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Q9Z4N9

- Q9Z4N9_BACCE

UniProt

Q9Z4N9 - Q9Z4N9_BACCE

Protein

Beta-amylase

Gene
N/A
Organism
Bacillus cereus
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi86 – 861Calcium
    Metal bindingi90 – 901Calcium
    Metal bindingi91 – 911Calcium
    Metal bindingi171 – 1711Calcium
    Metal bindingi174 – 1741Calcium

    GO - Molecular functioni

    1. beta-amylase activity Source: UniProtKB-EC
    2. starch binding Source: InterPro

    GO - Biological processi

    1. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    GlycosidaseUniRule annotationImported, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

    Protein family/group databases

    CAZyiCBM20. Carbohydrate-Binding Module Family 20.
    GH14. Glycoside Hydrolase Family 14.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-amylaseUniRule annotation (EC:3.2.1.2UniRule annotation)
    OrganismiBacillus cereusImported
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030 PotentialImportedAdd
    BLAST
    Chaini31 – 546516beta-amylaseImportedPRO_5000049300Add
    BLAST

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CQYX-ray1.95A448-546[»]
    ProteinModelPortaliQ9Z4N9.
    SMRiQ9Z4N9. Positions 31-546.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z4N9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 14 family.UniRule annotation

    Keywords - Domaini

    SignalImported

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProiIPR002044. CBM_fam20.
    IPR001554. Glyco_hydro_14.
    IPR018238. Glyco_hydro_14_CS.
    IPR000125. Glyco_hydro_14A_bac.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF00686. CBM_20. 1 hit.
    PF01373. Glyco_hydro_14. 1 hit.
    [Graphical view]
    PRINTSiPR00750. BETAAMYLASE.
    PR00841. GLHYDLASE14A.
    SMARTiSM01065. CBM_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00506. BETA_AMYLASE_1. 1 hit.
    PS00679. BETA_AMYLASE_2. 1 hit.
    PS51166. CBM20. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Z4N9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK    50
    KIPEVTNWET FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR 100
    FAQSVKNAGM KMIPIISTHQ CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS 150
    ETGTVNKETL NPLASDVIRK EYGELYTAFA AAMKPYKDVI AKIYLSGGPA 200
    GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK YGSLNEVNKA 250
    WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE 300
    LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF 350
    KSAKLDVTFT CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL 400
    SIGNEEEYKR VAEMAFNYNF AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV 450
    MQTIVVKNVP TTIGDTVYIT GNRAELGSWD TKQYPIQLYY DSHSNDWRGN 500
    VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT SHTSSW 546
    Length:546
    Mass (Da):61,629
    Last modified:May 1, 1999 - v1
    Checksum:iA8F7CFC96ED6979B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020313 Genomic DNA. Translation: BAA34650.1.
    PIRiA48961.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020313 Genomic DNA. Translation: BAA34650.1 .
    PIRi A48961.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CQY X-ray 1.95 A 448-546 [» ]
    ProteinModelPortali Q9Z4N9.
    SMRi Q9Z4N9. Positions 31-546.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM20. Carbohydrate-Binding Module Family 20.
    GH14. Glycoside Hydrolase Family 14.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q9Z4N9.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    3.20.20.80. 1 hit.
    InterProi IPR002044. CBM_fam20.
    IPR001554. Glyco_hydro_14.
    IPR018238. Glyco_hydro_14_CS.
    IPR000125. Glyco_hydro_14A_bac.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF00686. CBM_20. 1 hit.
    PF01373. Glyco_hydro_14. 1 hit.
    [Graphical view ]
    PRINTSi PR00750. BETAAMYLASE.
    PR00841. GLHYDLASE14A.
    SMARTi SM01065. CBM_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00506. BETA_AMYLASE_1. 1 hit.
    PS00679. BETA_AMYLASE_2. 1 hit.
    PS51166. CBM20. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Kinetic study of active site structure of beta-amylase from Bacillus cereus var. mycoides."
      Nitta Y., Shirakawa M., Takasaki Y.
      Biosci. Biotechnol. Biochem. 60:823-827(1996)
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Cloning, sequencing, and expression of a beta-amylase gene from Bacillus cereus var. mycoides and characterization of its products."
      Yamaguchi T., Matsumoto Y., Shirakawa M., Kibe M., Hibino T., Kozaki S., Takasaki Y., Nitta Y.
      Biosci. Biotechnol. Biochem. 60:1255-1259(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    3. Oyama T.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    4. "Structure of Separated Starch-Binding Domain of Bacillus cereus B-amylase."
      Yoon H.J., Hirata A., Adachi M., Sekine A., Utsumi S., Mikami B.
      Submitted (AUG-1999) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 448-546.

    Entry informationi

    Entry nameiQ9Z4N9_BACCE
    AccessioniPrimary (citable) accession number: Q9Z4N9
    Entry historyi
    Integrated into UniProtKB/TrEMBL: May 1, 1999
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    3D-structureImported

    External Data

    Dasty 3