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amyX pullulanase [ Bacillus subtilis subsp. subtilis str. 168 ]

Gene ID: 937292, updated on 6-Oct-2023

Summary

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Gene symbol
amyX
Gene description
pullulanase
Locus tag
BSU_29930
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Bacillus subtilis subsp. subtilis str. 168 (strain: 168, sub-species: subtilis, type-material: type strain of Bacillus subtilis)
Lineage
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus
Old locus tag
BSU29930
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Genomic context

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Sequence:
NC_000964.3 (3061651..3063807, complement)

NC_000964.3Genomic Context describing neighboring genes Neighboring gene hypothetical protein Neighboring gene putative kinase/phosphotransferase Neighboring gene putative phospholipid kinase Neighboring gene putative hydrolase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000964.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Functional characterization of tryptophan437 at subsite +2 in pullulanase from Bacillus subtilis str. 168. Li X, et al. Int J Biol Macromol, 2019 Jul 15. PMID 31028806
  2. Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168. Malle D, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2006 Apr 1. PMID 16582490, Free PMC Article
  3. Role of maltogenic amylase and pullulanase in maltodextrin and glycogen metabolism of Bacillus subtilis 168. Shim JH, et al. J Bacteriol, 2009 Aug. PMID 19465663, Free PMC Article
  4. Bacillus subtilis, the model Gram-positive bacterium: 20 years of annotation refinement. Borriss R, et al. Microb Biotechnol, 2018 Jan. PMID 29280348, Free PMC Article
  5. An updated metabolic view of the Bacillus subtilis 168 genome. Belda E, et al. Microbiology (Reading), 2013 Apr. PMID 23429746

See all (7) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. Trp437 at subsite +2 plays crucial role in catalysis of PulA
    Title: Functional characterization of tryptophan437 at subsite +2 in pullulanase from Bacillus subtilis str. 168.
  2. Glycogen breakdown requests that pullulanase hydrolyzes the alpha-1,6-glycosidic linkage at the branch point to release a linear maltooligosaccharide that is then hydrolyzed into maltose and maltotriose by MAase.
    Title: Role of maltogenic amylase and pullulanase in maltodextrin and glycogen metabolism of Bacillus subtilis 168.
  3. The crystal contains two molecules of pullulanase in the asymmetric unit, with a solvent content of 53.15%. The crystal diffracted to 2.1 angstroms resolution at a synchrotron and is suitable for structure determination.
    Title: Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168.
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General gene information

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Homology

General protein information

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Preferred Names
pullulanase
NP_390871.2
  • Evidence 1a: Function from experimental evidences in the studied strain; PubMedId: 9453151, 16582490, 19465663, 23973973; Product type e: enzyme

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000964.3 Reference assembly

    Range
    3061651..3063807 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_390871.2 pullulanase [Bacillus subtilis subsp. subtilis str. 168]

    See identical proteins and their annotated locations for NP_390871.2

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A0D1LBT8
    Conserved Domains (2) summary
    TIGR02104
    Location:95 → 691
    pulA_typeI; pullulanase, type I
    pfam17999
    Location:8 → 92
    PulA_N1; Pullulanase N1-terminal domain
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
C0SPA0.1

Gene LinkOut

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Other Literature Sources
Molecular Biology Databases