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P22861 (AMYG_SCHOC) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 1

EC=3.2.1.3
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene names
Name:GAM1
OrganismSchwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis)
Taxonomic identifier27300 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeSchwanniomyces

Protein attributes

Sequence length958 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This glucoamylase has a specificity toward both alpha-1,4 and alpha-1,6 linkages.

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.

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 31 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

glucan 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 – 2222 Potential
Chain23 – 958936Glucoamylase 1
PRO_0000018586

Regions

Compositional bias26 – 4116Ser-rich
Compositional bias530 – 54213Ser/Thr-rich

Sites

Active site4701 By similarity
Active site4731 By similarity
Active site6381Proton donor By similarity

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation781N-linked (GlcNAc...) Potential
Glycosylation1071N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation5131N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential
Glycosylation6021N-linked (GlcNAc...) Potential
Glycosylation8131N-linked (GlcNAc...) Potential
Glycosylation9071N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P22861 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 47938DB9BC308260

FASTA958106,508
        10         20         30         40         50         60 
MIFLKLIKSI VIGLGLVSAI QAAPASSIGS SASASSSSES SQATIPNDVT LGVKQIPNIF 

        70         80         90        100        110        120 
NDSAVDANAA AKGYDLVNVT NTPRGLTGIL KLKEATNIYG YDFDYLNLTV EYQADTRLNV 

       130        140        150        160        170        180 
HIEPTDLSDV FVLPEHLVVK PLVEGDAQSY NFDNSDLVFE YSNTDFSFEV IRSSTKEVLF 

       190        200        210        220        230        240 
STKGNPLVFS NQFIQFNSSL PKNHVITGLG ESIHGLVNEP GSVKTLFAND VGDPIDGNIY 

       250        260        270        280        290        300 
GVHPVYLDQR YDTETTHAVY WRTSAIQEVL IGEESITWRA LSGVIDLYFF SGPTPKDAIQ 

       310        320        330        340        350        360 
QYVKEIGLPA FQPYWSLGYH QCRWGYDTIE KLSEVVENFK KFNIPLETIW SDIDYMDSYK 

       370        380        390        400        410        420 
DFTYDPHRFP LDEYRKFLDE LHKNNQHYVP ILDAAIYVPN PNNATDNEYQ PFHYGNETDV 

       430        440        450        460        470        480 
FLKNPDGSLY IGAVWQVTLF SRFLSRKHSD MDKVIKDWYE LTPFDGIWAD MNEVSSFCVG 

       490        500        510        520        530        540 
SCGTGKYFEN PAYPPFTVGS KATSYPVGFD VSNASEWKSI QSSISATAKT SSTSSVSSSS 

       550        560        570        580        590        600 
STIDYMNTLA PGKGNINYPP YAIYNMQGDS DLATHAVSPN ATHADGTVEY DIHNLYGYLQ 

       610        620        630        640        650        660 
ENATYHALLE VFPNKRPFMI SRSTFPRAGK WTGHWGGDNT ADWAYAYFSI PQAFSMGIAG 

       670        680        690        700        710        720 
LPFFGADVCG FNGNSDSELC SRWMQLGSFF PFYRNHNYLG AIDQEPYVWE SVAEATRTSM 

       730        740        750        760        770        780 
AIRYLLLPYY YTLLHESHTT GLPILRAFSW QFPNDRSLSG VDNQFFVGDG LVVTPVLEPG 

       790        800        810        820        830        840 
VDKVKGVFPG AGKEEVYYDW YTQREVHFKD GKNETLDAPL GHIPLHIRGG NVLPTQEPGY 

       850        860        870        880        890        900 
TVAESRQNPF GLIVALDNDG KAQGSLYLDD GESLVVDSSL LVSFSVSDNT LSASPSGDYK 

       910        920        930        940        950 
ADQPLANVTI LGVGHKPKSV KFENANVDFT YKKSTVFVTG LDKYTKDGAF SKDFTITW 

« Hide

References

[1]"Cloning of the Schwanniomyces occidentalis glucoamylase gene (GAM1) and its expression in Saccharomyces cerevisiae."
Dohmen R.J., Strasser A.W.M., Dahlems U.M., Hollenberg C.P.
Gene 95:111-121(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 26076 / DSM 3794 / CBS 2864 / BCRC 22059 / NCYC 954 / NRRL Y-2470.
[2]"Striking structural and functional similarities suggest that intestinal sucrase-isomaltase, human lysosomal alpha-glucosidase and Schwanniomyces occidentalis glucoamylase are derived from a common ancestral gene."
Naim H.Y., Niermann T., Kleinhans U., Hollenberg C.P., Strasser A.W.M.
FEBS Lett. 294:109-112(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO OTHER FAMILY 31 MEMBERS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60207 Genomic DNA. Translation: AAA33923.1.
PIRJN0102.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH31. Glycoside Hydrolase Family 31.
mycoCLAPGLA31A_DEBOC.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR011013. Gal_mutarotase_SF_dom.
IPR000322. Glyco_hydro_31.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF01055. Glyco_hydro_31. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 2 hits.
SSF74650. SSF74650. 1 hit.
PROSITEPS00129. GLYCOSYL_HYDROL_F31_1. 1 hit.
PS00707. GLYCOSYL_HYDROL_F31_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYG_SCHOC
AccessionPrimary (citable) accession number: P22861
Secondary accession number(s): Q92336
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: October 16, 2013
This is version 56 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries