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P69327 (AMYG_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucoamylase

EC=3.2.1.3
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene names
Name:GLAA
OrganismAspergillus awamori (Black koji mold)
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length640 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCarbohydrate metabolism
Polysaccharide degradation
   Coding sequence diversityAlternative splicing
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionglucan 1,4-alpha-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

starch binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform G1 (identifier: P69327-1)

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: P69327-2)

The sequence of this isoform differs from the canonical sequence as follows:
     527-534: STSSTSCT → TTRSGMSL
     535-640: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 246
PRO_0000001459
Chain25 – 640616Glucoamylase
PRO_0000001460

Regions

Domain533 – 640108CBM20

Sites

Active site2001Proton acceptor Ref.3
Active site2031Proton donor Ref.3
Binding site1441Substrate

Amino acid modifications

Glycosylation1951N-linked (GlcNAc...)
CAR_000112
Glycosylation4191N-linked (GlcNAc...)
CAR_000113
Glycosylation4651O-linked (Man) By similarity
Glycosylation4671O-linked (Man)
Glycosylation4681O-linked (Man)
Glycosylation4761O-linked (Man)
Glycosylation4771O-linked (Man)
Glycosylation4831O-linked (Man)
Glycosylation4841O-linked (Man)
Glycosylation4861O-linked (Man)
Glycosylation4881O-linked (Man)
Glycosylation4921O-linked (Man) By similarity
Glycosylation4961O-linked (Man) By similarity
Glycosylation4991O-linked (Man) By similarity
Glycosylation5001O-linked (Man) By similarity
Glycosylation5011O-linked (Man) By similarity
Glycosylation5021O-linked (Man) By similarity
Glycosylation5041O-linked (Man) By similarity
Glycosylation5061O-linked (Man) By similarity
Glycosylation5081O-linked (Man) By similarity
Glycosylation5101O-linked (Man) By similarity
Glycosylation5121O-linked (Man) By similarity
Glycosylation5131O-linked (Man) By similarity
Glycosylation5141O-linked (Man) By similarity
Glycosylation5151O-linked (Man) By similarity
Glycosylation5171O-linked (Man) By similarity
Glycosylation5181O-linked (Man) By similarity
Glycosylation5201O-linked (Man) By similarity
Glycosylation5221O-linked (Man) By similarity
Glycosylation5241O-linked (Man) By similarity
Glycosylation5251O-linked (Man) By similarity
Glycosylation5261O-linked (Man) By similarity
Glycosylation5271O-linked (Man) By similarity
Glycosylation5281O-linked (Man) By similarity
Glycosylation5291O-linked (Man) By similarity
Glycosylation5301O-linked (Man) By similarity
Glycosylation5311O-linked (Man) By similarity
Glycosylation5321O-linked (Man) By similarity
Glycosylation5341O-linked (Man) By similarity
Glycosylation5351O-linked (Man) By similarity
Disulfide bond234 ↔ 237 Ref.6
Disulfide bond246 ↔ 473 Ref.6
Disulfide bond286 ↔ 294 Ref.6

Natural variations

Alternative sequence527 – 5348STSSTSCT → TTRSGMSL in isoform G2.
VSP_012836
Alternative sequence535 – 640106Missing in isoform G2.
VSP_000262

Experimental info

Mutagenesis1441W → Y: 2% of wild-type activity. Ref.4

Secondary structure

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

Details...

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 

« Hide

Isoform G2 [UniParc].

Checksum: 94D188E946D0C12E
Show »

FASTA53456,730

References

[1]"Molecular cloning and characterization of the glucoamylase gene of Aspergillus awamori."
Nunberg J.H., Meade J.H., Cole G., Lawyer F.C., McCabe P., Schweickart V., Tal R., Wittman V.P., Flatgaard J.E., Innis M.A.
Mol. Cell. Biol. 4:2306-2315(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS G1 AND G2).
[2]Nunberg J.H., Meade J.H., Cole G., Lawyer F.C., McCabe P., Schweickart V., Tal R., Wittman V.P., Flatgaard J.E., Innis M.A.
Submitted (FEB-1985) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Catalytic mechanism of fungal glucoamylase as defined by mutagenesis of Asp176, Glu179 and Glu180 in the enzyme from Aspergillus awamori."
Sierks M.R., Ford C., Reilly P.J., Svensson B.
Protein Eng. 3:193-198(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITES, MUTAGENESIS.
[4]"Site-directed mutagenesis at the active site Trp120 of Aspergillus awamori glucoamylase."
Sierks M.R., Ford C., Reilly P.J., Svensson B.
Protein Eng. 2:621-625(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TRP-144.
[5]"Functional roles and subsite locations of Leu177, Trp178 and Asn182 of Aspergillus awamori glucoamylase determined by site-directed mutagenesis."
Sierks M.R., Ford C., Reilly P.J., Svensson B.
Protein Eng. 6:75-79(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[6]"Crystal structure of glucoamylase from Aspergillus awamori var. X100 to 2.2-A resolution."
Aleshin A., Golubev A., Firsov L.M., Honzatko R.B.
J. Biol. Chem. 267:19291-19298(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-495, GLYCOSYLATION, DISULFIDE BONDS.
Strain: Var. X100.
[7]"Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori var. X100 to 2.4-A resolution."
Aleshin A., Firsov L.M., Honzatko R.B.
J. Biol. Chem. 269:15631-15639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-495.
Strain: Var. X100.
[8]"Refined crystal structures of glucoamylase from Aspergillus awamori var. X100."
Aleshin A., Hoffman C., Firsov L.M., Honzatko R.B.
J. Mol. Biol. 238:575-591(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-495, GLYCOSYLATION.
Strain: Var. X100.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
K02465 mRNA. Translation: AAB59296.1.
K02465 mRNA. Translation: AAB59297.1.
PIRA29166.
A29776. A93066.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGMX-ray2.30A25-495[»]
1DOGX-ray2.30A25-495[»]
1GAHX-ray2.00A25-496[»]
1GAIX-ray1.70A25-497[»]
1GLMX-ray2.40A25-495[»]
3GLYX-ray2.20A25-495[»]
ProteinModelPortalP69327.
SMRP69327. Positions 25-640.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP69327.

Protein family/group databases

mycoCLAPGLA15A_ASPAW.

PTM databases

UniCarbKBP69327.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR015902. Glyco_hydro_13.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERPTHR10357. PTHR10357. 1 hit.
PfamPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSPR00736. GLHYDRLASE15.
SMARTSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP69327.

Entry information

Entry nameAMYG_ASPAW
AccessionPrimary (citable) accession number: P69327
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: December 11, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries