GuaB

• Description: IMP dehydrogenase
  
  

Gene name	guaB
Synonyms	guaA
Essential	yes PubMed
Product	IMP dehydrogenase
Function	biosynthesis of GMP
Metabolic function and regulation of this protein in SubtiPathways: Purine synthesis, Nucleotides (regulation)
MW, pI	52 kDa, 6.168
Gene length, protein length	1464 bp, 488 aa
Immediate neighbours	yaaC, dacA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, essential genes, phosphoproteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

• Locus tag: BSU00090

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Inosine 5'-phosphate + NAD⁺ + H₂O = xanthosine 5'-phosphate + NADH (according to Swiss-Prot)

• Protein family: IMPDH/GMPR family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated (STY) PubMed, S-cysteinlyation after diamide stress (Cys-308) PubMed, PubMed

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 1VRD (from Thermotoga maritima msb8, 60% identity, 80% similarity)

• UniProt: P21879

• KEGG entry: [3]

• E.C. number: 1.1.1.205

Expression and regulation

• Operon: guaB

• Sigma factor:

• Regulation:
  • activated during growth in the presence of branched chain amino acids (CodY) PubMed
  • inhibition of enzymatic activity by (p)ppGpp during the ´stringent response´

• Regulatory mechanism:
  • CodY: transcription activation PubMed

• Additional information: the mRNA is very stable (half-life > 15 min) PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Falko Hochgräfe, Jörg Mostertz, Dierk-Christoph Pöther, Dörte Becher, John D Helmann, Michael Hecker
S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.
J Biol Chem: 2007, 282(36);25981-5
[PubMed:17611193] [WorldCat.org] [DOI] (P p)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [WorldCat.org] [DOI] (P p)

Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455] [WorldCat.org] [DOI] (P p)

H H Saxild, P Nygaard
Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing purine nucleotide pools.
J Gen Microbiol: 1991, 137(10);2387-94
[PubMed:1722815] [WorldCat.org] [DOI] (P p)

J M Lopez, A Dromerick, E Freese
Response of guanosine 5'-triphosphate concentration to nutritional changes and its significance for Bacillus subtilis sporulation.
J Bacteriol: 1981, 146(2);605-13
[PubMed:6111556] [WorldCat.org] [DOI] (P p)

PubMed