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Reviewed, UniProtKB/Swiss-Prot Q07181 (PGLR_GIBFU)

Last modified January 19, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
      Short name=PG
    EC=3.2.1.15
Alternative name(s):
    FmPG
    Pectinase
Gene names
Name: PGA
OrganismGibberella fujikuroi (Bakanae and foot rot disease fungus) (Fusarium moniliforme)
Taxonomic identifier5127 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeGibberellaGibberella fujikuroi complex

Protein attributes

Sequence length373 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 8 PbH1 repeats.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide 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 – 2424 Potential
Chain25 – 373349Polygalacturonase
PRO_0000024786

Regions

Repeat136 – 15823PbH1 1
Repeat159 – 19739PbH1 2
Repeat198 – 21922PbH1 3
Repeat220 – 24021PbH1 4
Repeat249 – 27022PbH1 5
Repeat278 – 30023PbH1 6
Repeat312 – 33322PbH1 7
Repeat345 – 36925PbH1 8

Sites

Active site2121Proton donor By similarity
Active site2341 By similarity

Amino acid modifications

Glycosylation651N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation2801N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 42
Disulfide bond214 ↔ 230
Disulfide bond340 ↔ 345
Disulfide bond364 ↔ 371

Experimental info

Mutagenesis1881H → P: Reduces activity by 98.2%. Lowers affinity for substrate 50-fold. Ref.2
Mutagenesis1911D → A: Loss of activity. No effect on Km for substrate. Ref.2
Mutagenesis212 – 2132DD → EE: Loss of activity. No effect on Km for substrate.
Mutagenesis212 – 2132DD → NN: Loss of activity. No effect on Km for substrate.
Mutagenesis2671R → A: Loss of activity. Lowers affinity for substrate over 10-fold. Ref.2
Mutagenesis2691K → E: Reduces activity by 99.87%. Lowers affinity for substrate over 10-fold. Ref.2

Secondary structure

......................................................... 373
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q07181-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: D77BCACAC7FFBD8F

FASTA37338,915
        10         20         30         40         50         60 
MVRNIVSRLC SQLFALPSSS LQERDPCSVT EYSGLATAVS SCKNIVLNGF QVPTGKQLDL 

        70         80         90        100        110        120 
SSLQNDSTVT FKGTTTFATT ADNDFNPIVI SGSNITITGA SGHVIDGNGQ AYWDGKGSNS 

       130        140        150        160        170        180 
NSNQKPDHFI VVQKTTGNSK ITNLNIQNWP VHCFDITGSS QLTISGLILD NRAGDKPNAK 

       190        200        210        220        230        240 
SGSLPAAHNT DGFDISSSDH VTLDNNHVYN QDDCVAVTSG TNIVVSNMYC SGGHGLSIGS 

       250        260        270        280        290        300 
VGGKSDNVVD GVQFLSSQVV NSQNGCRIKS NSGATGTINN VTYQNIALTN ISTYGVDVQQ 

       310        320        330        340        350        360 
DYLNGGPTGK PTNGVKISNI KFIKVTGTVA SSAQDWFILC GDGSCSGFTF SGNAITGGGK 

       370 
TSSCNYPTNT CPS 

« Hide

References

[1]"Cloning and characterization of a gene encoding the endopolygalacturonase of Fusarium moniliforme."
Caprari C., Richter A., Bergmann C., Lo Cicero S., Salvi G., Cervone F., de Lorenzo G.
Mycol. Res. 97:497-505(1993) [Agricola: IND93032473]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structural requirements of endopolygalacturonase for the interaction with PGIP (polygalacturonase-inhibiting protein)."
Federici L., Caprari C., Mattei B., Savino C., Di Matteo A., De Lorenzo G., Cervone F., Tsernoglou D.
Proc. Natl. Acad. Sci. U.S.A. 98:13425-13430(2001) [PubMed: 11687632] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 25-373, MUTAGENESIS OF HIS-188; ASP-191; 212-ASP-ASP-213; ARG-267 AND LYS-269.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02239 Genomic DNA. Translation: AAA74586.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HG8X-ray1.73A25-373[»]
ModBaseSearch...

Protein family/group databases

CAZyGH28. Glycoside Hydrolase Family 28.

Enzyme and pathway databases

BRENDA3.2.1.15. 97815.

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. 8 hits.
[Graphical view]
PROSITEPS00502. POLYGALACTURONASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGLR_GIBFU
AccessionPrimary (citable) accession number: Q07181
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 19, 2010
This is version 64 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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