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P26214 (PGLR2_ASPNG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endopolygalacturonase II
Short name=EPG-II
EC=3.2.1.15
Alternative name(s):
Pectinase 2
Polygalacturonase II
Short name=PG-II
Polygalacturonase X2
Gene names
Name:pgaII
Synonyms:pg2
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.

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 5 PbH1 repeats.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   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 – 2121 Potential
Propeptide22 – 276 Potential
PRO_0000024770
Chain28 – 362335Endopolygalacturonase II
PRO_0000024771

Regions

Repeat156 – 18631PbH1 1
Repeat209 – 22921PbH1 2
Repeat238 – 25922PbH1 3
Repeat267 – 28923PbH1 4
Repeat301 – 32222PbH1 5

Sites

Active site2011Proton donor
Active site2231

Amino acid modifications

Glycosylation2401N-linked (GlcNAc...) (high mannose)
CAR_000232
Disulfide bond30 ↔ 45
Disulfide bond203 ↔ 219
Disulfide bond329 ↔ 334
Disulfide bond353 ↔ 362

Experimental info

Mutagenesis1801D → E or N: Reduces activity by 99.9%. No effect on Km for substrate. Ref.3
Mutagenesis2011D → E or N: Reduces activity by 99.9%. No effect on Km for substrate. Ref.3
Mutagenesis2021D → E: Reduces activity by 99.4%. No effect on Km for substrate. Ref.3
Mutagenesis2021D → N: Reduces activity by 99.9%. No effect on Km for substrate. Ref.3
Mutagenesis2231H → A: Reduces activity by 99.5%. No effect on Km for substrate. Ref.3
Mutagenesis2561R → N: Reduces activity by 86%. Reduces Km for substrate 10-fold. Ref.3
Mutagenesis2581K → N: Reduces activity by 99.2%. Reduces Km for substrate 10-fold. Ref.3

Secondary structure

1 ............................................................. 362
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P26214 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 952A79F612BC8000

FASTA36237,684
        10         20         30         40         50         60 
MHSFASLLAY GLVAGATFAS ASPIEARDSC TFTTAAAAKA GKAKCSTITL NNIEVPAGTT 

        70         80         90        100        110        120 
LDLTGLTSGT KVIFEGTTTF QYEEWAGPLI SMSGEHITVT GASGHLINCD GARWWDGKGT 

       130        140        150        160        170        180 
SGKKKPKFFY AHGLDSSSIT GLNIKNTPLM AFSVQANDIT FTDVTINNAD GDTQGGHNTD 

       190        200        210        220        230        240 
AFDVGNSVGV NIIKPWVHNQ DDCLAVNSGE NIWFTGGTCI GGHGLSIGSV GDRSNNVVKN 

       250        260        270        280        290        300 
VTIEHSTVSN SENAVRIKTI SGATGSVSEI TYSNIVMSGI SDYGVVIQQD YEDGKPTGKP 

       310        320        330        340        350        360 
TNGVTIQDVK LESVTGSVDS GATEIYLLCG SGSCSDWTWD DVKVTGGKKS TACKNFPSVA 


SC

« Hide

References

[1]"Molecular cloning, nucleotide sequence and expression of the gene encoding prepro-polygalacturonase II of Aspergillus niger."
Bussink H.J.D., Kester H.C.M., Visser J.
FEBS Lett. 273:127-130(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-40 AND 151-161.
Strain: ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400.
[2]"Identification of the glycosylation site and glycan structures of recombinant endopolygalacturonase II by mass spectrometry."
Yang Y., Bergmann C., Benen J., Orlando R.
Rapid Commun. Mass Spectrom. 11:1257-1262(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE OF CARBOHYDRATE ON ASN-240, MASS SPECTROMETRY.
[3]"1.68-A crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis."
van Santen Y., Benen J.A.E., Schroeter K.-H., Kalk K.H., Armand S., Visser J., Dijkstra B.W.
J. Biol. Chem. 274:30474-30480(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS), MUTAGENESIS OF ASP-180; ASP-201; ASP-202; HIS-223; ARG-256 AND LYS-258.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X58893 Genomic DNA. Translation: CAA41694.1.
PIRS12895.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CZFX-ray1.68A/B1-362[»]
ProteinModelPortalP26214.
SMRP26214. Positions 28-362.
ModBaseSearch...

Protein family/group databases

CAZyGH28. Glycoside Hydrolase Family 28.
mycoCLAPPGA28II_ASPNG.

PTM databases

GlycoSuiteDBP26214.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG5434.

Enzyme and pathway databases

SABIO-RKP26214.

Family and domain databases

Gene3D2.160.20.10. 1 hit.
InterProIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamPF00295. Glyco_hydro_28. 1 hit.
[Graphical view]
SMARTSM00710. PbH1. 5 hits.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
PROSITEPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26214.

Entry information

Entry namePGLR2_ASPNG
AccessionPrimary (citable) accession number: P26214
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: April 3, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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