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Protein

Glucoamylase GLU1

Gene

GLU1

Organism
Saccharomycopsis fibuligera (Yeast)
Status
Reviewed-Annotation score: Annotation score: 2 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 sitei166SubstrateBy similarity1
Active sitei234Proton acceptorPROSITE-ProRule annotation1
Active sitei237Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.3. 2072.

Protein family/group databases

CAZyiGH15. Glycoside Hydrolase Family 15.
mycoCLAPiGLA15A_SACFI.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucoamylase GLU1 (EC:3.2.1.3)
Alternative name(s):
1,4-alpha-D-glucan glucohydrolase
Glucan 1,4-alpha-glucosidase
Gene namesi
Name:GLU1
OrganismiSaccharomycopsis fibuligera (Yeast)
Taxonomic identifieri4944 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycopsidaceaeSaccharomycopsis

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Add BLAST27
ChainiPRO_000000147528 – 519Glucoamylase GLU1Add BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi115N-linked (GlcNAc...)Sequence analysis1
Glycosylationi127N-linked (GlcNAc...)Sequence analysis1
Glycosylationi205N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1519
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi45 – 62Combined sources18
Beta strandi69 – 71Combined sources3
Beta strandi85 – 89Combined sources5
Beta strandi92 – 94Combined sources3
Helixi95 – 111Combined sources17
Turni112 – 114Combined sources3
Helixi116 – 133Combined sources18
Helixi145 – 151Combined sources7
Helixi173 – 191Combined sources19
Helixi209 – 215Combined sources7
Helixi217 – 227Combined sources11
Helixi244 – 263Combined sources20
Helixi267 – 285Combined sources19
Turni287 – 289Combined sources3
Turni294 – 297Combined sources4
Helixi303 – 307Combined sources5
Helixi317 – 325Combined sources9
Turni328 – 330Combined sources3
Helixi341 – 357Combined sources17
Helixi359 – 361Combined sources3
Beta strandi365 – 367Combined sources3
Beta strandi380 – 385Combined sources6
Helixi390 – 410Combined sources21
Beta strandi414 – 417Combined sources4
Helixi418 – 420Combined sources3
Helixi421 – 427Combined sources7
Helixi431 – 433Combined sources3
Helixi438 – 440Combined sources3
Beta strandi441 – 446Combined sources6
Helixi451 – 474Combined sources24
Beta strandi483 – 485Combined sources3
Turni487 – 489Combined sources3
Beta strandi492 – 495Combined sources4
Helixi499 – 516Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYXX-ray1.70A28-519[»]
2F6DX-ray1.60A28-519[»]
2FBAX-ray1.10A28-519[»]
ProteinModelPortaliP08017.
SMRiP08017.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08017.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 15 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR000165. Glucoamylase.
IPR011613. Glyco_hydro_15/PHK.
[Graphical view]
PfamiPF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PRINTSiPR00736. GLHYDRLASE15.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08017-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFGVLFSVF AAIVSALPLQ EGPLNKRAYP SFEAYSNYKV DRTDLETFLD
60 70 80 90 100
KQKEVSLYYL LQNIAYPEGQ FNNGVPGTVI ASPSTSNPDY YYQWTRDSAI
110 120 130 140 150
TFLTVLSELE DNNFNTTLAK AVEYYINTSY NLQRTSNPSG SFDDENHKGL
160 170 180 190 200
GEPKFNTDGS AYTGAWGRPQ NDGPALRAYA ISRYLNDVNS LNEGKLVLTD
210 220 230 240 250
SGDINFSSTE DIYKNIIKPD LEYVIGYWDS TGFDLWEENQ GRHFFTSLVQ
260 270 280 290 300
QKALAYAVDI AKSFDDGDFA NTLSSTASTL ESYLSGSDGG FVNTDVNHIV
310 320 330 340 350
ENPDLLQQNS RQGLDSATYI GPLLTHDIGE SSSTPFDVDN EYVLQSYYLL
360 370 380 390 400
LEDNKDRYSV NSAYSAGAAI GRYPEDVYNG DGSSEGNPWF LATAYAAQVP
410 420 430 440 450
YKLAYDAKSA SNDITINKIN YDFFNKYIVD LSTINSAYQS SDSVTIKSGS
460 470 480 490 500
DEFNTVADNL VTFGDSFLQV ILDHINDDGS LNEQLNRYTG YSTGAYSLTW
510
SSGALLEAIR LRNKVKALA
Length:519
Mass (Da):57,539
Last modified:August 1, 1988 - v1
Checksum:iBE73035AD1B77652
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25641 mRNA. Translation: AAA83997.1.
M17355 Genomic DNA. Translation: AAA34649.1.
PIRiA54549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25641 mRNA. Translation: AAA83997.1.
M17355 Genomic DNA. Translation: AAA34649.1.
PIRiA54549.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYXX-ray1.70A28-519[»]
2F6DX-ray1.60A28-519[»]
2FBAX-ray1.10A28-519[»]
ProteinModelPortaliP08017.
SMRiP08017.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH15. Glycoside Hydrolase Family 15.
mycoCLAPiGLA15A_SACFI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.1.3. 2072.

Miscellaneous databases

EvolutionaryTraceiP08017.

Family and domain databases

Gene3Di1.50.10.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR000165. Glucoamylase.
IPR011613. Glyco_hydro_15/PHK.
[Graphical view]
PfamiPF00723. Glyco_hydro_15. 1 hit.
[Graphical view]
PRINTSiPR00736. GLHYDRLASE15.
SUPFAMiSSF48208. SSF48208. 1 hit.
PROSITEiPS00820. GLUCOAMYLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMYG_SACFI
AccessioniPrimary (citable) accession number: P08017
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 2, 2016
This is version 92 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

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.