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P36924

- AMYB_BACCE

UniProt

P36924 - AMYB_BACCE

Protein

Beta-amylase

Gene

spoII

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (11 Jul 2002)
      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.

    Cofactori

    Binds 1 calcium ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei79 – 791Substrate
    Metal bindingi86 – 861Calcium
    Metal bindingi90 – 901Calcium
    Metal bindingi91 – 911Calcium
    Binding sitei119 – 1191Substrate
    Binding sitei127 – 1271Substrate
    Metal bindingi171 – 1711Calcium
    Metal bindingi174 – 1741Calcium
    Active sitei202 – 2021Proton donor
    Binding sitei317 – 3171Substrate
    Binding sitei322 – 3221Substrate
    Binding sitei360 – 3601Substrate
    Active sitei397 – 3971Proton acceptor
    Binding sitei427 – 4271Substrate

    GO - Molecular functioni

    1. beta-amylase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. 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

    Keywords - Ligandi

    Calcium, Metal-binding

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-amylase (EC:3.2.1.2)
    Alternative name(s):
    1,4-alpha-D-glucan maltohydrolase
    Gene namesi
    Name:spoII
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi194 – 1941Y → E: Reduces activity by 60%. 1 Publication
    Mutagenesisi194 – 1941Y → F: Reduces activity by 64%. 1 Publication
    Mutagenesisi194 – 1941Y → H: Reduces activity by 97%. 1 Publication
    Mutagenesisi194 – 1941Y → Q: Reduces activity by 80%. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Add
    BLAST
    Chaini31 – 546516Beta-amylasePRO_0000001453Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi121 ↔ 1291 Publication

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    Secondary structure

    1
    546
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi32 – 343
    Beta strandi42 – 465
    Helixi52 – 543
    Helixi58 – 7013
    Beta strandi73 – 819
    Helixi82 – 854
    Helixi96 – 10712
    Beta strandi111 – 1177
    Beta strandi121 – 1244
    Helixi135 – 1406
    Beta strandi142 – 1443
    Beta strandi146 – 1494
    Helixi165 – 18218
    Helixi184 – 1896
    Beta strandi193 – 1953
    Helixi199 – 2013
    Beta strandi202 – 2043
    Turni210 – 2134
    Helixi227 – 24115
    Helixi244 – 2518
    Helixi258 – 2603
    Helixi267 – 2726
    Helixi274 – 2763
    Helixi278 – 30629
    Turni307 – 3104
    Beta strandi314 – 3185
    Turni323 – 3264
    Beta strandi328 – 3303
    Turni331 – 3344
    Helixi335 – 3384
    Helixi343 – 35311
    Beta strandi356 – 3605
    Turni370 – 3723
    Helixi376 – 39015
    Beta strandi394 – 3974
    Helixi405 – 41713
    Beta strandi421 – 4266
    Helixi428 – 4325
    Helixi435 – 44410
    Beta strandi449 – 45810
    Beta strandi466 – 4738
    Helixi474 – 4763
    Turni477 – 4793
    Beta strandi481 – 4844
    Beta strandi489 – 4913
    Turni492 – 4954
    Beta strandi496 – 5049
    Beta strandi509 – 5168
    Beta strandi522 – 5254
    Beta strandi530 – 5345
    Beta strandi541 – 5455

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B90X-ray2.50A31-546[»]
    1B9ZX-ray2.10A31-546[»]
    1CQYX-ray1.95A448-546[»]
    1ITCX-ray2.10A31-546[»]
    1J0YX-ray2.10A/B/C/D31-546[»]
    1J0ZX-ray2.20A/B/C/D31-546[»]
    1J10X-ray2.10A/B/C/D31-546[»]
    1J11X-ray2.00A/B/C/D31-546[»]
    1J12X-ray2.10A/B/C/D31-546[»]
    1J18X-ray2.00A31-546[»]
    1VEMX-ray1.85A31-546[»]
    1VENX-ray2.02A31-546[»]
    1VEOX-ray2.12A31-546[»]
    1VEPX-ray2.06A31-546[»]
    5BCAX-ray2.20A/B/C/D31-546[»]
    ProteinModelPortaliP36924.
    SMRiP36924. Positions 31-546.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36924.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini444 – 546103CBM20PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni398 – 3992Substrate binding

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 14 family.Curated
    Contains 1 CBM20 (carbohydrate binding type-20) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    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.

    P36924-1 [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:July 11, 2002 - v2
    Checksum:iA8F7CFC96ED6979B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024519 Genomic DNA. Translation: BAA75890.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024519 Genomic DNA. Translation: BAA75890.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B90 X-ray 2.50 A 31-546 [» ]
    1B9Z X-ray 2.10 A 31-546 [» ]
    1CQY X-ray 1.95 A 448-546 [» ]
    1ITC X-ray 2.10 A 31-546 [» ]
    1J0Y X-ray 2.10 A/B/C/D 31-546 [» ]
    1J0Z X-ray 2.20 A/B/C/D 31-546 [» ]
    1J10 X-ray 2.10 A/B/C/D 31-546 [» ]
    1J11 X-ray 2.00 A/B/C/D 31-546 [» ]
    1J12 X-ray 2.10 A/B/C/D 31-546 [» ]
    1J18 X-ray 2.00 A 31-546 [» ]
    1VEM X-ray 1.85 A 31-546 [» ]
    1VEN X-ray 2.02 A 31-546 [» ]
    1VEO X-ray 2.12 A 31-546 [» ]
    1VEP X-ray 2.06 A 31-546 [» ]
    5BCA X-ray 2.20 A/B/C/D 31-546 [» ]
    ProteinModelPortali P36924.
    SMRi P36924. 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 P36924.

    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. "Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme."
      Nanmori T., Nagai M., Shimizu Y., Shinke R., Mikami B.
      Appl. Environ. Microbiol. 59:623-627(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
      Strain: BQ10-S1.
    2. Nanmori T., Mikami B., Shimizu Y.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose."
      Mikami B., Adachi M., Kage T., Sarikaya E., Nanmori T., Shinke R., Utsumi S.
      Biochemistry 38:7050-7061(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    4. "Crystal structures of beta-amylase from Bacillus cereus var mycoides in complexes with substrate analogs and affinity-labeling reagents."
      Oyama T., Miyake H., Kusunoki M., Nitta Y.
      J. Biochem. 133:467-474(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 31-546 IN COMPLEXES WITH SUBSTRATE ANALOGS.
    5. "Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type."
      Hirata A., Adachi M., Utsumi S., Mikami B.
      Biochemistry 43:12523-12531(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-546 IN COMPLEX WITH CALCIUM IONS AND MALTOSE, MUTAGENESIS OF TYR-194, DISULFIDE BOND.

    Entry informationi

    Entry nameiAMYB_BACCE
    AccessioniPrimary (citable) accession number: P36924
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: July 11, 2002
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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