Reviewed,
UniProtKB/Swiss-Prot Q8MIR0 (TDH_PIG)
Last modified
January 19, 2010.
Version 30.
History...
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90%,
50% identity |
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: L-threonine 3-dehydrogenase, mitochondrial EC=1.1.1.103 | ||
| Gene names |
| ||
| Organism | Sus scrofa (Pig) | ||
| Taxonomic identifier | 9823 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus |
Protein attributes
| Sequence length | 373 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)
| Catalytic activity | L-threonine + NAD+ = L-2-amino-3-oxobutanoate + NADH. Ref.2 |
| Pathway | |
| Subcellular location | |
| Sequence similarities | Belongs to the sugar epimerase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellular metabolic process Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | L-threonine 3-dehydrogenase activity Inferred from electronic annotation. Source: EC coenzyme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion | |||||||
| Chain | ? – 373 | L-threonine 3-dehydrogenase, mitochondrial | PRO_0000298785 | ||||||
Regions | |||||||||
| Nucleotide binding | 9 – 46 | 38 | NAD By similarity UniProtKB Q8R059 | ||||||
Sites | |||||||||
| Active site | 195 | 1 | Proton acceptor By similarity UniProtKB Q8R059 | ||||||
Experimental info | |||||||||
| Sequence conflict | 65 | 1 | G → Q AA sequence Ref.2 | ||||||
| Sequence conflict | 309 | 1 | K → R AA sequence Ref.2 | ||||||
| Sequence conflict | 331 | 1 | W → I AA sequence Ref.2 | ||||||
| Sequence conflict | 341 | 1 | R → A AA sequence Ref.2 | ||||||
Sequences
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References
| [1] | "Molecular cloning and tissue distribution of mammalian L-threonine 3-dehydrogenases." Edgar A.J. BMC Biochem. 3:19-19(2002) [PubMed: 12097150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Purification and structural characterization of porcine L-threonine dehydrogenase." Kao Y.-C., Davis L. Protein Expr. Purif. 5:423-431(1994) [PubMed: 7827500] [Abstract] Cited for: PROTEIN SEQUENCE OF 51-111; 145-180; 200-218; 222-249 AND 274-342, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY095535 mRNA. Translation: AAM18208.1. |
| RefSeq | NP_999169.1. |
| UniGene | Ssc.51 |
3D structure databases | |
| SMR | Q8MIR0. Positions 55-362. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 397065. |
| KEGG | ssc:397065. |
Organism-specific databases | |
| CTD | 397065. |
Phylogenomic databases | |
| HOVERGEN | Q8MIR0. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.103. 249. |
Family and domain databases | |
| InterPro | IPR001509. Epimerase_deHydtase. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01370. Epimerase. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TDH_PIG | ||||||||
| Accession | Primary (citable) accession number: Q8MIR0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


