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Reviewed, UniProtKB/Swiss-Prot Q12554 (PGLR3_ASPNG)

Last modified June 16, 2009. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Polygalacturonase-3
    EC=3.2.1.15
Alternative name(s):
    Polygalacturonase III
      Short name=PG-III
      Short name=PGC
    Pectinase-3
Gene names
Name: pgaC
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length383 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

Random hydrolysis of (1->4)-alpha-D-galactosiduronic linkages in pectate and other galacturonans.

Subcellular location

Secreted Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 28 family.

Contains 4 PbH1 repeats.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cell wall organization

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpolygalacturonase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Propeptide17 – 4024 Potential
PRO_0000024772
Chain41 – 383343Polygalacturonase-3
PRO_0000024773

Sites

Active site2211Proton donor By similarity
Active site2431 By similarity

Amino acid modifications

Glycosylation2601N-linked (GlcNAc...) Potential
Disulfide bond44 ↔ 62 By similarity
Disulfide bond223 ↔ 239 By similarity
Disulfide bond348 ↔ 353 By similarity
Disulfide bond372 ↔ 381 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12554-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D6A4ED2149FC7A3A

FASTA38340,502
        10         20         30         40         50         60 
MVRQLILISS LLAAVAVRAP ADPAHPMVTE APDVNLVEKR ATTCTFSGSE GASKASKSKT 

        70         80         90        100        110        120 
SCSTIYLSDV AVPSGTTLDL SDLNDGTHVI FQGETTFGYE EWEGPLVRVS GTDITVEGES 

       130        140        150        160        170        180 
DAVLNGDGSR WWDGEGGNGG KTKPKFFYAH DLTSSTIKSI YIENSPVQVF SIDGSTDLTM 

       190        200        210        220        230        240 
TDITVDNTDG DTDDLAANTD GFDIGESTYI TITGAEIYNQ DDCVAINSGE NIYFSASVCS 

       250        260        270        280        290        300 
GGHGLSIGSV GGRDDNTVKN VTFYDVNVLK SQQAIRIKTI YGDTGSVSEV TYHEIAFSDA 

       310        320        330        340        350        360 
TDYGIVIEQN YDDTSKTPTT GVPITDFVLE NIVGTCEDDD CTEVYIACGD GSCSDWTWTG 

       370        380 
VSVTGGSVSD DCLNVPSGIS CDL 

« Hide

References

[1]"The polygalacturonases of Aspergillus niger are encoded by a family of diverged genes."
Bussink H.J.D., Buxton F.P., Fraaye B.A., de Graaff L.H., Visser J.
Eur. J. Biochem. 208:83-90(1992) [PubMed: 1511691] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.

Cross-references

Sequence databases

X64356 Genomic DNA. Translation: CAA45707.1.

3D structure databases

HSSPHSSP built from PDB template 1IB4 based on UniProtKB O74213.
ModBaseSearch...

Protein family/group databases

CAZyGH28. Glycoside Hydrolase Family 28.

Enzyme and pathway databases

BRENDA3.2.1.15. 277.

Family and domain databases

InterProIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
PfamPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTSM00710. PbH1. 4 hits.
[Graphical view]
PROSITEPS00502. POLYGALACTURONASE. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGLR3_ASPNG
AccessionPrimary (citable) accession number: Q12554
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

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