P52713
Gene name |
alh-8 (F13D12.4) |
Protein name |
Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial |
Names |
MMSDH, Malonate-semialdehyde dehydrogenase [acylating] |
Species |
Caenorhabditis elegans |
KEGG Pathway |
cel:CELE_F13D12.4 |
EC number |
1.2.1.27: With NAD(+) or NADP(+) as acceptor |
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 P52713
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P52713-F1 | Predicted | AlphaFoldDB |
No variants for P52713
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P52713 | |||||
No associated diseases with P52713
Functions
| Description | ||
|---|---|---|
| EC Number | 1.2.1.27 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| fatty-acyl-CoA binding | Binding to a fatty-acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group. |
| malonate-semialdehyde dehydrogenase (acetylating) activity | Catalysis of the reaction: 3-oxopropanoate + CoA + NADP+ = acetyl-CoA + CO2 + NADPH + H+. |
| malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity | Catalysis of the reaction: 3-oxopropanoate + coenzyme A(4-) + NAD(1-) <=> acetyl-CoA(4-) + carbon dioxide + NADH(2-). |
| methylmalonate-semialdehyde dehydrogenase (acylating) activity | Catalysis of the reaction: 2-methyl-3-oxopropanoate + CoA + NAD+ = propanoyl-CoA + CO2 + NADH + H+. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| thymine catabolic process | The chemical reactions and pathways resulting in the breakdown of thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base. |
| thymine metabolic process | The chemical reactions and pathways involving thymine, 5-methyluracil, one of the two major pyrimidine bases present (as thymidine) in DNA but not found in RNA other than (as ribothymidine) in transfer RNA, where it is a minor base. |
| valine catabolic process | The chemical reactions and pathways resulting in the breakdown of valine, 2-amino-3-methylbutanoic acid. |
| valine metabolic process | The chemical reactions and pathways involving valine, 2-amino-3-methylbutanoic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLSRLARVQP | KCQQLAHFST | SKSAAAAPTV | KLWIDGQAVE | SKTTDFVELT | NPATNEVIAM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VPNATQAEMQ | AAVDSAKNAF | NTWKNTSPLT | RQQCMFKLQA | LIKRDMKKLA | ESITIEQGKT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LPDAEGDVSR | GLQVVEHACS | VPSLMMGETL | PNVSRDMDTH | SYRIPLGVTA | GICPFNFPAM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IPLWMFPVAL | ATGNTMVIKP | SEQDPGAAQL | LVELAKEAGV | PDGCVNIIHG | QHSAVNFICD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NPDIKAISFV | GGDAAGKHIY | ERGAKNGKRV | QSNMGAKNHG | VIMADANKEQ | TLNQLTAAAF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GAAGQRCMAL | TTAVLVGEAR | AWLPELVEKA | KNLKVNAGWK | PDTDIGPLIS | KQSKARVLRL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IESAKKEGAQ | VPLDGSNITV | PGFENGNFVG | PTILAGVKPN | MTCYREEIFG | PVLVVMEAEN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LNEAIEIINN | NPYGNGTAIF | TSNGATARKF | TNEVDVGQIG | INVPIPVPLP | MFSFTGSRGS |
| 490 | 500 | 510 | 520 | ||
| FLGDLNFYGK | AGIQFYTQWK | TVTQYWNESL | TELKPQMSFP | QLK |