Reviewed,
UniProtKB/Swiss-Prot Q2FF63 (THD1_STAA3)
Last modified
June 16, 2009.
Version 19.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Threonine dehydratase biosynthetic EC=4.3.1.19 Alternative name(s): Threonine deaminase | ||||
| Gene names |
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| Organism | Staphylococcus aureus (strain USA300) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 367830 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 422 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the formation of alpha-ketobutyrate from threonine in a two-step reaction. The first step is a dehydration of threonine, followed by rehydration and liberation of ammonia By similarity. |
| Catalytic activity | L-threonine = 2-oxobutanoate + NH3. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from L-threonine: step 1/1. |
| Sequence similarities | Belongs to the serine/threonine dehydratase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-threonine ammonia-lyase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete genome sequence of USA300, an epidemic clone of community-acquired meticillin-resistant Staphylococcus aureus." Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G., Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F., Perdreau-Remington F. Lancet 367:731-739(2006) [PubMed: 16517273] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000255 Genomic DNA. Translation: ABD20804.1. | |
| RefSeq | YP_494665.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3915391. |
| GenomeReviews | Gene locus SAUSA300_2014 in contig CP000255_GR. |
| KEGG | saa:SAUSA300_2014. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q2FF63. |
| OMA | Q2FF63. IFMPTTT. |
Family and domain databases | |
| InterPro | IPR001926. PyrdxlP-dep_enz_bsu. IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS. IPR001721. Thr_deHydtase_C. IPR011820. Threonine_deHydtase. [Graphical view] |
| Pfam | PF00291. PALP. 1 hit. PF00585. Thr_dehydrat_C. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02079. THD1. 1 hit. |
| PROSITE | PS00165. DEHYDRATASE_SER_THR. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | THD1_STAA3 | ||||||||
| Accession | Primary (citable) accession number: Q2FF63 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


