O50584 (LTAE_PSEUN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 46.
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: Low specificity L-threonine aldolase Short name=Low specificity L-TA EC=4.1.2.48 | ||||
| Gene names |
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| Organism | Pseudomonas sp. (strain NCIMB 10558) | ||||
| Taxonomic identifier | 268808 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 346 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. Can also act on L-erythro-phenylserine, L-threo-phenylserine, L-beta-3,4-methylenedioxyphenylserine and L-beta-3,4-dihydroxyphenylserine. |
| Catalytic activity | L-threonine = glycine + acetaldehyde. L-allo-threonine = glycine + acetaldehyde. |
| Cofactor | Pyridoxal phosphate. |
| Subunit structure | Homotetramer Probable. |
| Sequence similarities | Belongs to the threonine aldolase family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 8.0-8.5. Temperature dependence: Optimum temperature is 25 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro threonine aldolase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 346 | 346 | Low specificity L-threonine aldolase | PRO_0000121578 | |||||
Amino acid modifications | |||||||||
| Modified residue | 207 | 1 | N6-(pyridoxal phosphate)lysine Probable | ||||||
Experimental info | |||||||||
| Mutagenesis | 207 | 1 | K → A: Loss of activity. Ref.1 | ||||||
| Mutagenesis | 207 | 1 | K → R: 1000-fold decrease in activity. Ref.1 | ||||||
Sequences
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References
| [1] | "Gene cloning, nucleotide sequencing, and purification and characterization of the low-specificity L-threonine aldolase from Pseudomonas sp. strain NCIMB 10558." Liu J.-Q., Ito S., Dairi T., Itoh N., Kataoka M., Shimizu S., Yamada H. Appl. Environ. Microbiol. 64:549-554(1998) [PubMed: 9464392] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, MUTAGENESIS OF LYS-207, CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB001577 Genomic DNA. Translation: BAA24794.1. |
3D structure databases | |
| ProteinModelPortal | O50584. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001597. ArAA_b-elim_lyase/Thr_aldolase. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit. |
| Pfam | PF01212. Beta_elim_lyase. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LTAE_PSEUN | ||||||||
| Accession | Primary (citable) accession number: O50584 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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