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P08017

- AMYG_SACFI

UniProt

P08017 - AMYG_SACFI

Protein

Glucoamylase GLU1

Gene

GLU1

Organism
Saccharomycopsis fibuligera (Yeast)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      Previous versions | rss
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    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

    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

    MKFGVLFSVF AAIVSALPLQ EGPLNKRAYP SFEAYSNYKV DRTDLETFLD    50
    KQKEVSLYYL LQNIAYPEGQ FNNGVPGTVI ASPSTSNPDY YYQWTRDSAI 100
    TFLTVLSELE DNNFNTTLAK AVEYYINTSY NLQRTSNPSG SFDDENHKGL 150
    GEPKFNTDGS AYTGAWGRPQ NDGPALRAYA ISRYLNDVNS LNEGKLVLTD 200
    SGDINFSSTE DIYKNIIKPD LEYVIGYWDS TGFDLWEENQ GRHFFTSLVQ 250
    QKALAYAVDI AKSFDDGDFA NTLSSTASTL ESYLSGSDGG FVNTDVNHIV 300
    ENPDLLQQNS RQGLDSATYI GPLLTHDIGE SSSTPFDVDN EYVLQSYYLL 350
    LEDNKDRYSV NSAYSAGAAI GRYPEDVYNG DGSSEGNPWF LATAYAAQVP 400
    YKLAYDAKSA SNDITINKIN YDFFNKYIVD LSTINSAYQS SDSVTIKSGS 450
    DEFNTVADNL VTFGDSFLQV ILDHINDDGS LNEQLNRYTG YSTGAYSLTW 500
    SSGALLEAIR LRNKVKALA 519
    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