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Reviewed, UniProtKB/Swiss-Prot P26989 (AMYH_SACFI)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glucoamylase GLA1
    EC=3.2.1.3
Alternative name(s):
    Glucan 1,4-alpha-glucosidase
    1,4-alpha-D-glucan glucohydrolase
Gene names
Name: GLA1
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 existenceInferred 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.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 519492Glucoamylase GLA1
PRO_0000001476

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

Sequences

Sequence LengthMass (Da)Tools
P26989-1 [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: A15A009A7640053C

FASTA51957,542
        10         20         30         40         50         60 
MRFGVLISVF VAIVSALPLQ EGPLNKRAYP SFEAYSNYKV DRTDLETFLD KQKDVSLYYL 

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

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

       190        200        210        220        230        240 
ISRYLNDVNS LNKGKLVLTD 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 YKLVYDAKSA SNDITINKIN 

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

       490        500        510 
LNEQLNRNTG YSTSAYSLTW SSGALLEAIR LRNKVKALA 

« Hide

References

[1]"The nucleotide sequence of the glucoamylase gene GLA1 from Saccharomycopsis fibuligera KZ."
Hostinova E., Balanova J., Gasperik J.
FEMS Microbiol. Lett. 67:103-108(1991) [PubMed: 1840532] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: KZ.
[2]Hostinova E.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
Strain: KZ.

Cross-references

Sequence databases

X58117 Genomic DNA. Translation: CAA41120.1.

3D structure databases

HSSPHSSP built from PDB template 1AYX based on UniProtKB P08017.
SMRP26989. Positions 28-519.
ModBaseSearch...

Protein family/group databases

CAZyGH15. Glycoside Hydrolase Family 15.

Enzyme and pathway databases

BRENDA3.2.1.3. 97837.

Family and domain databases

InterProIPR012341. 6hp_glycosidase.
IPR000165. Glyco_hydro_15.
IPR011613. Glyco_hydro_15_rel.
[Graphical view]
Gene3DG3DSA:1.50.10.10. CelA/Cel48F_cat. 1 hit.
PfamPF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PRINTSPR00736. GLHYDRLASE15.
PROSITEPS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYH_SACFI
AccessionPrimary (citable) accession number: P26989
Secondary accession number(s): P78745
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1998
Last modified: June 16, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (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

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