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Reviewed, UniProtKB/Swiss-Prot Q9L7P2 (ALGL_PSESY)

Last modified February 9, 2010. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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
OrganismPseudomonas syringae pv. syringae
Taxonomic identifier321 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae

Protein attributes

Sequence length378 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 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

Periplasm HAMAP MF_00557.

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 componentPeriplasm
   DomainSignal
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processalginic acid catabolic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpoly(beta-D-mannuronate) lyase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Ref.1
Chain29 – 378350Alginate lyase HAMAP MF_00557
PRO_0000024922

Experimental info

Mutagenesis2041H → A: Loss of activity. Ref.1
Mutagenesis2071W → A: Loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9L7P2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 33E5894BC6404F14

FASTA37842,542
        10         20         30         40         50         60 
MQTPKLIRPT LLSMAILSSM AWATGASAAL VPPKGYDAPI EKMKTGDHNF SCEAIPKPYT 

        70         80         90        100        110        120 
DKLVFRSKYE GSDKARATLN AVSEEAFRDA TKDITTLERG VSKVVMQYMR DGRPEQLDCA 

       130        140        150        160        170        180 
LNMMTTWAKA DALESREFNH TGKSMRKWAL GSMSSAYLRL KFSESHPLAN RQQDAKIIET 

       190        200        210        220        230        240 
WFSKLADQVV SDWSNLPLEK INNHSYWAAW SVMATAVATN RQDLFDWAVK EYKVAANQVD 

       250        260        270        280        290        300 
KDGFLPNEMK RRQRALSYHN YALPPLAMIA SFAQANGVDL RPENNGALKR LGDRVLAGVK 

       310        320        330        340        350        360 
DPSIFAEHNG EKQDMTDLKK DPKFAWLEPY CSLYTCSPDV LEEKHEKQPF KTFRLGGDLT 

       370 
KVYDPTHEKG DKGDNDGS 

« Hide

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

ModBaseSearch...

Protein family/group databases

CAZyPL5. Polysaccharide Lyase Family 5.

Family and domain databases

HAMAPMF_00557. Alginate_lyase.
[Tree]
InterProIPR008397. Alginate_lyase.
IPR008929. Chondroitin_lyas.
[Graphical view]
Gene3DG3DSA:1.50.10.110. Alginate_lyase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALGL_PSESY
AccessionPrimary (citable) accession number: Q9L7P2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: October 1, 2000
Last modified: February 9, 2010
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents