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Q03045 (AMYG_HORRE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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 P

EC=3.2.1.3
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene names
Name:GAMP
OrganismHormoconis resinae (Creosote fungus) (Amorphotheca resinae)
Taxonomic identifier5101 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesLeotiomycetes incertae sedisMyxotrichaceaeAmorphotheca

Protein attributes

Sequence length616 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.

Subcellular location

Secreted.

Sequence similarities

Belongs to the glycosyl hydrolase 15 family.

Contains 1 CBM20 (carbohydrate binding type-20) domain.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 616587Glucoamylase P
PRO_0000001471

Regions

Domain501 – 608108CBM20

Sites

Active site2051Proton acceptor By similarity
Active site2081Proton donor By similarity
Binding site1491Substrate By similarity

Amino acid modifications

Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation4271N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q03045 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: B5F4DC8EEBB152FB

FASTA61666,432
        10         20         30         40         50         60 
MRLLPSSCAG ALSLLCSLAI AAPTELKARD LSSFIASERA IALQGALNNI GPDGSAVPGA 

        70         80         90        100        110        120 
GAGFVVASPS KANPDYFYTW SRDSALTLKM IIDEFILGNT TLQTIIEQYI HAQAVLQTVS 

       130        140        150        160        170        180 
NPSGTFLPDG VGLGEPKFMV DGTRFNGPWG RPQRDGPALR AIALMTYSNW LIKNGQFAEA 

       190        200        210        220        230        240 
KTKIWPIIAN DLSYVGQYWN QSGFDLWEET YASSFFTIQN QHRALVEGAQ LAHDLGVTCT 

       250        260        270        280        290        300 
GCDQAPEVLC FLQSFWNGKY IVSNINVNNG RTGLDGNSIL GAISTFDIDA YCDSPTLQPC 

       310        320        330        340        350        360 
HSQSLANFKV LTDTFRNLYT INAGIPEGQG VAVGRYAEDV YMGGNPWYLI TTAAAEFLYD 

       370        380        390        400        410        420 
AVAQWKARHV LTVDETSLAF FKDIYPEVTV REYKSGNANS PFAQIMDAVT AYADSYVAIA 

       430        440        450        460        470        480 
EKYIPSNGSL SEQFNRDTGT PLSAIDLTWS YAAFITMSQR RAGQYPSSWG SRNALPPPTT 

       490        500        510        520        530        540 
CSASSTPGIY TPATAAGAPN VTSSCQVSIT FNINATTYYG ENLYVIGNSS DLGAWNIADA 

       550        560        570        580        590        600 
YPLSASAYTQ DRPLWSAAIP LNAGEVISYQ YVRQEDCDQP YIYETVNRTL TVPACGGAAV 

       610 
TTDDAWMGPV GSSGNC 

« Hide

References

[1]"Glucoamylase P gene of Hormoconis resinae: molecular cloning, sequencing and introduction into Trichoderma reesei."
Joutsjoki V.V., Torkkeli T.K.
FEMS Microbiol. Lett. 78:237-243(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 20495 / CBS 174.61 / NRRL 6437.
[2]"Cloning and expression of Hormoconis resinae glucoamylase P cDNA in Saccharomyces cerevisiae."
Vainio A.E.I., Torkkeli H.T., Tuusa T., Aho S.A., Fagerstroem B.R., Korhola M.P.
Curr. Genet. 24:38-44(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ATCC 20495 / CBS 174.61 / NRRL 6437.
[3]"Comparison of two glucoamylases from Hormoconis resinae."
Fagerstroem R., Vainio A.E.I., Suoranta K., Pakula T., Kalkkinen N., Torkkeli H.T.
J. Gen. Microbiol. 136:913-920(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 72-76, CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68143 Genomic DNA. Translation: CAA48243.1.
X67708 mRNA. Translation: CAA47945.1.
PIRS33908.

3D structure databases

ProteinModelPortalQ03045.
SMRQ03045. Positions 30-503.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.
mycoCLAPGLA15P_HORRE.

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.
IPR011613. Glyco_hydro_15.
IPR013783. Ig-like_fold.
[Graphical view]
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYG_HORRE
AccessionPrimary (citable) accession number: Q03045
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 81 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