Q6A2H0 (SSDH_PANTR) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 58.
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: Succinate-semialdehyde dehydrogenase, mitochondrial EC=1.2.1.24 Alternative name(s): Aldehyde dehydrogenase family 5 member A1 NAD(+)-dependent succinic semialdehyde dehydrogenase | ||
| Gene names |
| ||
| Organism | Pan troglodytes (Chimpanzee) | ||
| Taxonomic identifier | 9598 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pan |
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 transcript level |
General annotation (Comments)
| Function | Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) By similarity. |
| Catalytic activity | Succinate semialdehyde + NAD+ + H2O = succinate + NADH. |
| Enzyme regulation | Redox-regulated. Inhibited under oxydizing conditions By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Mitochondrion By similarity. |
| Sequence similarities | Belongs to the aldehyde dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Disulfide bond |
| Gene Ontology (GO) | |
| Biological process | central nervous system development Inferred from sequence or structural similarity. Source: UniProtKB gamma-aminobutyric acid catabolic processInferred from sequence or structural similarity. Source: UniProtKB protein homotetramerizationInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fractionInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | succinate-semialdehyde dehydrogenase activity Inferred 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 – 47 | 47 | Mitochondrion Potential | ||||||||
| Chain | 48 – 535 | 488 | Succinate-semialdehyde dehydrogenase, mitochondrial | PRO_0000007186 | |||||||
Regions | |||||||||||
| Nucleotide binding | 228 – 231 | 4 | NAD By similarity | ||||||||
| Nucleotide binding | 284 – 289 | 6 | NAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 306 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 340 | 1 | Nucleophile By similarity | ||||||||
| Binding site | 213 | 1 | NAD By similarity | ||||||||
| Binding site | 213 | 1 | Substrate By similarity | ||||||||
| Binding site | 334 | 1 | Substrate By similarity | ||||||||
| Binding site | 498 | 1 | Substrate By similarity | ||||||||
| Site | 205 | 1 | Transition state stabilizer By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 126 | 1 | N6-acetyllysine By similarity | ||||||||
| Modified residue | 358 | 1 | N6-acetyllysine By similarity | ||||||||
| Disulfide bond | 340 ↔ 342 | In inhibited form By similarity | |||||||||
Sequences
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References
| [1] | "Comparative analysis of succinic semialdehyde dehydrogenase in non three ape species." Blasi P., Malaspina P. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ621752 mRNA. Translation: CAF21869.1. |
| RefSeq | NP_001008991.1. NM_001008991.1. |
| UniGene | Ptr.6190. |
3D structure databases | |
| ProteinModelPortal | Q6A2H0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6A2H0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 449515. |
| KEGG | ptr:449515. |
Organism-specific databases | |
| CTD | 7915. |
Phylogenomic databases | |
| eggNOG | prNOG06436. |
| GeneTree | ENSGT00550000075018. |
| HOVERGEN | HBG108515. |
Enzyme and pathway databases | |
| BRENDA | 1.2.1.24. 4497. |
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. IPR010102. Succ_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 | K00139. |
| Pfam | PF00171. Aldedh. 1 hit. [Graphical view] |
| SUPFAM | SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit. |
| TIGRFAMs | TIGR01780. SSADH. 1 hit. |
| PROSITE | PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SSDH_PANTR | ||||||||
| Accession | Primary (citable) accession number: Q6A2H0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with