Reviewed,
UniProtKB/Swiss-Prot O50660 (ALGL_AZOCH)
Last modified
November 25, 2008.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Alginate lyase EC=4.2.2.3 Alternative name(s): Poly(beta-D-mannuronate) lyase Poly(mana) alginate lyase | ||
| Gene names |
| ||
| Organism | Azotobacter chroococcum mcd 1 | ||
| Taxonomic identifier | 355 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Azotobacter |
Protein attributes
| Sequence length | 372 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)
| Function | Depolymerizes alginate by cleaving the beta-1,4 glycosidic bond. Degrades deacetylated polymannuronate alginate more efficiently than non-deacetylated polyM. Is able to degrade its own alginate, but at a lower efficiency than that produced from M.pyriferia and P.aeruginosa. HAMAP MF_00557 |
| Catalytic activity | Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends. HAMAP MF_00557 |
| Enzyme regulation | Monovalent cations such as potassium and sodium enhance activity, as well as a combined action of these cations with magnesium. However, other cations like calcium, cobalt, manganese and zinc, or the presence of EDTA, do not affect the enzymatic activity. HAMAP MF_00557 |
| Subcellular location | |
| Sequence similarities | Belongs to the polysaccharide lyase 5 family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 7.5. HAMAP MF_00557 Temperature dependence: Optimum temperature is 30 degrees Celsius. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Molecular function | Lyase |
Gene Ontology (GO) | |
| Biological process | alginic acid catabolic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: InterPro |
| Molecular function | poly(beta-D-mannuronate) lyase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | |||||
| Chain | 23 – 372 | 350 | Alginate lyase HAMAP MF_00557 | PRO_0000024915 | ||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and expression of the algL gene, encoding the Azotobacter chroococcum alginate lyase: purification and characterization of the enzyme." Pecina A., Pascual A., Paneque A. J. Bacteriol. 181:1409-1414(1999) [PubMed: 10049370] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 4412 / NCIB 8003 / X-50. |
Cross-references
Sequence databases | |
|---|---|
| AJ223605 Genomic DNA. Translation: CAA11481.1. | |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| HAMAP | MF_00557. [Tree] |
| InterPro | IPR008397. Alginate_lyase. [Graphical view] |
| Gene3D | G3DSA:1.50.10.110. Alginate_lyase. 1 hit. |
| Pfam | PF05426. Alginate_lyase. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ALGL_AZOCH | ||||||||
| Accession | Primary (citable) accession number: O50660 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


