GuaB

• Description: IMP dehydrogenase
  
  

Gene name	guaB
Synonyms	guaA
Essential	yes PubMed
Product	IMP dehydrogenase
Function	biosynthesis of GMP
Gene expression levels in SubtiExpress: GuaB
Metabolic function and regulation of this protein in SubtiPathways: guaB
MW, pI	52 kDa, 6.168
Gene length, protein length	1464 bp, 488 aa
Immediate neighbours	yaaC, dacA
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, essential genes, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

CodY regulon

The gene

Basic information

• Locus tag: BSU00090

Phenotypes of a mutant

• essential PubMed
• reduced expression of guaB suppresses the requirement of a relA sasA sasB triple mutant for branched chain amino acids, methionine and threonine PubMed

Database entries

• BsubCyc: BSU00090

• 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
  • Cys308 is S-cysteinylated after diamide stress PubMed, PubMed
  • Cys308 is S-bacillithiolated by NaOCl stress in B. subtilis and other Bacillus species PubMed

• Cofactors:

• Effectors of protein activity:
  • inhibition of enzymatic activity by (p)ppGpp during the ´stringent response´PubMed

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU00090

• 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 PubMed

• Expression browser: guaB PubMed

• Sigma factor:

• Regulation:
  • activated during growth in the presence of branched chain amino acids (CodY) PubMed

• Regulatory mechanism:
  • CodY: transcription activation PubMed

• Additional information:
  • the mRNA is very stable (half-life > 15 min) PubMed
  • inhibition of enzymatic activity by (p)ppGpp during the ´stringent response´PubMed
  • belongs to the 100 most abundant proteins PubMed

Biological materials

• Mutant:

• Expression vector:
  • purification from B. subtilis with an N-terminal Strep-tag, for SPINE, (in pGP380): pGP901, available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Allison Kriel, Shaun R Brinsmade, Jessica L Tse, Ashley K Tehranchi, Alycia N Bittner, Abraham L Sonenshein, Jue D Wang
GTP dysregulation in Bacillus subtilis cells lacking (p)ppGpp results in phenotypic amino acid auxotrophy and failure to adapt to nutrient downshift and regulate biosynthesis genes.
J Bacteriol: 2014, 196(1);189-201
[PubMed:24163341] [WorldCat.org] [DOI] (I p)

Allison Kriel, Alycia N Bittner, Sok Ho Kim, Kuanqing Liu, Ashley K Tehranchi, Winnie Y Zou, Samantha Rendon, Rui Chen, Benjamin P Tu, Jue D Wang
Direct regulation of GTP homeostasis by (p)ppGpp: a critical component of viability and stress resistance.
Mol Cell: 2012, 48(2);231-41
[PubMed:22981860] [WorldCat.org] [DOI] (I p)

Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)