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Q00293 (PGLRX_ASPTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 66. 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 X
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:pgaX
OrganismAspergillus tubingensis
Taxonomic identifier5068 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates. Ref.1

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 5 PbH1 repeats.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.2. Ref.1

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentSecreted
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
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 – 2222 Ref.1
Chain23 – 435413Exopolygalacturonase X
PRO_0000024822

Regions

Repeat199 – 22931PbH1 1
Repeat230 – 25122PbH1 2
Repeat253 – 27321PbH1 3
Repeat326 – 34722PbH1 4
Repeat361 – 40949PbH1 5

Sites

Active site2441Proton donor By similarity
Active site2671 By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Potential
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Disulfide bond246 ↔ 263 By similarity
Disulfide bond391 ↔ 397 By similarity

Experimental info

Sequence conflict251R → L AA sequence Ref.1
Sequence conflict311C → T AA sequence Ref.1
Sequence conflict411P → L AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q00293 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C47CD97FCD1657C0

FASTA43547,296
        10         20         30         40         50         60 
MRLTHVLSHT LGLLALGATA EAFSRSREAA CGPKKPFRPL PTSQSRDKTC HVRSHGDGTD 

        70         80         90        100        110        120 
DSDYILSALN QCNHGGKVVF DEDKEYIIGT ALNMTFLKNI DLEVLGTILF TNDTDYWQAN 

       130        140        150        160        170        180 
SFKQGFQNAT TFFQLGGEDV NMYGGGTING NGQVWYDLYA EDDLILRPIL MGIIGLNGGT 

       190        200        210        220        230        240 
IGPLKLRYSP QYYHFVANSS NVLFDGIDIS GYSKSDNEAK NTDGWDTYRS NNIVIQNSVI 

       250        260        270        280        290        300 
NNGDDCVSFK PNSTNILVQN LHCNGSHGIS VGSLGQYKDE VDIVENVYVY NISMFNASDM 

       310        320        330        340        350        360 
ARIKVWPGTP SALSADLQGG GGSGSVKNIT YDTALIDNVD WAIEITQCYG QKNTTLCNEY 

       370        380        390        400        410        420 
PSSLTISDVH IKNFRGTTSG SEDPYVGTIV CSSPDTCSDI YTSNINVTSP DGTNDFVCDN 

       430 
VDESLLSVNC TATSD

« Hide

References

[1]"Primary structure and characterization of an exopolygalacturonase from Aspergillus tubingensis."
Kester H.C.M., Kusters-Van Someren M.A., Mueller Y., Visser J.
Eur. J. Biochem. 240:738-746(1996) [PubMed: 8856078] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 23-41; 172-191 AND 301-315, GLYCOSYLATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X99795 Genomic DNA. Translation: CAA68128.1.
PIRS74208.

3D structure databases

ProteinModelPortalQ00293.
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 namePGLRX_ASPTU
AccessionPrimary (citable) accession number: Q00293
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
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

SIMILARITY comments

Index of protein domains and families

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