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Protein

Glucoamylase I

Gene

gaI

Organism
Aspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei143SubstrateBy similarity1
Active sitei199Proton acceptorPROSITE-ProRule annotation1
Active sitei202Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase I (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:gaI
OrganismiAspergillus kawachii (White koji mold) (Aspergillus awamori var. kawachi)
Taxonomic identifieri40384 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Add BLAST18
PropeptideiPRO_000000146319 – 246
ChainiPRO_000000146425 – 639Glucoamylase IAdd BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi194N-linked (GlcNAc...)By similarity1
Disulfide bondi233 ↔ 236By similarity
Disulfide bondi245 ↔ 472By similarity
Disulfide bondi285 ↔ 293By similarity
Glycosylationi418N-linked (GlcNAc...)By similarity1
Glycosylationi464O-linked (Man)By similarity1
Glycosylationi466O-linked (Man)By similarity1
Glycosylationi467O-linked (Man)By similarity1
Glycosylationi475O-linked (Man)By similarity1
Glycosylationi476O-linked (Man)By similarity1
Glycosylationi482O-linked (Man)By similarity1
Glycosylationi483O-linked (Man)By similarity1
Glycosylationi485O-linked (Man)By similarity1
Glycosylationi487O-linked (Man)By similarity1
Glycosylationi491O-linked (Man)By similarity1
Glycosylationi495O-linked (Man)By similarity1
Glycosylationi498O-linked (Man)By similarity1
Glycosylationi499O-linked (Man)By similarity1
Glycosylationi500O-linked (Man)By similarity1
Glycosylationi501O-linked (Man)By similarity1
Glycosylationi503O-linked (Man)By similarity1
Glycosylationi505O-linked (Man)By similarity1
Glycosylationi507O-linked (Man)By similarity1
Glycosylationi511O-linked (Man)By similarity1
Glycosylationi512O-linked (Man)By similarity1
Glycosylationi513O-linked (Man)By similarity1
Glycosylationi514O-linked (Man)By similarity1
Glycosylationi516O-linked (Man)By similarity1
Glycosylationi517O-linked (Man)By similarity1
Glycosylationi519O-linked (Man)By similarity1
Glycosylationi521O-linked (Man)By similarity1
Glycosylationi523O-linked (Man)By similarity1
Glycosylationi524O-linked (Man)By similarity1
Glycosylationi525O-linked (Man)By similarity1
Glycosylationi526O-linked (Man)By similarity1
Glycosylationi527O-linked (Man)By similarity1
Glycosylationi528O-linked (Man)By similarity1
Glycosylationi529O-linked (Man)By similarity1
Glycosylationi530O-linked (Man)By similarity1
Glycosylationi531O-linked (Man)By similarity1
Glycosylationi533O-linked (Man)By similarity1
Glycosylationi534O-linked (Man)By similarity1

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

PTM databases

UniCarbKBiP23176.

Structurei

3D structure databases

ProteinModelPortaliP23176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini532 – 639CBM20PROSITE-ProRule annotationAdd BLAST108

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni494 – 531Raw-starch-adsorbable GP-I sequenceAdd BLAST38

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated
Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR011613. Glyco_hydro_15/PHK.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFiPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSiPR00736. GLHYDRLASE15.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23176-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFRSLLALS GLVCSGLANV ISKRATLDSW LSNEATVART AILNNIGADG
60 70 80 90 100
AWVSGADSGI VVASPSTDNP DYFYTWTRDS GLVIKTLVDL FRNGDTDLLS
110 120 130 140 150
TIEHYISSQA IIQGVSNPSG DLSSGGLGEP KFNVDETAYT GSWGRPQRDG
160 170 180 190 200
PALRATAMIG FGQVLLDNGY TSAATEIVWP LVRNDLSYVA QYWNQTGYDL
210 220 230 240 250
WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA PQILCYLQSF
260 270 280 290 300
WTGSYILANF DSRRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN
310 320 330 340 350
HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FQSTLAAAEQ
360 370 380 390 400
LYDALYQWDK QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV
410 420 430 440 450
KTFADGFVSI VETHAASNGS LSEQFDKSDG DELSARDLTW SYAALLTANN
460 470 480 490 500
RRNSVVPPSW GETSASSWPG TCAATSASGT YSSVTVTSWP SIVATGGTTT
510 520 530 540 550
TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV TFDLTATTTY
560 570 580 590 600
GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPLWYVTV TLPAGESFEY
610 620 630
KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR
Length:639
Mass (Da):68,272
Last modified:November 1, 1991 - v1
Checksum:iE112B31A4DD8DD6B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00427 Genomic DNA. Translation: BAA00331.1.
PIRiJT0479.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00427 Genomic DNA. Translation: BAA00331.1.
PIRiJT0479.

3D structure databases

ProteinModelPortaliP23176.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.
GH15. Glycoside Hydrolase Family 15.

PTM databases

UniCarbKBiP23176.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
2.60.40.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000165. Glucoamylase.
IPR008291. Glucoamylase_SBD.
IPR011613. Glyco_hydro_15/PHK.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00686. CBM_20. 1 hit.
PF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PIRSFiPIRSF001031. Glu-a-glcsd_SBD. 1 hit.
PRINTSiPR00736. GLHYDRLASE15.
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 1 hit.
SSF49452. SSF49452. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMYG_ASPKA
AccessioniPrimary (citable) accession number: P23176
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 5, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.