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P21332

- O16G_BACCE

UniProt

P21332 - O16G_BACCE

Protein

Oligo-1,6-glucosidase

Gene

malL

Organism
Bacillus cereus
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei199 – 1991Nucleophile
    Active sitei255 – 2551Proton donor
    Sitei329 – 3291Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. cation binding Source: InterPro
    2. oligo-1,6-glucosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-3340-MONOMER.
    SABIO-RKP21332.

    Protein family/group databases

    CAZyiGH13. Glycoside Hydrolase Family 13.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Oligo-1,6-glucosidase (EC:3.2.1.10)
    Alternative name(s):
    Dextrin 6-alpha-D-glucanohydrolase
    Oligosaccharide alpha-1,6-glucosidase
    Sucrase-isomaltase
    Short name:
    Isomaltase
    Gene namesi
    Name:malL
    OrganismiBacillus cereus
    Taxonomic identifieri1396 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 558558Oligo-1,6-glucosidasePRO_0000054313Add
    BLAST

    Structurei

    Secondary structure

    1
    558
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 84
    Beta strandi11 – 144
    Helixi16 – 183
    Beta strandi22 – 276
    Helixi30 – 345
    Helixi37 – 437
    Beta strandi47 – 504
    Turni59 – 624
    Beta strandi66 – 716
    Helixi73 – 753
    Helixi78 – 9013
    Beta strandi94 – 996
    Helixi109 – 1146
    Helixi123 – 1253
    Beta strandi132 – 1354
    Beta strandi145 – 1528
    Turni153 – 1564
    Beta strandi157 – 1604
    Helixi175 – 19016
    Beta strandi195 – 1984
    Helixi201 – 2033
    Helixi224 – 2263
    Turni227 – 2293
    Helixi233 – 24311
    Helixi245 – 2473
    Beta strandi251 – 2555
    Helixi261 – 2688
    Helixi270 – 2723
    Helixi282 – 2843
    Beta strandi292 – 2965
    Helixi301 – 31414
    Beta strandi316 – 3194
    Helixi333 – 3364
    Helixi344 – 35613
    Beta strandi358 – 3658
    Helixi368 – 3703
    Helixi380 – 3823
    Helixi386 – 39712
    Helixi403 – 41311
    Helixi415 – 4184
    Turni428 – 4314
    Helixi443 – 4464
    Helixi450 – 4556
    Helixi460 – 47314
    Helixi475 – 4795
    Beta strandi481 – 4866
    Beta strandi490 – 49910
    Beta strandi502 – 5098
    Beta strandi511 – 5133
    Beta strandi515 – 5184
    Beta strandi528 – 5358
    Beta strandi543 – 5475
    Beta strandi552 – 5576

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UOKX-ray2.00A1-558[»]
    ProteinModelPortaliP21332.
    SMRiP21332. Positions 1-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21332.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family.Curated

    Family and domain databases

    Gene3Di2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProiIPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    [Graphical view]
    SMARTiSM00642. Aamy. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P21332-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKQWWKESV VYQIYPRSFM DSNGDGIGDL RGIISKLDYL KELGIDVIWL    50
    SPVYESPNDD NGYDISDYCK IMNEFGTMED WDELLHEMHE RNMKLMMDLV 100
    VNHTSDEHNW FIESRKSKDN KYRDYYIWRP GKEGKEPNNW GAAFSGSAWQ 150
    YDEMTDEYYL HLFSKKQPDL NWDNEKVRQD VYEMMKFWLE KGIDGFRMDV 200
    INFISKEEGL PTVETEEEGY VSGHKHFMNG PNIHKYLHEM NEEVLSHYDI 250
    MTVGEMPGVT TEEAKLYTGE ERKELQMVFQ FEHMDLDSGE GGKWDVKPCS 300
    LLTLKENLTK WQKALEHTGW NSLYWNNHDQ PRVVSRFGND GMYRIESAKM 350
    LATVLHMMKG TPYIYQGEEI GMTNVRFESI DEYRDIETLN MYKEKVMERG 400
    EDIEKVMQSI YIKGRDNART PMQWDDQNHA GFTTGEPWIT VNPNYKEINV 450
    KQAIQNKDSI FYYYKKLIEL RKNNEIVVYG SYDLILENNP SIFAYVRTYG 500
    VEKLLVIANF TAEECIFELP EDISYSEVEL LIHNYDVENG PIENITLRPY 550
    EAMVFKLK 558
    Length:558
    Mass (Da):66,013
    Last modified:May 1, 1991 - v1
    Checksum:i502336D7A77C7182
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53507 Genomic DNA. Translation: CAA37583.1.
    PIRiS13579.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53507 Genomic DNA. Translation: CAA37583.1 .
    PIRi S13579.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UOK X-ray 2.00 A 1-558 [» ]
    ProteinModelPortali P21332.
    SMRi P21332. Positions 1-558.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH13. Glycoside Hydrolase Family 13.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-3340-MONOMER.
    SABIO-RK P21332.

    Miscellaneous databases

    EvolutionaryTracei P21332.

    Family and domain databases

    Gene3Di 2.60.40.1180. 1 hit.
    3.20.20.80. 2 hits.
    InterProi IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR006589. Glyco_hydro_13_sub_cat_dom.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    [Graphical view ]
    SMARTi SM00642. Aamy. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene."
      Watanabe K., Kitamura K., Iha H., Suzuki Y.
      Eur. J. Biochem. 192:609-620(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
      Strain: ATCC 7064 / NRS 201.
    2. "Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0-A resolution X-ray analysis."
      Kizaki H., Hata Y., Watanabe K., Katsube Y., Suzuki Y.
      J. Biochem. 113:646-649(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
      Strain: ATCC 7064 / NRS 201.
    3. "The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0-A resolution: structural characterization of proline-substitution sites for protein thermostabilization."
      Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y.
      J. Mol. Biol. 269:142-153(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Strain: ATCC 7064 / NRS 201.

    Entry informationi

    Entry nameiO16G_BACCE
    AccessioniPrimary (citable) accession number: P21332
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 1, 1991
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 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