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P22832

- AMYG_ASPSH

UniProt

P22832 - AMYG_ASPSH

Protein

Glucoamylase

Gene

glaA

Organism
Aspergillus shirousami
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      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 sitei143 – 1431SubstrateBy similarity
    Active sitei199 – 1991Proton acceptorPROSITE-ProRule annotation
    Active sitei202 – 2021Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. glucan 1,4-alpha-glucosidase activity Source: UniProtKB-EC
    2. starch binding Source: InterPro

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    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.
    mycoCLAPiGLA15A_ASPSH.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucoamylase (EC:3.2.1.3)
    Alternative name(s):
    1,4-alpha-D-glucan glucohydrolase
    Glucan 1,4-alpha-glucosidase
    Gene namesi
    Name:glaA
    Synonyms:gla
    OrganismiAspergillus shirousami
    Taxonomic identifieri5070 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 246By similarityPRO_0000001467
    Chaini25 – 639615GlucoamylasePRO_0000001468Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi194 – 1941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi233 ↔ 236By similarity
    Disulfide bondi245 ↔ 472By similarity
    Disulfide bondi285 ↔ 293By similarity
    Glycosylationi418 – 4181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi464 – 4641O-linked (Man)By similarity
    Glycosylationi466 – 4661O-linked (Man)By similarity
    Glycosylationi467 – 4671O-linked (Man)By similarity
    Glycosylationi475 – 4751O-linked (Man)By similarity
    Glycosylationi476 – 4761O-linked (Man)By similarity
    Glycosylationi482 – 4821O-linked (Man)By similarity
    Glycosylationi483 – 4831O-linked (Man)By similarity
    Glycosylationi485 – 4851O-linked (Man)By similarity
    Glycosylationi487 – 4871O-linked (Man)By similarity
    Glycosylationi488 – 4881O-linked (Man)By similarity
    Glycosylationi491 – 4911O-linked (Man)By similarity
    Glycosylationi495 – 4951O-linked (Man)By similarity
    Glycosylationi498 – 4981O-linked (Man)By similarity
    Glycosylationi499 – 4991O-linked (Man)By similarity
    Glycosylationi500 – 5001O-linked (Man)By similarity
    Glycosylationi501 – 5011O-linked (Man)By similarity
    Glycosylationi503 – 5031O-linked (Man)By similarity
    Glycosylationi505 – 5051O-linked (Man)By similarity
    Glycosylationi507 – 5071O-linked (Man)By similarity
    Glycosylationi511 – 5111O-linked (Man)By similarity
    Glycosylationi512 – 5121O-linked (Man)By similarity
    Glycosylationi513 – 5131O-linked (Man)By similarity
    Glycosylationi514 – 5141O-linked (Man)By similarity
    Glycosylationi516 – 5161O-linked (Man)By similarity
    Glycosylationi517 – 5171O-linked (Man)By similarity
    Glycosylationi519 – 5191O-linked (Man)By similarity
    Glycosylationi521 – 5211O-linked (Man)By similarity
    Glycosylationi523 – 5231O-linked (Man)By similarity
    Glycosylationi524 – 5241O-linked (Man)By similarity
    Glycosylationi525 – 5251O-linked (Man)By similarity
    Glycosylationi527 – 5271O-linked (Man)By similarity
    Glycosylationi528 – 5281O-linked (Man)By similarity
    Glycosylationi529 – 5291O-linked (Man)By similarity
    Glycosylationi530 – 5301O-linked (Man)By similarity
    Glycosylationi531 – 5311O-linked (Man)By similarity
    Glycosylationi533 – 5331O-linked (Man)By similarity
    Glycosylationi534 – 5341O-linked (Man)By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP22832.
    SMRiP22832. Positions 25-639.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini532 – 639108CBM20PROSITE-ProRule annotationAdd
    BLAST

    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.
    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.

    P22832-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSFRSLLALS GLVCSGLASV ISKRATLDSW LSNEATVART AILNNIGADG    50
    AWVSGADSGI VVASPSTDNP DYFYTWTRDS GIVLKTLVDL FRNGDTDLLS 100
    TIEHYISSQA IIQGVSNPSG DLSSGGLGEP KFNVDETAYA GSWGRPQRDG 150
    PALRATAMIG FGQWLLDNGY TSAATEIVWP LVRNDLSYVA QYWNQTGYDL 200
    WEEVNGSSFF TIAVQHRALV EGSAFATAVG SSCSWCDSQA PQILCYLQSF 250
    WTGSYILANF DSSRSGKDTN TLLGSIHTFD PEAGCDDSTF QPCSPRALAN 300
    HKEVVDSFRS IYTLNDGLSD SEAVAVGRYP EDSYYNGNPW FLCTLAAAEQ 350
    LYDALYQWDK QGSLEITDVS LDFFKALYSG AATGTYSSSS STYSSIVSAV 400
    KTFADGFVSI VETHAASNGS LSEQFDKSDG DELSARDLTW SYAALLTANN 450
    RRNSVVPPSW GETSASSVPG TCAATSASGT YSSVTVTSWP SIVATGGTTT 500
    TATTTGSGGV TSTSKTTTTA SKTSTTTSST SCTTPTAVAV TFDLTATTTY 550
    GENIYLVGSI SQLGDWETSD GIALSADKYT SSNPPWYVTV TLPAGESFEY 600
    KFIRVESDDS VEWESDPNRE YTVPQACGES TATVTDTWR 639
    Length:639
    Mass (Da):68,131
    Last modified:August 1, 1991 - v1
    Checksum:iE93DAE55EED72326
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10460 Genomic DNA. Translation: BAA01254.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10460 Genomic DNA. Translation: BAA01254.1 .

    3D structure databases

    ProteinModelPortali P22832.
    SMRi P22832. Positions 25-639.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM20. Carbohydrate-Binding Module Family 20.
    GH15. Glycoside Hydrolase Family 15.
    mycoCLAPi GLA15A_ASPSH.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 1.50.10.10. 1 hit.
    2.60.40.10. 1 hit.
    InterProi IPR008928. 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 ]
    Pfami PF00686. CBM_20. 1 hit.
    PF00723. Glyco_hydro_15. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001031. Glu-a-glcsd_SBD. 1 hit.
    PRINTSi PR00736. GLHYDRLASE15.
    SMARTi SM01065. CBM_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48208. SSF48208. 1 hit.
    SSF49452. SSF49452. 1 hit.
    PROSITEi PS51166. CBM20. 1 hit.
    PS00820. GLUCOAMYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the glucoamylase gene of Aspergillus shirousami and its expression in Aspergillus oryzae."
      Shibuya I., Gomi K., Iimura Y., Takahashi K., Tamura G., Hara S.
      Agric. Biol. Chem. 54:1905-1914(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiAMYG_ASPSH
    AccessioniPrimary (citable) accession number: P22832
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

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

    External Data

    Dasty 3