Reviewed,
UniProtKB/Swiss-Prot Q9L7P2 (ALGL_PSESY)
Last modified
February 9, 2010.
Version 45.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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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 |
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| Organism | Pseudomonas syringae pv. syringae | ||
| Taxonomic identifier | 321 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas syringae |
Protein attributes
| Sequence length | 378 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 from P.aeruginosa more efficiently than non-deacetylated polyM. AlgL from P.syringae degrades also its own alginate, which may indicate a role in cleaving preformed alginate and/or in determining the length of the alginate polymer. 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 | The monovalent cation sodium enhances activity but is not absolutely required. HAMAP MF_00557 |
| Subcellular location | |
| Sequence similarities | Belongs to the polysaccharide lyase 5 family. |
| Biophysicochemical properties | pH dependence: Optimum pH is 7.0. HAMAP MF_00557 Temperature dependence: Optimum temperature is 42 degrees Celsius. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Molecular function | Lyase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | alginic acid catabolic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | poly(beta-D-mannuronate) lyase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Characterization of alginate lyase from Pseudomonas syringae pv. syringae." Preston L.A., Wong T.Y., Bender C.L., Schiller N.L. J. Bacteriol. 182:6268-6271(2000) [PubMed: 11029455] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-38, MUTAGENESIS OF HIS-204 AND TRP-207. Strain: FF5. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF222020 Genomic DNA. Translation: AAF32371.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | PL5. Polysaccharide Lyase Family 5. |
Family and domain databases | |
| HAMAP | MF_00557. Alginate_lyase. [Tree] |
| InterPro | IPR008397. Alginate_lyase. IPR008929. Chondroitin_lyas. [Graphical view] |
| Gene3D | G3DSA:1.50.10.110. Alginate_lyase. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ALGL_PSESY | ||||||||
| Accession | Primary (citable) accession number: Q9L7P2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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