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Q59478 (ALYA_KLEPN) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 50. 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:alyA
OrganismKlebsiella pneumoniae
Taxonomic identifier573 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length307 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades alginates that contain guluronic acid.

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.

Subcellular location

Secreted.

Sequence similarities

Belongs to the polysaccharide lyase 7 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

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 – 2020 Ref.1
Chain21 – 307287Alginate lyase
PRO_0000024925

Sequences

Sequence LengthMass (Da)Tools
Q59478 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 76A1F9AAE082632E

FASTA30733,512
        10         20         30         40         50         60 
MLKSGVMVAS LCLFSVPSRA AVPAPGDKFE LSGWSLSVPV DSDNDGKADQ IKEKTLAAGY 

        70         80         90        100        110        120 
RNSDFFTLSD AGGMVFKAPI SGAKTSKNTT YTRSELREML RKGDTSIATQ GVSRNNWVLS 

       130        140        150        160        170        180 
SAPLSEQKKA GGVDGTLEAT LSVDHVTTTG VNWQVGRVII GQIHANNDEP IRLYYRKLPH 

       190        200        210        220        230        240 
HQKGSVYFAH EPRKGFGDEQ WYEMIGTLQP SHGNQTAAPT EPEAGIALGE TFSYRIDATG 

       250        260        270        280        290        300 
NKLTVTLMRE GRPDVVKTVD MSKSGYSEAG QYLYFKAGVY NQNKTGKPDD YVQATFYRLK 


ATHGAQR 

« Hide

References

[1]"Alginate lyase from Klebsiella pneumoniae, subsp. aerogenes: gene cloning, sequence analysis and high-level production in Escherichia coli."
Baron A.J., Wong T.Y., Hicks S.J., Gacesa P., Willcock D., McPherson M.J.
Gene 143:61-66(1994) [PubMed: 8200539] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-51.
Strain: Subsp. aerogenes 25.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19657 Genomic DNA. Translation: AAA25049.1.

3D structure databases

ProteinModelPortalQ59478.
ModBaseSearch...

Protein family/group databases

CAZyPL7. Polysaccharide Lyase Family 7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR014895. Alginate_lyase_2.
IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PfamPF08787. Alginate_lyase2. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALYA_KLEPN
AccessionPrimary (citable) accession number: Q59478
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: September 21, 2011
This is version 50 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