Q7QC84 (MMSA_ANOGA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 65.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial Short name=MMSDH Short name=Malonate-semialdehyde dehydrogenase [acylating] EC=1.2.1.18 EC=1.2.1.27 | ||
| Gene names |
| ||
| Organism | Anopheles gambiae (African malaria mosquito) | ||
| Taxonomic identifier | 7165 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles |
Protein attributes
| Sequence length | 521 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA By similarity. UniProtKB Q02252 |
| Catalytic activity | 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH. UniProtKB P42412 3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H. UniProtKB Q02252 |
| Subunit structure | Homotetramer By similarity. UniProtKB Q02252 |
| Subcellular location | Mitochondrion By similarity UniProtKB Q02252. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | malonate-semialdehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: EC methylmalonate-semialdehyde dehydrogenase (acylating) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 521 | Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial | PRO_0000043372 | ||||||
Regions | |||||||||
| Nucleotide binding | 196 – 200 | 5 | NAD Potential | ||||||
| Nucleotide binding | 248 – 253 | 6 | NAD Potential | ||||||
Sites | |||||||||
| Active site | 304 | 1 | Nucleophile By similarity UniProtKB Q02252 | ||||||
| Binding site | 404 | 1 | NAD Potential | ||||||
Sequences
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References
| [1] | "The genome sequence of the malaria mosquito Anopheles gambiae." Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. Hoffman S.L.Science 298:129-149(2002) [PubMed: 12364791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PEST. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AAAB01008859 Genomic DNA. Translation: EAA07972.4. |
| RefSeq | XP_312441.4. XM_312441.5. |
3D structure databases | |
| ProteinModelPortal | Q7QC84. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q7QC84. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | AGAP002499-RA; AGAP002499-PA; AGAP002499. |
| GeneID | 1273463. |
| KEGG | aga:AgaP_AGAP002499. |
| VectorBase | AGAP002499. Anopheles gambiae. |
Organism-specific databases | |
| CTD | 1273463. |
Phylogenomic databases | |
| eggNOG | inNOG06001. |
| GeneTree | EMGT00050000005689. |
| HOGENOM | HBG752218. |
| InParanoid | Q7QC84. |
| OMA | IISNVKP. |
| OrthoDB | EOG4N5TC3. |
| PhylomeDB | Q7QC84. |
Family and domain databases | |
| InterPro | IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR010061. MeMal-semiAld_DH. [Graphical view] |
| Gene3D | G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit. |
| KO | K00140. |
| PANTHER | PTHR11699:SF27. MMSDH. 1 hit. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR01722. MMSDH. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MMSA_ANOGA | ||||||||
| Accession | Primary (citable) accession number: Q7QC84 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with