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Reviewed, UniProtKB/Swiss-Prot P69328 (AMYG_ASPNG)

Last modified June 16, 2009. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glucoamylase
    EC=3.2.1.3
Alternative name(s):
    Glucan 1,4-alpha-glucosidase
    1,4-alpha-D-glucan glucohydrolase
Gene names
Name: GLAA
OrganismAspergillus niger
Taxonomic identifier5061 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 246 Ref.3 Ref.4
PRO_0000001461
Chain25 – 640616Glucoamylase
PRO_0000001462

Regions

Domain533 – 640108CBM20

Sites

Active site2001Proton acceptor By similarity
Active site2031Proton donor By similarity
Binding site1441Substrate By similarity

Amino acid modifications

Glycosylation1951N-linked (GlcNAc...) By similarity
Glycosylation4191N-linked (GlcNAc...) By similarity
Glycosylation4651O-linked (Man)
Glycosylation4671O-linked (Man)
Glycosylation4681O-linked (Man)
Glycosylation4761O-linked (Man)
Glycosylation4771O-linked (Man)
Glycosylation4831O-linked (Man)
Glycosylation4841O-linked (Man)
Glycosylation4861O-linked (Man)
Glycosylation4881O-linked (Man)
Glycosylation4891O-linked (Man)
Glycosylation4921O-linked (Man)
Glycosylation4961O-linked (Man)
Glycosylation4991O-linked (Man)
Glycosylation5001O-linked (Man)
Glycosylation5011O-linked (Man)
Glycosylation5021O-linked (Man)
Glycosylation5041O-linked (Man)
Glycosylation5061O-linked (Man)
Glycosylation5081O-linked (Man)
Glycosylation5101O-linked (Man)
Glycosylation5121O-linked (Man)
Glycosylation5131O-linked (Man)
Glycosylation5141O-linked (Man)
Glycosylation5151O-linked (Man)
Glycosylation5171O-linked (Man)
Glycosylation5181O-linked (Man)
Glycosylation5201O-linked (Man)
Glycosylation5221O-linked (Man)
Glycosylation5241O-linked (Man)
Glycosylation5251O-linked (Man)
Glycosylation5261O-linked (Man)
Glycosylation5271O-linked (Man)
Glycosylation5281O-linked (Man)
Glycosylation5291O-linked (Man)
Glycosylation5301O-linked (Man)
Glycosylation5311O-linked (Man)
Glycosylation5321O-linked (Man)
Glycosylation5341O-linked (Man)
Glycosylation5351O-linked (Man)
Disulfide bond234 ↔ 237 By similarity
Disulfide bond246 ↔ 473 By similarity
Disulfide bond286 ↔ 294 By similarity

Natural variations

Alternative sequence527 – 5348STSSTSCT → TTRSGMSL in isoform G2.
VSP_012837
Alternative sequence535 – 640106Missing in isoform G2.
VSP_012838

Secondary structure

1 ........................ 640
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Isoform G1 [UniParc].

Last modified November 1, 1986. Version 1.
Checksum: 26F58DD18AD7F702

FASTA64068,309
        10         20         30         40         50         60 
MSFRSLLALS GLVCTGLANV ISKRATLDSW LSNEATVART AILNNIGADG AWVSGADSGI 

        70         80         90        100        110        120 
VVASPSTDNP DYFYTWTRDS GLVLKTLVDL FRNGDTSLLS TIENYISAQA IVQGISNPSG 

       130        140        150        160        170        180 
DLSSGAGLGE PKFNVDETAY TGSWGRPQRD GPALRATAMI GFGQWLLDNG YTSTATDIVW 

       190        200        210        220        230        240 
PLVRNDLSYV AQYWNQTGYD LWEEVNGSSF FTIAVQHRAL VEGSAFATAV GSSCSWCDSQ 

       250        260        270        280        290        300 
APEILCYLQS FWTGSFILAN FDSSRSGKDA NTLLGSIHTF DPEAACDDST FQPCSPRALA 

       310        320        330        340        350        360 
NHKEVVDSFR SIYTLNDGLS DSEAVAVGRY PEDTYYNGNP WFLCTLAAAE QLYDALYQWD 

       370        380        390        400        410        420 
KQGSLEVTDV SLDFFKALYS DAATGTYSSS SSTYSSIVDA VKTFADGFVS IVETHAASNG 

       430        440        450        460        470        480 
SMSEQYDKSD GEQLSARDLT WSYAALLTAN NRRNSVVPAS WGETSASSVP GTCAATSAIG 

       490        500        510        520        530        540 
TYSSVTVTSW PSIVATGGTT TTATPTGSGS VTSTSKTTAT ASKTSTSTSS TSCTTPTAVA 

       550        560        570        580        590        600 
VTFDLTATTT YGENIYLVGS ISQLGDWETS DGIALSADKY TSSDPLWYVT VTLPAGESFE 

       610        620        630        640 
YKFIRIESDD SVEWESDPNR EYTVPQACGT STATVTDTWR

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Isoform G2.

Checksum: 94D188E946D0C12E
Show »

FASTA53456,730

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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.

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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.
PIRALASGR. A90986.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AC0NMR-A533-640[»]
1ACZNMR-A533-640[»]
1KULNMR-A533-640[»]
1KUMNMR-A533-640[»]
SMRP69328. Positions 25-497.
ModBaseSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.

Enzyme and pathway databases

BRENDA3.2.1.3. 277.

Family and domain databases

InterProIPR012341. 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]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
PfamPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSPR00736. GLHYDRLASE15.
ProDomPD001568. Glyco_hydro_CBD. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameAMYG_ASPNG
AccessionPrimary (citable) accession number: P69328
Secondary accession number(s): P04064, Q92201, Q99179
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: November 1, 1986
Last modified: June 16, 2009
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents