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hutI imidazolone-5-propionate hydrolase [ Bacillus subtilis subsp. subtilis str. 168 ]

Gene ID: 937531, updated on 12-Feb-2021

Summary

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Gene symbol
hutI
Gene description
imidazolone-5-propionate hydrolase
Locus tag
BSU_39370
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
BSU39370
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Genomic context

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Sequence:
NC_000964.3 (4045245..4046510)

NC_000964.3Genomic Context describing neighboring genes Neighboring gene transcriptional antiterminator Neighboring gene histidine ammonia-lyase (histidase) Neighboring gene urocanase Neighboring gene formiminoglutamate hydrolase Neighboring gene histidine degradation metabolites permease Neighboring gene pyrimidine-nucleoside phosphorylase

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. Local structure investigation of the active site of the imidazolonepropionase from Bacillus subtilis by XANES spectroscopy and ab initio calculations. Yang F, et al. J Synchrotron Radiat, 2008 Mar. PMID 18296777
  2. Protein preparation, crystallization and preliminary X-ray analysis of imidazolonepropionase from Bacillus subtilis. Yu Y, et al. Biochim Biophys Acta, 2006 Jan. PMID 16198643
  3. A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis. Yu Y, et al. J Biol Chem, 2006 Dec 1. PMID 16990261
  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. Bond length between Zn & catalytic water is 0.36A shorter then that in PDB. This new conformation & occurrence of a short water-to-zinc bond length support the nucleophilic attack catalytic mechanism proposed for this enzyme.
    Title: Local structure investigation of the active site of the imidazolonepropionase from Bacillus subtilis by XANES spectroscopy and ab initio calculations.
  2. analysis of the crystal structure of the imidazolonepropionase from Bacillus subtilis
    Title: A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis.
  3. crystallization and X-ray crystallography
    Title: Protein preparation, crystallization and preliminary X-ray analysis of imidazolonepropionase from Bacillus subtilis.
Submit: New GeneRIF Correction

Pathways from PubChem

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General gene information

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Homology

General protein information

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Preferred Names
imidazolone-5-propionate hydrolase
NP_391816.1
  • Evidence 1a: Function from experimental evidences in the studied strain; PubMedId: 16990261, 17395359, 18296777; 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
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_391816.1 imidazolone-5-propionate hydrolase [Bacillus subtilis subsp. subtilis str. 168]

    See identical proteins and their annotated locations for NP_391816.1

    Status: PROVISIONAL

    Conserved Domains (1) summary
    PRK09356
    Location:6 → 414
    PRK09356; imidazolonepropionase; Validated
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P42084.1

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

Other Literature Sources
Molecular Biology Databases