Reviewed,
UniProtKB/Swiss-Prot P22832 (AMYG_ASPSH)
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June 16, 2009.
Version 70.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Glucoamylase EC=3.2.1.3 Alternative name(s): Glucan 1,4-alpha-glucosidase 1,4-alpha-D-glucan glucohydrolase | ||||
| Gene names |
| ||||
| Organism | Aspergillus shirousami | ||||
| Taxonomic identifier | 5070 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 639 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. |
| Sequence similarities | Belongs to the glycosyl hydrolase 15 family. Contains 1 CBM20 (carbohydrate binding type-20) domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Polysaccharide degradation |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Cleavage on pair of basic residues Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | carbohydrate binding Inferred from electronic annotation. Source: InterPro glucan 1,4-alpha-glucosidase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | Potential | ||||||||
| Propeptide | 19 – 24 | 6 | By similarity | PRO_0000001467 | |||||||
| Chain | 25 – 639 | 615 | Glucoamylase | PRO_0000001468 | |||||||
Regions | |||||||||||
| Domain | 532 – 639 | 108 | CBM20 | ||||||||
Sites | |||||||||||
| Active site | 199 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 202 | 1 | Proton donor By similarity | ||||||||
| Binding site | 143 | 1 | Substrate By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 194 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 205 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 418 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 464 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 466 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 467 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 475 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 476 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 482 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 483 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 485 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 487 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 488 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 491 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 495 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 498 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 499 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 500 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 501 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 503 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 505 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 507 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 511 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 512 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 513 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 514 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 516 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 517 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 519 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 521 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 523 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 524 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 525 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 527 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 528 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 529 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 530 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 531 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 533 | 1 | O-linked (Man) By similarity | ||||||||
| Glycosylation | 534 | 1 | O-linked (Man) By similarity | ||||||||
| Disulfide bond | 233 ↔ 236 | By similarity | |||||||||
| Disulfide bond | 245 ↔ 472 | By similarity | |||||||||
| Disulfide bond | 285 ↔ 293 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Molecular cloning of the glucoamylase gene of Aspergillus shirousami and its expression in Aspergillus oryzae." Shibuya I., Gomi K., Iimura Y., Takahashi K., Tamura G., Hara S. Agric. Biol. Chem. 54:1905-1914(1990) [PubMed: 1368603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| D10460 Genomic DNA. Translation: BAA01254.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GAI based on UniProtKB P04064. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | CBM20. Carbohydrate-Binding Module Family 20. GH15. Glycoside Hydrolase Family 15. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.3. 290852. |
Family and domain databases | |
| InterPro | IPR012341. 6hp_glycosidase. IPR008291. Glucamylse_SBD. IPR000165. Glyco_hydro_15. IPR011613. Glyco_hydro_15_rel. IPR002044. Glyco_hydro_carb-bd. IPR013783. Ig-like_fold. [Graphical view] |
| Gene3D | G3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit. G3DSA:2.60.40.10. Ig-like_fold. 1 hit. |
| Pfam | PF00686. CBM_20. 1 hit. PF00723. Glyco_hydro_15. 1 hit. [Graphical view] |
| PIRSF | PIRSF001031. Glu-a-glcsd_SBD. 1 hit. |
| PRINTS | PR00736. GLHYDRLASE15. |
| ProDom | PD001568. Glyco_hydro_CBD. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| PROSITE | PS51166. CBM20. 1 hit. PS00820. GLUCOAMYLASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMYG_ASPSH | ||||||||
| Accession | Primary (citable) accession number: P22832 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


