Q02253 (MMSA_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 114.
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: Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial Short name=MMSDH Short name=Malonate-semialdehyde dehydrogenase [acylating] EC=1.2.1.18 EC=1.2.1.27 Alternative name(s): Aldehyde dehydrogenase family 6 member A1 | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 535 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA. |
| Catalytic activity | 2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH. 3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Tissue specificity | Expressed in the head and flagellum of epididymal sperm but not in testicular sperm (at protein level). Kidney > liver > heart > muscle > brain. Ref.5 |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
| Mass spectrometry | Molecular mass is 57770.57 Da from positions 1 - 535. Determined by MALDI. Ref.5 |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | beta-alanine catabolic process Inferred from direct assay Ref.2. Source: RGD thymine catabolic processInferred from direct assay Ref.2. Source: RGD valine catabolic processInferred from direct assay Ref.2. Source: RGD |
| 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 direct assay Ref.2. Source: UniProtKB methylmalonate-semialdehyde dehydrogenase (acylating) activityInferred from direct assay Ref.2. Source: UniProtKB thiolester hydrolase activityInferred from direct assay PubMed 1540637. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 32 | 32 | Mitochondrion Ref.1 Ref.2 Ref.3 | ||||||
| Chain | 33 – 535 | 503 | Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial | PRO_0000007190 | |||||
Regions | |||||||||
| Nucleotide binding | 209 – 213 | 5 | NAD Potential | ||||||
| Nucleotide binding | 261 – 266 | 6 | NAD Potential | ||||||
Sites | |||||||||
| Active site | 317 | 1 | Nucleophile By similarity | ||||||
| Binding site | 417 | 1 | NAD Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 55 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 117 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 331 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 45 | 1 | D → N AA sequence Ref.1 | ||||||
| Sequence conflict | 50 | 1 | E → Q AA sequence Ref.1 | ||||||
| Sequence conflict | 166 | 1 | D → N AA sequence Ref.1 | ||||||
| Sequence conflict | 168 | 1 | D → N AA sequence Ref.1 | ||||||
| Sequence conflict | 184 | 1 | P → T AA sequence Ref.1 | ||||||
| Sequence conflict | 190 | 1 | M → G AA sequence Ref.1 | ||||||
Sequences
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References
| [1] | "CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution." Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W., Harris R.A. J. Biol. Chem. 267:19724-19729(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 33-50 AND 166-190. Tissue: Liver. |
| [2] | "Purification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase." Goodwin G.W., Rougraff P.M., Davis E.J., Harris R.A. J. Biol. Chem. 264:14965-14971(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-50, CHARACTERIZATION. |
| [3] | "The effect of ligand binding on the proteolytic pattern of methylmalonate semialdehyde dehydrogenase." Kedishvili N.Y., Popov K.M., Harris R.A. Arch. Biochem. Biophys. 290:21-26(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS. |
| [4] | Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 56-70, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord. |
| [5] | "Differential proteomics leads to identification of domain specific epididymal sperm proteins." Suryawanshi A.R., Khan S.A., Gajbhiye R.K., Gurav M.Y., Khole V.V. J. Androl. 32:240-259(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, MASS SPECTROMETRY. Strain: Holtzman. Tissue: Sperm. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M93401 mRNA. Translation: AAA41638.1. |
| IPI | IPI00205018. |
| PIR | A44097. |
| RefSeq | NP_112319.2. NM_031057.2. |
| UniGene | Rn.2098. |
3D structure databases | |
| ProteinModelPortal | Q02253. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q02253. 1 interaction. |
| STRING | 10116.ENSRNOP00000015545. |
Proteomic databases | |
| PaxDb | Q02253. |
| PRIDE | Q02253. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 81708. |
| KEGG | rno:81708. |
| UCSC | RGD:621556. rat. |
Organism-specific databases | |
| CTD | 4329. |
| RGD | 621556. Aldh6a1. |
Phylogenomic databases | |
| eggNOG | COG1012. |
| HOGENOM | HOG000271507. |
| HOVERGEN | HBG105023. |
| InParanoid | Q02253. |
| KO | K00140. |
| OrthoDB | EOG4HHP25. |
Enzyme and pathway databases | |
| SABIO-RK | Q02253. |
Gene expression databases | |
| Genevestigator | Q02253. |
| GermOnline | ENSRNOG00000011419. Rattus norvegicus. |
Family and domain databases | |
| Gene3D | 3.40.309.10. 1 hit. 3.40.605.10. 1 hit. |
| 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] |
| PANTHER | PTHR11699:SF27. PTHR11699:SF27. 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... |
Other | |
| NextBio | 615332. |
Entry information
| Entry name | MMSA_RAT | ||||||||
| Accession | Primary (citable) accession number: Q02253 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
