Reviewed,
UniProtKB/Swiss-Prot P69328 (AMYG_ASPNG)
Last modified
June 16, 2009.
Version 36.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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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 niger | ||
| Taxonomic identifier | 5061 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus |
Protein attributes
| Sequence length | 640 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
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 |
| Coding sequence diversity | Alternative splicing |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Cleavage on pair of basic residues Disulfide bond Glycoprotein |
| Technical term | 3D-structure Direct protein sequencing |
| 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... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform G1 (identifier: P69328-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform G2 (identifier: P69328-2) The sequence of this isoform differs from the canonical sequence as follows: 527-534: STSSTSCT → TTRSGMSL 535-640: Missing. |
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 | Ref.3 Ref.4 | PRO_0000001461 | ||||||||||||||||||||||||||||
| Chain | 25 – 640 | 616 | Glucoamylase | PRO_0000001462 | ||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||
| Domain | 533 – 640 | 108 | CBM20 | |||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||
| Active site | 200 | 1 | Proton acceptor By similarity | |||||||||||||||||||||||||||||
| Active site | 203 | 1 | Proton donor By similarity | |||||||||||||||||||||||||||||
| Binding site | 144 | 1 | Substrate By similarity | |||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||
| Glycosylation | 195 | 1 | N-linked (GlcNAc...) By similarity | |||||||||||||||||||||||||||||
| Glycosylation | 419 | 1 | N-linked (GlcNAc...) By similarity | |||||||||||||||||||||||||||||
| Glycosylation | 465 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 467 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 468 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 476 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 477 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 483 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 484 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 486 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 488 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 489 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 492 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 496 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 499 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 500 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 501 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 502 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 504 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 506 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 508 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 510 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 512 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 513 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 514 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 515 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 517 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 518 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 520 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 522 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 524 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 525 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 526 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 527 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 528 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 529 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 530 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 531 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 532 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 534 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Glycosylation | 535 | 1 | O-linked (Man) | |||||||||||||||||||||||||||||
| Disulfide bond | 234 ↔ 237 | By similarity | ||||||||||||||||||||||||||||||
| Disulfide bond | 246 ↔ 473 | By similarity | ||||||||||||||||||||||||||||||
| Disulfide bond | 286 ↔ 294 | By similarity | ||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||
| Alternative sequence | 527 – 534 | 8 | STSSTSCT → TTRSGMSL in isoform G2. | VSP_012837 | ||||||||||||||||||||||||||||
| Alternative sequence | 535 – 640 | 106 | Missing in isoform G2. | VSP_012838 | ||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Beta strand | 540 – 546 | 7 | ||||||||||||||||||||||||||||||
| Beta strand | 554 – 561 | 8 | ||||||||||||||||||||||||||||||
| Helix | 562 – 564 | 3 | ||||||||||||||||||||||||||||||
| Turn | 565 – 567 | 3 | ||||||||||||||||||||||||||||||
| Turn | 569 – 571 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 572 – 574 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 576 – 579 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 581 – 584 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 586 – 588 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 598 – 606 | 9 | ||||||||||||||||||||||||||||||
| Beta strand | 608 – 610 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 620 – 623 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 632 – 638 | 7 | ||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Two different types of intervening sequences in the glucoamylase gene from Aspergillus niger." Boel E., Hansen M.T., Hjort I., Hoegh I., Fiil N.P. EMBO J. 3:1581-1585(1984) [PubMed: 6204865] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS G1 AND G2). |
| [2] | "Glucoamylases G1 and G2 from Aspergillus niger are synthesized from two different but closely related mRNAs." Boel E., Hjort I., Svensson B., Norris F., Norris K.E., Fiil N.P. EMBO J. 3:1097-1102(1984) [PubMed: 6203744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS G1 AND G2). |
| [3] | "Characterization of a glucoamylase G2 from Aspergillus niger." Svensson B., Larsen K., Gunnarsson A. Eur. J. Biochem. 154:497-502(1986) [PubMed: 3081341] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-640, COMPARISON OF FORMS G1 AND G2. |
| [4] | "The complete amino acid sequence of the glycoprotein, glucoamylase G1, from Aspergillus niger." Svensson B., Larsen K., Svendsen I., Boel E. Carlsberg Res. Commun. 48:529-544(1983) Cited for: PROTEIN SEQUENCE OF 25-640 (ISOFORM G1), GLYCOSYLATION. |
| [5] | "Regulation of the glaA gene of Aspergillus niger." Fowler T., Berka R.M., Ward M. Curr. Genet. 18:537-545(1990) [PubMed: 2076554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-11. Strain: ATCC 10864 / NRRL 330 / CBS 122.49 / IFO 6661. |
| [6] | "O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding." Williamson G., Belshaw N.J., Williamson M.P. Biochem. J. 282:423-428(1992) [PubMed: 1546955] [Abstract] Cited for: CONFORMATION OF O-GLYCOSYLATED REGION. |
| [7] | "Production, purification and characterization of the catalytic domain of glucoamylase from Aspergillus niger." Stoffer B., Frandsen T.P., Busk P.K., Schneider P., Svendsen I., Svensson B. Biochem. J. 292:197-202(1993) [PubMed: 8503847] [Abstract] Cited for: CHARACTERIZATION OF CATALYTIC DOMAIN. |
| [8] | "Solution structure of the granular starch binding domain of glucoamylase from Aspergillus niger by nuclear magnetic resonance spectroscopy." Sorimachi K., Jacks A.J., le Gal-Coeffet M.-F., Williamson G., Archer D.B., Williamson M.P. J. Mol. Biol. 259:970-987(1996) [PubMed: 8683599] [Abstract] Cited for: STRUCTURE BY NMR OF 533-640. |
| [9] | "Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin." Sorimachi K., le Gal-Coeffet M.-F., Williamson G., Archer D.B., Williamson M.P. Structure 5:647-661(1997) [PubMed: 9195884] [Abstract] Cited for: STRUCTURE BY NMR OF 533-640. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X00548 mRNA. Translation: CAA25219.1. X00712 Genomic DNA. Translation: CAA25303.1. X00712 Genomic DNA. Translation: CAA25304.1. X56442 Genomic DNA. Translation: CAA39825.1. | |||||||||||||||||||||||||||||||
| PIR | ALASGR. A90986. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||
| SMR | P69328. Positions 25-497. | ||||||||||||||||||||||||||||||
| 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. 277. | ||||||||||||||||||||||||||||||
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_ASPNG | ||||||||
| Accession | Primary (citable) accession number: P69328 Secondary accession number(s): P04064, Q92201, Q99179 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


