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O74213 (PGLR1_ASPAC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 66. 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 I
EC=3.2.1.15
Alternative name(s):
Pectinase 1
Polygalacturonase I
Short name=PG-I
Gene names
Name:pgaI
Synonyms:pg1, pga1
OrganismAspergillus aculeatus
Taxonomic identifier5053 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length378 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
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cellular 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 – 2020 Potential
Propeptide21 – 3919 Potential
PRO_0000024762
Chain40 – 378339Endopolygalacturonase I
PRO_0000024763

Regions

Repeat174 – 20431PbH1 1
Repeat205 – 22622PbH1 2
Repeat227 – 24721PbH1 3
Repeat256 – 27722PbH1 4
Repeat285 – 30723PbH1 5

Sites

Active site2191Proton donor
Active site2411

Amino acid modifications

Glycosylation441O-linked (Man...) Ref.3
Glycosylation461O-linked (Man...) Ref.3
Glycosylation481O-linked (Man...) Ref.3
Glycosylation521O-linked (Man...) Ref.3
Glycosylation531O-linked (Man...) Ref.3
Glycosylation551O-linked (Man...) Ref.3
Glycosylation571O-linked (Man...) Ref.3
Glycosylation621O-linked (Man...) Ref.3
Glycosylation631O-linked (Man...) Ref.3
Glycosylation731O-linked (Man...) Ref.3
Glycosylation2581N-linked (GlcNAc...) Ref.3
Disulfide bond43 ↔ 61
Disulfide bond221 ↔ 237
Disulfide bond345 ↔ 350
Disulfide bond369 ↔ 378

Secondary structure

1 ................................................................ 378
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O74213 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: DC5B9B6E1D2059C8

FASTA37838,528
        10         20         30         40         50         60 
MHLNTTLLVS LALGAASVLA SPAPPAITAP PTAEEIAKRA TTCTFSGSNG ASSASKSKTS 

        70         80         90        100        110        120 
CSTIVLSNVA VPSGTTLDLT KLNDGTHVIF SGETTFGYKE WSGPLISVSG SDLTITGASG 

       130        140        150        160        170        180 
HSINGDGSRW WDGEGGNGGK TKPKFFAAHS LTNSVISGLK IVNSPVQVFS VAGSDYLTLK 

       190        200        210        220        230        240 
DITIDNSDGD DNGGHNTDAF DIGTSTYVTI SGATVYNQDD CVAVNSGENI YFSGGYCSGG 

       250        260        270        280        290        300 
HGLSIGSVGG RSDNTVKNVT FVDSTIINSD NGVRIKTNID TTGSVSDVTY KDITLTSIAK 

       310        320        330        340        350        360 
YGIVVQQNYG DTSSTPTTGV PITDFVLDNV HGSVVSSGTN ILISCGSGSC SDWTWTDVSV 

       370 
SGGKTSSKCT NVPSGASC

« Hide

References

[1]"Molecular and biochemical characterization of three functionally different polygalacturonases from the filamentous fungus Aspergillus aculeatus."
Kauppinen S., Andersen L.N., Christgau S., Dalboege H., Kofod L.V.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: KSM 510.
[2]"Molecular and biochemical characterization of three polygalacturonases from the filamentous fungus Aspergillus aculeatus."
Schnorr K.M., Kauppinen S.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The X-ray structure of Aspergillus aculeatus polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex."
Cho S.W., Lee S., Shin W.
J. Mol. Biol. 311:863-878(2001) [PubMed: 11518536] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-378, GLYCOSYLATION AT THR-44; SER-46; SER-48; SER-52; SER-53; SER-55; SER-57; SER-62; THR-63; SER-73 AND ASN-258.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF054893 mRNA. Translation: AAC23565.1.
AJ581480 mRNA. Translation: CAE46193.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IA5X-ray2.00A40-378[»]
1IB4X-ray2.00A/B40-378[»]
ProteinModelPortalO74213.
SMRO74213. Positions 40-378.
ModBaseSearch...

Protein family/group databases

CAZyGH28. Glycoside Hydrolase Family 28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000743. Glyco_hydro_28.
IPR006626. PbH1.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
Gene3DG3DSA:2.160.20.10. Pectin_lyas_fold. 1 hit.
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...

Entry information

Entry namePGLR1_ASPAC
AccessionPrimary (citable) accession number: O74213
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1998
Last modified: May 31, 2011
This is version 66 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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