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P08017

- AMYG_SACFI

UniProt

P08017 - AMYG_SACFI

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Protein

Glucoamylase GLU1

Gene

GLU1

Organism
Saccharomycopsis fibuligera (Yeast)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei166 – 1661SubstrateBy similarity
Active sitei234 – 2341Proton acceptorPROSITE-ProRule annotation
Active sitei237 – 2371Proton donorPROSITE-ProRule annotation

GO - Molecular functioni

  1. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

BRENDAi3.2.1.3. 5499.

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 519492Glucoamylase GLU1PRO_0000001475Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

Secondary structure

1
519
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi45 – 6218
Beta strandi69 – 713
Beta strandi85 – 895
Beta strandi92 – 943
Helixi95 – 11117
Turni112 – 1143
Helixi116 – 13318
Helixi145 – 1517
Helixi173 – 19119
Helixi209 – 2157
Helixi217 – 22711
Helixi244 – 26320
Helixi267 – 28519
Turni287 – 2893
Turni294 – 2974
Helixi303 – 3075
Helixi317 – 3259
Turni328 – 3303
Helixi341 – 35717
Helixi359 – 3613
Beta strandi365 – 3673
Beta strandi380 – 3856
Helixi390 – 41021
Beta strandi414 – 4174
Helixi418 – 4203
Helixi421 – 4277
Helixi431 – 4333
Helixi438 – 4403
Beta strandi441 – 4466
Helixi451 – 47424
Beta strandi483 – 4853
Turni487 – 4893
Beta strandi492 – 4954
Helixi499 – 51618

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AYXX-ray1.70A28-519[»]
2F6DX-ray1.60A28-519[»]
2FBAX-ray1.10A28-519[»]
ProteinModelPortaliP08017.
SMRiP08017. Positions 28-519.
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.
[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:
EMBL
GenBank
DDBJ
Links Updated
L25641 mRNA. Translation: AAA83997.1.
M17355 Genomic DNA. Translation: AAA34649.1.
PIRiA54549.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L25641 mRNA. Translation: AAA83997.1 .
M17355 Genomic DNA. Translation: AAA34649.1 .
PIRi A54549.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AYX X-ray 1.70 A 28-519 [» ]
2F6D X-ray 1.60 A 28-519 [» ]
2FBA X-ray 1.10 A 28-519 [» ]
ProteinModelPortali P08017.
SMRi P08017. Positions 28-519.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH15. Glycoside Hydrolase Family 15.
mycoCLAPi GLA15A_SACFI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.2.1.3. 5499.

Miscellaneous databases

EvolutionaryTracei P08017.

Family and domain databases

Gene3Di 1.50.10.10. 1 hit.
InterProi IPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR000165. Glucoamylase.
IPR011613. Glyco_hydro_15.
[Graphical view ]
Pfami PF00723. Glyco_hydro_15. 1 hit.
[Graphical view ]
PRINTSi PR00736. GLHYDRLASE15.
SUPFAMi SSF48208. SSF48208. 1 hit.
PROSITEi PS00820. GLUCOAMYLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the glucoamylase gene GLU1 in the yeast Saccharomycopsis fibuligera."
    Itoh T., Ohtsuki I., Yamashita I., Fukui S.
    J. Bacteriol. 169:4171-4176(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Structure of glucoamylase from Saccharomycopsis fibuligera at 1.7-A resolution."
    Sevcik J., Solovicova A., Hostinova E., Gasperik J., Wilson K.S., Dauter Z.
    Acta Crystallogr. D 54:854-866(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

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: October 1, 2014
This is version 84 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

External Data

Dasty 3