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Q01172 (PELA_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Pectin lyase A

Short name=PLA
EC=4.2.2.10
Alternative name(s):
Pectin lyase II
Short name=PLII
Gene names
Name:pelA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length379 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pectinolytic enzymes 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.

Catalytic activity

Eliminative cleavage of (1->4)-alpha-D-galacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.

Subcellular location

Secreted Probable.

Post-translational modification

N-glycosylated at Asn-129 and O-glycosylated at Thr-88 when expressed in Aspergillus nidulans. The protein from strain 4M-147 is O-glycosylated at Thr-88 and Ser-368. Ref.3 modeled GalNAc at the O-glycosylation site, a glycosylation not observed in fungi. The O-linked saccharide is probably mannose.

Sequence similarities

Belongs to the polysaccharide lyase 1 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cell wall biogenesis/degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionLyase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpectin lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1
Chain21 – 379359Pectin lyase A
PRO_0000024896

Sites

Active site2561 Potential

Amino acid modifications

Glycosylation881O-linked (Man)
Glycosylation1291N-linked (GlcNAc...) Probable
Glycosylation3681O-linked (Man); in strain 4M-147
Disulfide bond83 ↔ 102
Disulfide bond92 ↔ 226
Disulfide bond322 ↔ 330

Natural variations

Natural variant321E → K in strain: 4M-147. Ref.3
Natural variant391D → S in strain: 4M-147. Ref.3
Natural variant1211V → T in strain: 4M-147. Ref.3
Natural variant2331G → A in strain: 4M-147. Ref.3
Natural variant2681C → A in strain: 4M-147. Ref.3
Natural variant2731F → W in strain: 4M-147. Ref.3
Natural variant3091A → E in strain: 4M-147. Ref.3
Natural variant3161T → S in strain: 4M-147. Ref.3
Natural variant3371C → S in strain: 4M-147. Ref.3

Secondary structure

............................................................................. 379
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01172 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 4DF1326BFFCA77B5

FASTA37939,855
        10         20         30         40         50         60 
MKYSTIFSAA AAVFAGSAAA VGVSGSAEGF AEGVTGGGDA TPVYPDTIDE LVSYLGDDEA 

        70         80         90        100        110        120 
RVIVLTKTFD FTDSEGTTTG TGCAPWGTAS ACQVAIDQDD WCENYEPDAP SVSVEYYNAG 

       130        140        150        160        170        180 
VLGITVTSNK SLIGEGSSGA IKGKGLRIVS GAENIIIQNI AVTDINPKYV WGGDAITLDD 

       190        200        210        220        230        240 
CDLVWIDHVT TARIGRQHYV LGTSADNRVS LTNNYIDGVS DYSATCDGYH YWGIYLDGDA 

       250        260        270        280        290        300 
DLVTMKGNYI YHTSGRSPKV QDNTLLHCVN NYFYDISGHA FEIGEGGYVL AEGNVFQNVD 

       310        320        330        340        350        360 
TVLETYEGAA FTVPSTTAGE VCSTYLGRDC VINGFGCSGT FSEDSTSFLS DFEGKNIASA 

       370 
SAYTSVASRV VANAGQGNL 

« Hide

References

[1]"Structure of the Aspergillus niger pelA gene and its expression in Aspergillus niger and Aspergillus nidulans."
Kusters-Van Someren M.A., Harmsen J.A.M., Kester H.C.M., Visser J.
Curr. Genet. 20:293-299(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 21-40 AND 115-125.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]"Cloning and expression of a second Aspergillus niger pectin lyase gene (pelA): indications of a pectin lyase gene family in A. niger."
Harmsen J.A.M., Kurster-Van Sommeren M.A., Visser J.
Curr. Genet. 18:161-166(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[3]"Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases."
Mayans O., Scott M., Connerton I., Gravesen T., Benen J., Visser J., Pickersgill R., Jenkins J.
Structure 5:677-689(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-379 FOR STRAIN N400, X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 21-379 FOR STRAIN 4M-147, VARIANTS LYS-32; SER-39; THR-121; ALA-233; ALA-268; TRP-273; GLU-309; SER-316 AND SER-337.
Strain: 4M-147 and ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60724 Genomic DNA. Translation: CAA43130.1.
X55784 Genomic DNA. Translation: CAA39305.1.
PIRS17979.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IDJX-ray2.40A/B21-379[»]
1IDKX-ray1.93A21-379[»]
ProteinModelPortalQ01172.
SMRQ01172. Positions 21-379.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyPL1. Polysaccharide Lyase Family 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG306793.

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...

Other

EvolutionaryTraceQ01172.

Entry information

Entry namePELA_ASPNG
AccessionPrimary (citable) accession number: Q01172
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 13, 2013
This is version 90 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references