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B9J2G8

- GLGB_BACCQ

UniProt

B9J2G8 - GLGB_BACCQ

Protein

1,4-alpha-glucan branching enzyme GlgB

Gene

glgB

Organism
Bacillus cereus (strain Q1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (24 Mar 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.UniRule annotation

    Catalytic activityi

    Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei309 – 3091NucleophileUniRule annotation
    Active sitei352 – 3521Proton donorUniRule annotation

    GO - Molecular functioni

    1. 1,4-alpha-glucan branching enzyme activity Source: UniProtKB-HAMAP
    2. cation binding Source: InterPro
    3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro

    GO - Biological processi

    1. glycogen biosynthetic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen biosynthesis, Glycogen metabolism

    Enzyme and pathway databases

    BioCyciBCER361100:GJ7M-4673-MONOMER.
    UniPathwayiUPA00164.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,4-alpha-glucan branching enzyme GlgBUniRule annotation (EC:2.4.1.18UniRule annotation)
    Alternative name(s):
    1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferaseUniRule annotation
    Alpha-(1->4)-glucan branching enzymeUniRule annotation
    Glycogen branching enzymeUniRule annotation
    Short name:
    BEUniRule annotation
    Gene namesi
    Name:glgBUniRule annotation
    Ordered Locus Names:BCQ_4685
    OrganismiBacillus cereus (strain Q1)
    Taxonomic identifieri361100 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000441: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6456451,4-alpha-glucan branching enzyme GlgBPRO_1000147758Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    STRINGi361100.BCQ_4685.

    Structurei

    3D structure databases

    ProteinModelPortaliB9J2G8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 13 family. GlgB subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0296.
    HOGENOMiHOG000283037.
    KOiK00700.
    OMAiAKLLFMG.
    OrthoDBiEOG6JX7GT.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    HAMAPiMF_00685. GlgB.
    InterProiIPR006048. A-amylase_b_C.
    IPR006407. GlgB.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR004193. Glyco_hydro_13_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PANTHERiPTHR10357. PTHR10357. 1 hit.
    PfamiPF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    PF02922. CBM_48. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000463. GlgB. 1 hit.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    TIGRFAMsiTIGR01515. branching_enzym. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    B9J2G8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVINCEEVK RDEFHTEKYY ESYNIFGAHI VTEDEMRGVR FTVWAPHAKA    50
    MSVVGDFNEW DYEQHKMLQV TEEGIWSLFI PHIEEREIYK YAIETMAGDV 100
    ILKADPYAVY AEVRPNTASV VFDIKGYEWN DKNWSRKKKK KSVYKEAMTV 150
    YELHFGSWKK KEDGTLYSYR EMAEELIPYV VEHQFTHIEI MPLVEHPYDR 200
    SWGYQGTGYY AATSRFGTPH DLMHFVDECH KYGIGVILDW VPGHFCKDAH 250
    GLYLFDGTPT YEYKDKDVQE NPVWGTVNFD LGKREVRNFL ISNALFWMRY 300
    FHIDGFRVDA VANMLYWNKE GQEQSNEHAV SFLRELNEAV FAEDEDFLMT 350
    AEDSTAWPLV TAPTYEGGLG FNYKWNMGWM NDVLKYMECA PEYRKYIHDK 400
    MTFSLLYAYS ENFILPLSHD EVVHGKKSLL NKMPGDYWDK FAQLRLLYGY 450
    FFTHPGKKLL FMGGEFGQFD EWKDLEDLDW NLHDFEMHRY MHDYFKELIA 500
    LYKRSKPLWQ LDHSPEGFQW IDANNNEQSI FSFIRQGDKQ EDALVVVCNF 550
    TKATYENYKV GVPDFEYYNE ILNSDAEQYG GSGQVNKKRL KAIQEPYHNQ 600
    AAHVEITIPP FGVSILRPVK TRKGSKKQDG SKTKVRSNVT SRGKR 645
    Length:645
    Mass (Da):75,926
    Last modified:March 24, 2009 - v1
    Checksum:iBB622B9A824E9ABA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000227 Genomic DNA. Translation: ACM15111.1.
    RefSeqiWP_000111390.1. NC_011969.1.
    YP_002532400.1. NC_011969.1.

    Genome annotation databases

    EnsemblBacteriaiACM15111; ACM15111; BCQ_4685.
    GeneIDi7373696.
    KEGGibcq:BCQ_4685.
    PATRICi18917165. VBIBacCer120424_4747.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000227 Genomic DNA. Translation: ACM15111.1 .
    RefSeqi WP_000111390.1. NC_011969.1.
    YP_002532400.1. NC_011969.1.

    3D structure databases

    ProteinModelPortali B9J2G8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 361100.BCQ_4685.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACM15111 ; ACM15111 ; BCQ_4685 .
    GeneIDi 7373696.
    KEGGi bcq:BCQ_4685.
    PATRICi 18917165. VBIBacCer120424_4747.

    Phylogenomic databases

    eggNOGi COG0296.
    HOGENOMi HOG000283037.
    KOi K00700.
    OMAi AKLLFMG.
    OrthoDBi EOG6JX7GT.

    Enzyme and pathway databases

    UniPathwayi UPA00164 .
    BioCyci BCER361100:GJ7M-4673-MONOMER.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    2.60.40.1180. 1 hit.
    3.20.20.80. 1 hit.
    HAMAPi MF_00685. GlgB.
    InterProi IPR006048. A-amylase_b_C.
    IPR006407. GlgB.
    IPR015902. Glyco_hydro_13.
    IPR013780. Glyco_hydro_13_b.
    IPR006047. Glyco_hydro_13_cat_dom.
    IPR004193. Glyco_hydro_13_N.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    PANTHERi PTHR10357. PTHR10357. 1 hit.
    Pfami PF00128. Alpha-amylase. 1 hit.
    PF02806. Alpha-amylase_C. 1 hit.
    PF02922. CBM_48. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000463. GlgB. 1 hit.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    TIGRFAMsi TIGR01515. branching_enzym. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
      Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
      J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Q1.

    Entry informationi

    Entry nameiGLGB_BACCQ
    AccessioniPrimary (citable) accession number: B9J2G8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 28, 2009
    Last sequence update: March 24, 2009
    Last modified: October 1, 2014
    This is version 46 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

    Complete proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3