Reviewed,
UniProtKB/Swiss-Prot Q0VCW4 (SDHL_BOVIN)
Last modified
January 19, 2010.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-serine dehydratase/L-threonine deaminase EC=4.3.1.17 Alternative name(s): L-serine deaminase SDH L-threonine dehydratase EC=4.3.1.19 TDH | ||||
| Gene names |
| ||||
| Organism | Bos taurus (Bovine) | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Catalytic activity | L-serine = pyruvate + NH3. L-threonine = 2-oxobutanoate + NH3. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the serine/threonine dehydratase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Gluconeogenesis |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Gene Ontology (GO) | |
| Biological process | L-serine catabolic process Inferred from sequence or structural similarity. Source: UniProtKB gluconeogenesisInferred from electronic annotation. Source: UniProtKB-KW pyruvate biosynthetic processInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | L-serine ammonia-lyase activity Inferred from sequence or structural similarity. Source: UniProtKB L-threonine ammonia-lyase activityInferred from electronic annotation. Source: EC protein homodimerization activityInferred from sequence or structural similarity. Source: UniProtKB pyridoxal phosphate bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Thalamus. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC119966 mRNA. Translation: AAI19967.1. |
| IPI | IPI00707557. |
| RefSeq | NP_001069130.1. |
| UniGene | Bt.5878 |
3D structure databases | |
| SMR | Q0VCW4. Positions 1-325. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0VCW4. |
Genome annotation databases | |
| Ensembl | ENSBTAT00000045109; ENSBTAP00000042524; ENSBTAG00000031814; Bos taurus. [Genome view] |
| GeneID | 514346. |
| KEGG | bta:514346. |
Organism-specific databases | |
| CTD | 514346. |
Phylogenomic databases | |
| eggNOG | maNOG17826. |
| HOVERGEN | Q0VCW4. |
| InParanoid | Q0VCW4. |
| PhylomeDB | Q0VCW4. |
Enzyme and pathway databases | |
| BRENDA | 4.3.1.17. 251. |
Family and domain databases | |
| InterPro | IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. [Graphical view] |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| PROSITE | PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SDHL_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q0VCW4 | ||||||||
| Entry history |
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| 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


