionine decarboxylase, conserved site | 80 - 90 | IPR018166 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.1.50 | Carboxy-lyases |
| Subcellular Localization |
|
|
| PANTHER Family | PTHR11570 | S-ADENOSYLMETHIONINE DECARBOXYLASE |
| PANTHER Subfamily | PTHR11570:SF0 | S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME |
| PANTHER Protein Class |
decarboxylase
lyase |
|
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| catalytic complex | A protein complex which is capable of catalytic activity. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| adenosylmethionine decarboxylase activity | Catalysis of the reaction |
| protein heterodimerization activity | Binding to a nonidentical protein to form a heterodimer. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of spermidine biosynthetic process | Any process that activates or increases the frequency, rate or extent of spermidine biosynthetic process. |
| positive regulation of trypanothione biosynthetic process | Any process that activates or increases the frequency, rate or extent of trypanothione biosynthetic process. |
| S-adenosylmethioninamine metabolic process | The chemical reactions and pathways involving S-adenosylmethioninamine, (5-deoxy-5-adenosyl)(3-aminopropyl) methylsulfonium salt. |
| S-adenosylmethionine metabolic process | The chemical reactions and pathways involving S-adenosylmethionine, S-(5'-adenosyl)-L-methionine, an important intermediate in one-carbon metabolism. |
| spermidine biosynthetic process | The chemical reactions and pathways resulting in the formation of spermidine, N-(3-aminopropyl)-1,4-diaminobutane. |
| spermine biosynthetic process | The chemical reactions and pathways resulting in the formation of spermine, a polybasic amine found in human sperm, in ribosomes and in some viruses and involved in nucleic acid packaging. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSSCKDSLSL | MAMWGSIARF | DPKHERSFEG | PEKRLEVIMR | VVDGTHVSGL | LAHDDDVWQK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VIDAICAHIV | SREFNEYIRS | YVLSESSLFV | MKDRVILITC | GTITLLNCVP | LICEAVSTVC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GEVEWVSFMH | KNYSFPWEQK | GPHLSMAEEF | KTLRSHFPSG | QPFIFGPIDS | DHYFLYFHSD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VVQPSCSDDA | QLSMTMYGLD | RNQTKHWYSD | KMLPTGPETA | VIREATGLSE | VVDDSWILHD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LQYEPCGYSI | NAIRGSEYQT | IHITPEEHCS | FASYETNTCA | LNYSKCICGV | LRVFDPERFS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VIVFIDPDSA | VGKSYHSGGT | IGVEPEYYPN | YEAHHRTVNE | YTPGHWVLKV | NYVKRAVGTV |
| GTSAASGAKE |