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O50660 (ALGL_AZOCH) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alginate lyase

EC=4.2.2.3
Alternative name(s):
Poly(beta-D-mannuronate) lyase
Poly(mana) alginate lyase
Gene names
Name:algL
OrganismAzotobacter chroococcum mcd 1
Taxonomic identifier355 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeAzotobacter

Protein attributes

Sequence length372 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Periplasm HAMAP MF_00557.

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 componentPeriplasm
   DomainSignal
   Molecular functionLyase
Gene Ontology (GO)
   Biological processalginic acid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpoly(beta-D-mannuronate) lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 372350Alginate lyase HAMAP MF_00557
PRO_0000024915

Sequences

Sequence LengthMass (Da)Tools
O50660 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 23F6D24181038B18

FASTA37241,321
        10         20         30         40         50         60 
MKTRLALPCL LGSLLLSSAV HAASALVPPK GYYAALEIRK GEAQACQAVP EPYTGELVFR 

        70         80         90        100        110        120 
SKYEGSDSAR STLNKKAEKA FRAKTKPITE IERGVSRMVM RYMEKGRLRR AGMRPGLLDA 

       130        140        150        160        170        180 
WAEDDALLST EYNHTGKSMR KWALGSLAGA YLRLKFSTSQ PLAAYPEQAK RIEAWFAKVG 

       190        200        210        220        230        240 
DQVIKDWSDL PLKQINNHSY WAAWSVMAAG VATNRRPLFD WAVEQFHIAA KQVDPRGFLA 

       250        260        270        280        290        300 
NELKRRQRAL AYHNYSLPPL MMIAAFAQAN GVDLRGDNDG ALGRLAGNVL AGVEDPEPFA 

       310        320        330        340        350        360 
ERAGEDQDME DLETDAKFSW LEPYCALYAC SPALRERKAE MGPFKNFRLG GDVTRIFDPQ 

       370 
EKPSKSTVGN AD 

« Hide

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

EMBL
GenBank
DDBJ
AJ223605 Genomic DNA. Translation: CAA11481.1.

3D structure databases

ProteinModelPortalO50660.
ModBaseSearch...

Protein family/group databases

CAZyPL5. Polysaccharide Lyase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA4.2.2.3. 617.

Family and domain databases

HAMAPMF_00557. Alginate_lyase.
[Tree]
InterProIPR022859. Alginate_lyase.
IPR008397. Alginate_lyase_dom.
IPR008929. Chondroitin_lyas.
[Graphical view]
Gene3DG3DSA:1.50.10.110. Alginate_lyase. 1 hit.
PfamPF05426. Alginate_lyase. 1 hit.
[Graphical view]
SUPFAMSSF48230. Chondroitin_lyas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALGL_AZOCH
AccessionPrimary (citable) accession number: O50660
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: September 21, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families