Q29HB2 (MMSA_DROPS) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 42.
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 | Drosophila pseudoobscura pseudoobscura (Fruit fly) | ||
| Taxonomic identifier | 46245 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 520 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 Q02252 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. |
| Sequence caution | The sequence EAL31846.1 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | thymine metabolic process Inferred from sequence or structural similarity. Source: UniProtKB valine metabolic processInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | fatty-acyl-CoA binding Inferred from sequence or structural similarity. Source: UniProtKB malonate-semialdehyde dehydrogenase (acetylating) activityInferred from sequence or structural similarity. Source: UniProtKB methylmalonate-semialdehyde dehydrogenase (acylating) activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion Potential | |||||||
| Chain | ? – 520 | Probable methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial | PRO_0000312824 | ||||||
Regions | |||||||||
| Nucleotide binding | 195 – 199 | 5 | NAD Potential | ||||||
| Nucleotide binding | 247 – 252 | 6 | NAD Potential | ||||||
Sites | |||||||||
| Active site | 303 | 1 | Nucleophile By similarity UniProtKB Q02252 | ||||||
| Binding site | 403 | 1 | NAD Potential | ||||||
Sequences
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References
| [1] | "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution." Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L. Gibbs R.A.Genome Res. 15:1-18(2005) [PubMed: 15632085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MV2-25 / Tucson 14011-0121.94. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CH379064 Genomic DNA. Translation: EAL31846.1. Sequence problems. |
| RefSeq | XP_001354791.1. XM_001354755.1. |
3D structure databases | |
| ProteinModelPortal | Q29HB2. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4815188. |
| KEGG | dpo:Dpse_GA14712. |
Organism-specific databases | |
| FlyBase | FBgn0074739. Dpse\GA14712. |
Phylogenomic databases | |
| InParanoid | Q29HB2. |
| OMA | IISNVKP. |
| OrthoDB | EOG4N5TC3. |
| PhylomeDB | Q29HB2. |
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_DROPS | ||||||||
| Accession | Primary (citable) accession number: Q29HB2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| SIMILARITY comments Index of protein domains and families |

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