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P08017 (AMYG_SACFI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 83. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucoamylase GLU1

EC=3.2.1.3
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene names
Name:GLU1
OrganismSaccharomycopsis fibuligera (Yeast)
Taxonomic identifier4944 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycopsidaceaeSaccharomycopsis

Protein attributes

Sequence length519 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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 519492Glucoamylase GLU1
PRO_0000001475

Sites

Active site2341Proton acceptor By similarity
Active site2371Proton donor By similarity
Binding site1661Substrate By similarity

Amino acid modifications

Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...) Potential

Secondary structure

................................................................ 519
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08017 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: BE73035AD1B77652

FASTA51957,539
        10         20         30         40         50         60 
MKFGVLFSVF AAIVSALPLQ EGPLNKRAYP SFEAYSNYKV DRTDLETFLD KQKEVSLYYL 

        70         80         90        100        110        120 
LQNIAYPEGQ FNNGVPGTVI ASPSTSNPDY YYQWTRDSAI TFLTVLSELE DNNFNTTLAK 

       130        140        150        160        170        180 
AVEYYINTSY NLQRTSNPSG SFDDENHKGL GEPKFNTDGS AYTGAWGRPQ NDGPALRAYA 

       190        200        210        220        230        240 
ISRYLNDVNS LNEGKLVLTD SGDINFSSTE DIYKNIIKPD LEYVIGYWDS TGFDLWEENQ 

       250        260        270        280        290        300 
GRHFFTSLVQ QKALAYAVDI AKSFDDGDFA NTLSSTASTL ESYLSGSDGG FVNTDVNHIV 

       310        320        330        340        350        360 
ENPDLLQQNS RQGLDSATYI GPLLTHDIGE SSSTPFDVDN EYVLQSYYLL LEDNKDRYSV 

       370        380        390        400        410        420 
NSAYSAGAAI GRYPEDVYNG DGSSEGNPWF LATAYAAQVP YKLAYDAKSA SNDITINKIN 

       430        440        450        460        470        480 
YDFFNKYIVD LSTINSAYQS SDSVTIKSGS DEFNTVADNL VTFGDSFLQV ILDHINDDGS 

       490        500        510 
LNEQLNRYTG YSTGAYSLTW SSGALLEAIR LRNKVKALA 

« Hide

References

[1]"Nucleotide sequence of the glucoamylase gene GLU1 in the yeast Saccharomycopsis fibuligera."
Itoh T., Ohtsuki I., Yamashita I., Fukui S.
J. Bacteriol. 169:4171-4176(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7-A resolution."
Sevcik J., Solovicova A., Hostinova E., Gasperik J., Wilson K.S., Dauter Z.
Acta Crystallogr. D 54:854-866(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L25641 mRNA. Translation: AAA83997.1.
M17355 Genomic DNA. Translation: AAA34649.1.
PIRA54549.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYXX-ray1.70A28-519[»]
2F6DX-ray1.60A28-519[»]
2FBAX-ray1.10A28-519[»]
ProteinModelPortalP08017.
SMRP08017. Positions 28-519.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH15. Glycoside Hydrolase Family 15.
mycoCLAPGLA15A_SACFI.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.2.1.3. 5499.

Family and domain databases

Gene3D1.50.10.10. 1 hit.
InterProIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR000165. Glucoamylase.
IPR011613. Glyco_hydro_15.
[Graphical view]
PfamPF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PRINTSPR00736. GLHYDRLASE15.
SUPFAMSSF48208. SSF48208. 1 hit.
PROSITEPS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08017.

Entry information

Entry nameAMYG_SACFI
AccessionPrimary (citable) accession number: P08017
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 16, 2013
This is version 83 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