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Q9C2Z0 (PLYA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pectate lyase A

EC=4.2.2.2
Gene names
Name:plyA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester. Ref.1

Catalytic activity

Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Cofactor

Binds 1 calcium ion per subunit. Ref.1

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the polysaccharide lyase 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionLyase
   PTMGlycoprotein
Gene Ontology (GO)
   Biological_processpectin catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

pectate lyase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131
Chain32 – 323292Pectate lyase A
PRO_5000066020

Sites

Active site2221 Potential
Metal binding1361Calcium By similarity
Metal binding1651Calcium By similarity
Metal binding1691Calcium By similarity

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9C2Z0 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E7F438D307B816F2

FASTA32334,369
        10         20         30         40         50         60 
MTNFKWIVAA AGLLFGQVLA APTATSTHAK RATVSDAAFG YASLNGGTTG GAGGTTTTVS 

        70         80         90        100        110        120 
SYAAFTSAVS GDDAKVVYVD GTIKQTADQV KIGSNTSIIG KDANAILEGF GVLVKEKENV 

       130        140        150        160        170        180 
IIRNLGVSKV LADNGDAIGV QYSNNVWIDH CDVSSDRDHD KDYYDGLIDI THGSDYVTVS 

       190        200        210        220        230        240 
NTFIHDHWKA SLVGHSDSNE DEDSGHLTVT YANNYWYNVN SRAPSFRFGT GHVYNSYYLD 

       250        260        270        280        290        300 
VSDGINTRDG AQLLVESNQF VDSKKALYST DDGYAVSNDN DFGDSENTAE EGTLTSMPYD 

       310        320 
YTLLGSANVK AAVVGTAGQT LTF 

« Hide

References

[1]"Characterization of Aspergillus niger pectate lyase A."
Benen J.A., Kester H.C., Parenicova L., Visser J.
Biochemistry 39:15563-15569(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], GLYCOSYLATION, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ276331 Genomic DNA. Translation: CAC33162.1.

3D structure databases

ProteinModelPortalQ9C2Z0.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG3866.

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR002022. Amb_allergen_dom.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamPF00544. Pec_lyase_C. 1 hit.
[Graphical view]
SMARTSM00656. Amb_all. 1 hit.
[Graphical view]
SUPFAMSSF51126. SSF51126. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLYA_ASPNG
AccessionPrimary (citable) accession number: Q9C2Z0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 1, 2001
Last modified: November 13, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families