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Q00359 (PGLRX_COCCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Exopolygalacturonase
Short name=ExoPG
EC=3.2.1.67
Alternative name(s):
Galacturan 1,4-alpha-galacturonidase
Poly(1,4-alpha-D-galacturonide)galacturonohydrolase
Gene names
Name:PGX1
OrganismCochliobolus carbonum (Bipolaris zeicola)
Taxonomic identifier5017 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporineae › Pleosporaceae › Cochliobolus

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Hydrolysis of 1,4-alpha-D-galactosiduronic linkages in pectate and other galacturonans.

Catalytic activity

((1->4)-alpha-D-galacturonide)(n) + H2O = ((1->4)-alpha-D-galacturonide)(n-1) + D-galacturonate.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 28 family.

Contains 6 PbH1 repeats.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
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 functiongalacturan 1,4-alpha-galacturonidase activity

Inferred from electronic annotation. Source: EC

polygalacturonase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 446429Exopolygalacturonase
PRO_0000024823

Sites

Active site2501Proton donor By similarity
Active site2731 By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2581N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3021N-linked (GlcNAc...) Potential
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation3591N-linked (GlcNAc...) Potential
Glycosylation3691N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q00359 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 71C535D5720D6325

FASTA44647,764
        10         20         30         40         50         60 
MRVTDIISCA LLQASIALST PVEELGAKAV VAKRFPPVPF LPGKASSVPG SRNKTCMLKA 

        70         80         90        100        110        120 
LGGGKDDSAN ILSAVKQCNN GGHVVFPKGQ QFTIGTALDL TFLNGIDLDI QGTIQFTNDT 

       130        140        150        160        170        180 
DYWQANSFKQ VFQNATTFFQ LGGKDINVYG GGTLDGNGQA WYDLYAKDIY ILRPILFGLI 

       190        200        210        220        230        240 
GAKNAKISDL KFRYSPQWYT LVANSSQVVF SNIDIFGDSK SKNPAKNTDG WDTYRSDNII 

       250        260        270        280        290        300 
IQNSNINNGD DCVSFKPNST NILVQNLVCN GSHGISVGSL GQYPGEVDIV ENILVRNISM 

       310        320        330        340        350        360 
SNASDGARIK VWPGASSALS GDLQGGGGSG AVRNVTYDGM IVKNVDYAIE ITQCYGQKNL 

       370        380        390        400        410        420 
TLCNQFPSNL TISDITIKNF KGTTSKKYDP RVGYVVCSSP KVCSDISIEN IDVKSPSGTN 

       430        440 
LFTCANAEGI QSQVNCTVEG DKGGHS

« Hide

References

[1]"Targeted mutants of Cochliobolus carbonum lacking the two major extracellular polygalacturonases."
Scott-Craig J.S., Cheng Y.Q., Cervone F., de Lorenzo G., Pitkin J.W., Walton J.D.
Appl. Environ. Microbiol. 64:1497-1503(1998) [PubMed: 9546185] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 90305 / SB111 / 2R15.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L48982 Genomic DNA. Translation: AAC26146.1.

3D structure databases

ProteinModelPortalQ00359.
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. 6 hits.
[Graphical view]
SUPFAMSSF51126. Pectin_lyas_like. 1 hit.
PROSITEPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGLRX_COCCA
AccessionPrimary (citable) accession number: Q00359
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 31, 2011
This is version 64 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

SIMILARITY comments

Index of protein domains and families

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