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Q06749 (ALGL_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. 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
Ordered Locus Names:PA3547
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Depolymerizes alginate by cleaving the beta-1,4 glycosidic bond. May enhance the production of alginate by controlling the length of the polymer chain during export. 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

Subcellular location

Periplasm HAMAP MF_00557.

Sequence similarities

Belongs to the polysaccharide lyase 5 family.

Ontologies

Keywords
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
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 – 2727 Potential
Chain28 – 367340Alginate lyase HAMAP MF_00557
PRO_0000024918

Experimental info

Sequence conflict2691A → P in AAA71990. Ref.1
Sequence conflict337 – 3415KMLEA → NACSRP in AAA71990. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q06749 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: EAA3FE30032AB3BA

FASTA36740,829
        10         20         30         40         50         60 
MKTSHLIRIA LPGALAAALL ASQVSQAADL VPPPGYYAAV GERKGSAGSC PAVPPPYTGS 

        70         80         90        100        110        120 
LVFTSKYEGS DSARATLNVK AEKTFRSQIK DITDMERGAT KLVTQYMRSG RDGDLACALN 

       130        140        150        160        170        180 
WMSAWARAGA LQSDDFNHTG KSMRKWALGS LSGAYMRLKF SSSRPLAAHA EQSREIEDWF 

       190        200        210        220        230        240 
ARLGTQVVRD WSGLPLKKIN NHSYWAAWSV MSTAVVTNRR DLFDWAVSEF KVAANQVDEQ 

       250        260        270        280        290        300 
GFLPNELKRR QRALAYHNYA LPPLAMIAAF AQVNGVDLRQ ENHGALQRLA ERVMKGVDDE 

       310        320        330        340        350        360 
ETFEEKTGED QDMTDLKVDN KYAWLEPYCA LYRCEPKMLE AKKDREPFNS FRLGGEVTRV 


FSREGGS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the algL gene of Pseudomonas aeruginosa and purification of its alginate lyase product."
Boyd A., Ghosh M., May T.B., Shinabarger D., Keogh R., Chakrabarty A.M.
Gene 131:1-8(1993) [PubMed: 8370530] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of the Pseudomonas aeruginosa alginate lyase gene (algL): cloning, sequencing, and expression in Escherichia coli."
Schiller N.L., Monday S.R., Boyd C.M., Keen N.T., Ohman D.E.
J. Bacteriol. 175:4780-4789(1993) [PubMed: 8335634] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FRD1.
[3]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed: 10984043] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14597 Unassigned DNA. Translation: AAA71990.1.
U27829 Genomic DNA. Translation: AAA91127.1.
AE004091 Genomic DNA. Translation: AAG06935.1.
PIRH83202.
JN0777.
RefSeqNP_252237.1. NC_002516.2.

3D structure databases

ProteinModelPortalQ06749.
ModBaseSearch...

Protein family/group databases

CAZyPL5. Polysaccharide Lyase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID878552.
GenomeReviewsGene locus PA3547 in contig AE004091_GR.
KEGGpae:PA3547.
PATRIC19841707. VBIPseAer58763_3711.

Organism-specific databases

PseudoCAPPA3547.

Phylogenomic databases

HOGENOMHBG336064.
OMAAAWSVMA.
ProtClustDBPRK00325.

Enzyme and pathway databases

BioCycPAER208964:PA3547-MONOMER.
BRENDA4.2.2.3. 5087.

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.
KOK01729.
PfamPF05426. Alginate_lyase. 1 hit.
[Graphical view]
SUPFAMSSF48230. Chondroitin_lyas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALGL_PSEAE
AccessionPrimary (citable) accession number: Q06749
Secondary accession number(s): Q57292
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: December 15, 1998
Last modified: January 25, 2012
This is version 76 of the entry and version 2 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