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P07683

- AMYG_RHIOR

UniProt

P07683 - AMYG_RHIOR

Protein

Glucoamylase 1

Gene
N/A
Organism
Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 Nov 1995)
      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 sitei279 – 2791SubstrateBy similarity
    Active sitei336 – 3361Proton acceptorPROSITE-ProRule annotation
    Active sitei339 – 3391Proton 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

    Protein family/group databases

    CAZyiCBM21. Carbohydrate-Binding Module Family 21.
    GH15. Glycoside Hydrolase Family 15.
    mycoCLAPiGLA15E_RHIOR.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glucoamylase 1 (EC:3.2.1.3)
    Short name:
    Gluc 1
    Alternative name(s):
    1,4-alpha-D-glucan glucohydrolase
    Glucan 1,4-alpha-glucosidase
    Cleaved into the following 2 chains:
    Glucoamylase 2
    Short name:
    Gluc 2
    Glucoamylase 3
    Short name:
    Gluc 3
    OrganismiRhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar)
    Taxonomic identifieri64495 [NCBI]
    Taxonomic lineageiEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Add
    BLAST
    Chaini26 – 604579Glucoamylase 1PRO_0000001472Add
    BLAST
    Chaini116 – 604489Glucoamylase 3PRO_0000001473Add
    BLAST
    Chaini159 – 604446Glucoamylase 2PRO_0000001474Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi167 – 1671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Structurei

    Secondary structure

    1
    604
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi30 – 4415
    Beta strandi46 – 527
    Beta strandi55 – 573
    Beta strandi59 – 679
    Beta strandi78 – 803
    Beta strandi82 – 865
    Beta strandi93 – 997
    Beta strandi102 – 11514
    Beta strandi117 – 1204
    Beta strandi122 – 1254

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DJMNMR-A26-131[»]
    ProteinModelPortaliP07683.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07683.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 130105CBM21PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 11590Adsorption to raw starchAdd
    BLAST
    Regioni116 – 604489Starch degradationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 15 family.Curated
    Contains 1 CBM21 (carbohydrate binding type-21) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di1.50.10.10. 1 hit.
    InterProiIPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR005036. CBM_21.
    IPR000165. Glucoamylase.
    IPR011613. Glyco_hydro_15.
    [Graphical view]
    PfamiPF03370. CBM_21. 1 hit.
    PF00723. Glyco_hydro_15. 1 hit.
    [Graphical view]
    PRINTSiPR00736. GLHYDRLASE15.
    SUPFAMiSSF48208. SSF48208. 1 hit.
    PROSITEiPS51159. CBM21. 1 hit.
    PS00820. GLUCOAMYLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07683-1 [UniParc]FASTAAdd to Basket

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    MQLFNLPLKV SFFLVLSYFS LLVSAASIPS SASVQLDSYN YDGSTFSGKI    50
    YVKNIAYSKK VTVIYADGSD NWNNNGNTIA ASYSAPISGS NYEYWTFSAS 100
    INGIKEFYIK YEVSGKTYYD NNNSANYQVS TSKPTTTTAT ATTTTAPSTS 150
    TTTPPSRSEP ATFPTGNSTI SSWIKKQEGI SRFAMLRNIN PPGSATGFIA 200
    ASLSTAGPDY YYAWTRDAAL TSNVIVYEYN TTLSGNKTIL NVLKDYVTFS 250
    VKTQSTSTVC NCLGEPKFNP DASGYTGAWG RPQNDGPAER ATTFILFADS 300
    YLTQTKDASY VTGTLKPAIF KDLDYVVNVW SNGCFDLWEE VNGVHFYTLM 350
    VMRKGLLLGA DFAKRNGDST RASTYSSTAS TIANKISSFW VSSNNWIQVS 400
    QSVTGGVSKK GLDVSTLLAA NLGSVDDGFF TPGSEKILAT AVAVEDSFAS 450
    LYPINKNLPS YLGNSIGRYP EDTYNGNGNS QGNSWFLAVT GYAELYYRAI 500
    KEWIGNGGVT VSSISLPFFK KFDSSATSGK KYTVGTSDFN NLAQNIALAA 550
    DRFLSTVQLH AHNNGSLAEE FDRTTGLSTG ARDLTWSHAS LITASYAKAG 600
    APAA 604
    Length:604
    Mass (Da):65,162
    Last modified:November 1, 1995 - v2
    Checksum:i78421F1AAA93ADB9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00049 Genomic DNA. Translation: BAA00033.1.
    PIRiJP0001.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00049 Genomic DNA. Translation: BAA00033.1 .
    PIRi JP0001.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DJM NMR - A 26-131 [» ]
    ProteinModelPortali P07683.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P07683.
    ChEMBLi CHEMBL4449.

    Protein family/group databases

    CAZyi CBM21. Carbohydrate-Binding Module Family 21.
    GH15. Glycoside Hydrolase Family 15.
    mycoCLAPi GLA15E_RHIOR.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P07683.

    Family and domain databases

    Gene3Di 1.50.10.10. 1 hit.
    InterProi IPR008928. 6-hairpin_glycosidase-like.
    IPR012341. 6hp_glycosidase.
    IPR005036. CBM_21.
    IPR000165. Glucoamylase.
    IPR011613. Glyco_hydro_15.
    [Graphical view ]
    Pfami PF03370. CBM_21. 1 hit.
    PF00723. Glyco_hydro_15. 1 hit.
    [Graphical view ]
    PRINTSi PR00736. GLHYDRLASE15.
    SUPFAMi SSF48208. SSF48208. 1 hit.
    PROSITEi PS51159. CBM21. 1 hit.
    PS00820. GLUCOAMYLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rhizopus raw-starch-degrading glucoamylase: its cloning and expression in yeast."
      Ashikari T., Nakamura N., Tanaka Y., Kiuchi N., Shibano Y., Tanaka T., Amachi T., Yoshizumi H.
      Agric. Biol. Chem. 50:957-964(1986)
      [AGRICOLA] [Europe PMC]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: SAM0034.
    2. "Comparison of amino acid sequences of three glucoamylases and their structure-function relationships."
      Tanaka Y., Ashikari T., Nakamura N., Kiuchi N., Shibano Y., Amachi T., Yoshizumi H.
      Agric. Biol. Chem. 50:965-969(1986)
      [AGRICOLA] [Europe PMC]
      Cited for: HOMOLOGY, PREDICTED SECONDARY STRUCTURE.

    Entry informationi

    Entry nameiAMYG_RHIOR
    AccessioniPrimary (citable) accession number: P07683
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Rhizopus glucoamylase exists in multiple forms, Gluc 1, Gluc 2, and Gluc 3, all of which hydrolyze gelatinized starch at similar rates, but only the largest one (Gluc 1) is able to adsorb raw starch.
    Glucoamylase 3 may be 110-604 instead of 116-104.

    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