Q00293 · PGLRX_ASPTU

  • Protein
    Exopolygalacturonase X
  • Gene
    pgaX
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

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

Catalytic activity

pH Dependence

Optimum pH is 4.2.

Features

Showing features for active site.

143550100150200250300350400
TypeIDPosition(s)Description
Active site244Proton donor
Active site267

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functiongalacturan 1,4-alpha-galacturonidase activity
Molecular Functionpolygalacturonase activity
Biological Processcarbohydrate metabolic process
Biological Processcell wall organization

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Exopolygalacturonase X
  • EC number
  • Short names
    ExoPG
  • Alternative names
    • Galacturan 1,4-alpha-galacturonidase
    • Poly(1,4-alpha-D-galacturonide)galacturonohydrolase

Gene names

    • Name
      pgaX

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    Q00293

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond.

Type
IDPosition(s)Description
Signal1-22
ChainPRO_000002482223-435Exopolygalacturonase X
Glycosylation93N-linked (GlcNAc...) asparagine
Glycosylation112N-linked (GlcNAc...) asparagine
Glycosylation128N-linked (GlcNAc...) asparagine
Glycosylation198N-linked (GlcNAc...) asparagine
Disulfide bond246↔263
Glycosylation252N-linked (GlcNAc...) asparagine
Glycosylation264N-linked (GlcNAc...) asparagine
Glycosylation291N-linked (GlcNAc...) asparagine
Glycosylation296N-linked (GlcNAc...) asparagine
Glycosylation328N-linked (GlcNAc...) asparagine
Glycosylation353N-linked (GlcNAc...) asparagine
Disulfide bond391↔397
Glycosylation406N-linked (GlcNAc...) asparagine
Glycosylation429N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Structure

Family & Domains

Features

Showing features for region, repeat.

Type
IDPosition(s)Description
Region32-55Disordered
Repeat199-229PbH1 1
Repeat230-251PbH1 2
Repeat253-273PbH1 3
Repeat326-347PbH1 4
Repeat361-409PbH1 5

Sequence similarities

Belongs to the glycosyl hydrolase 28 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    435
  • Mass (Da)
    47,296
  • Last updated
    1996-11-01 v1
  • Checksum
    C47CD97FCD1657C0
MRLTHVLSHTLGLLALGATAEAFSRSREAACGPKKPFRPLPTSQSRDKTCHVRSHGDGTDDSDYILSALNQCNHGGKVVFDEDKEYIIGTALNMTFLKNIDLEVLGTILFTNDTDYWQANSFKQGFQNATTFFQLGGEDVNMYGGGTINGNGQVWYDLYAEDDLILRPILMGIIGLNGGTIGPLKLRYSPQYYHFVANSSNVLFDGIDISGYSKSDNEAKNTDGWDTYRSNNIVIQNSVINNGDDCVSFKPNSTNILVQNLHCNGSHGISVGSLGQYKDEVDIVENVYVYNISMFNASDMARIKVWPGTPSALSADLQGGGGSGSVKNITYDTALIDNVDWAIEITQCYGQKNTTLCNEYPSSLTISDVHIKNFRGTTSGSEDPYVGTIVCSSPDTCSDIYTSNINVTSPDGTNDFVCDNVDESLLSVNCTATSD

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict25in Ref. 1; AA sequence
Sequence conflict31in Ref. 1; AA sequence
Sequence conflict41in Ref. 1; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X99795
EMBL· GenBank· DDBJ
CAA68128.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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