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P23176 (AMYG_ASPKA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. 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 I

EC=3.2.1.3
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene names
Name:gaI
OrganismAspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi)
Taxonomic identifier40384 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length639 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818
Propeptide19 – 246
PRO_0000001463
Chain25 – 639615Glucoamylase I
PRO_0000001464

Regions

Domain532 – 639108CBM20
Region494 – 53138Raw-starch-adsorbable GP-I sequence

Sites

Active site1991Proton acceptor By similarity
Active site2021Proton donor By similarity
Binding site1431Substrate By similarity

Amino acid modifications

Glycosylation1941N-linked (GlcNAc...) By similarity
Glycosylation4181N-linked (GlcNAc...) By similarity
Glycosylation4641O-linked (Man) By similarity
Glycosylation4661O-linked (Man) By similarity
Glycosylation4671O-linked (Man) By similarity
Glycosylation4751O-linked (Man) By similarity
Glycosylation4761O-linked (Man) By similarity
Glycosylation4821O-linked (Man) By similarity
Glycosylation4831O-linked (Man) By similarity
Glycosylation4851O-linked (Man) By similarity
Glycosylation4871O-linked (Man) By similarity
Glycosylation4911O-linked (Man) By similarity
Glycosylation4951O-linked (Man) By similarity
Glycosylation4981O-linked (Man) By similarity
Glycosylation4991O-linked (Man) By similarity
Glycosylation5001O-linked (Man) By similarity
Glycosylation5011O-linked (Man) By similarity
Glycosylation5031O-linked (Man) By similarity
Glycosylation5051O-linked (Man) By similarity
Glycosylation5071O-linked (Man) By similarity
Glycosylation5111O-linked (Man) By similarity
Glycosylation5121O-linked (Man) By similarity
Glycosylation5131O-linked (Man) By similarity
Glycosylation5141O-linked (Man) By similarity
Glycosylation5161O-linked (Man) By similarity
Glycosylation5171O-linked (Man) By similarity
Glycosylation5191O-linked (Man) By similarity
Glycosylation5211O-linked (Man) By similarity
Glycosylation5231O-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
Glycosylation5331O-linked (Man) By similarity
Glycosylation5341O-linked (Man) By similarity
Disulfide bond233 ↔ 236 By similarity
Disulfide bond245 ↔ 472 By similarity
Disulfide bond285 ↔ 293 By similarity

Sequences

Sequence LengthMass (Da)Tools
P23176 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: E112B31A4DD8DD6B

FASTA63968,272
        10         20         30         40         50         60 
MSFRSLLALS GLVCSGLANV ISKRATLDSW LSNEATVART AILNNIGADG AWVSGADSGI 

        70         80         90        100        110        120 
VVASPSTDNP DYFYTWTRDS GLVIKTLVDL FRNGDTDLLS TIEHYISSQA IIQGVSNPSG 

       130        140        150        160        170        180 
DLSSGGLGEP KFNVDETAYT GSWGRPQRDG PALRATAMIG FGQVLLDNGY TSAATEIVWP 

       190        200        210        220        230        240 
LVRNDLSYVA QYWNQTGYDL WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA 

       250        260        270        280        290        300 
PQILCYLQSF WTGSYILANF DSRRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN 

       310        320        330        340        350        360 
HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FQSTLAAAEQ LYDALYQWDK 

       370        380        390        400        410        420 
QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV KTFADGFVSI VETHAASNGS 

       430        440        450        460        470        480 
LSEQFDKSDG DELSARDLTW SYAALLTANN RRNSVVPPSW GETSASSWPG TCAATSASGT 

       490        500        510        520        530        540 
YSSVTVTSWP SIVATGGTTT TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV 

       550        560        570        580        590        600 
TFDLTATTTY GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPLWYVTV TLPAGESFEY 

       610        620        630 
KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR 

« Hide

References

[1]"Molecular cloning of the glucoamylase I gene of Aspergillus awamori var. kawachi for localization of the raw-starch-affinity site."
Hayashida S., Kuroda K., Ohta K., Kuhara S., Fukuda K., Sakaki Y.
Agric. Biol. Chem. 53:923-929(1989)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Structure of the raw-starch-affinity site on the Aspergillus awamori var. kawachi glucoamylase I molecule."
Hayashida S., Nakahara K., Kuroda K., Miyata T., Iwanaga S.
Agric. Biol. Chem. 53:135-141(1989)
Cited for: PROTEIN SEQUENCE OF 494-538.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00427 Genomic DNA. Translation: BAA00331.1.
PIRJT0479.

3D structure databases

ProteinModelPortalP23176.
SMRP23176. Positions 25-639.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

PTM databases

UniCarbKBP23176.

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.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMYG_ASPKA
AccessionPrimary (citable) accession number: P23176
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 11, 2014
This is version 94 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