Q00293 · PGLRX_ASPTU
- ProteinExopolygalacturonase X
- GenepgaX
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids435 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Specific in hydrolyzing the terminal glycosidic bond of polygalacturonic acid and oligogalacturonates.
Catalytic activity
- [(1->4)-alpha-D-galacturonosyl](n) + H2O = alpha-D-galacturonate + [(1->4)-alpha-D-galacturonosyl](n-1)
[(1→4)-α-D-galacturonosyl](n) RHEA-COMP:14570 + CHEBI:15377 = CHEBI:58658 + [(1→4)-α-D-galacturonosyl](n-1) RHEA-COMP:14572
pH Dependence
Optimum pH is 4.2.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 244 | Proton donor | |||
Active site | 267 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | galacturan 1,4-alpha-galacturonidase activity | |
Molecular Function | polygalacturonase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | cell wall organization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameExopolygalacturonase X
- EC number
- Short namesExoPG
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionQ00293
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-22 | ||||
Chain | PRO_0000024822 | 23-435 | Exopolygalacturonase X | ||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 112 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 128 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 198 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 246↔263 | ||||
Glycosylation | 252 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 264 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 291 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 296 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 328 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 353 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 391↔397 | ||||
Glycosylation | 406 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 429 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for region, repeat.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 32-55 | Disordered | |||
Repeat | 199-229 | PbH1 1 | |||
Repeat | 230-251 | PbH1 2 | |||
Repeat | 253-273 | PbH1 3 | |||
Repeat | 326-347 | PbH1 4 | |||
Repeat | 361-409 | PbH1 5 | |||
Sequence similarities
Belongs to the glycosyl hydrolase 28 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length435
- Mass (Da)47,296
- Last updated1996-11-01 v1
- ChecksumC47CD97FCD1657C0
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 25 | in Ref. 1; AA sequence | |||
Sequence conflict | 31 | in Ref. 1; AA sequence | |||
Sequence conflict | 41 | in Ref. 1; AA sequence | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X99795 EMBL· GenBank· DDBJ | CAA68128.1 EMBL· GenBank· DDBJ | Genomic DNA |