Prs
- Description: phosphoribosylpyrophosphate synthetase, universally conserved protein
| Gene name | prs |
| Synonyms | |
| Essential | yes PubMed |
| Product | phosphoribosylpyrophosphate synthetase |
| Function | phosphoribosylpyrophosphate synthesis (biosynthesis of histidine) |
| Gene expression levels in SubtiExpress: prs | |
| Interactions involving this protein in SubtInteract: Prs | |
| Metabolic function and regulation of this protein in SubtiPathways: prs | |
| MW, pI | 34 kDa, 5.895 |
| Gene length, protein length | 951 bp, 317 aa |
| Immediate neighbours | gcaD, ctc |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, biosynthesis/ acquisition of nucleotides, essential genes, universally conserved proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU00510
Phenotypes of a mutant
essential PubMed
Database entries
- BsubCyc: BSU00510
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate (according to Swiss-Prot)
- Protein family: ribose-phosphate pyrophosphokinase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
- subject to feedback inhibition by two end products of purine biosynthesis, adenosine 5'-diphosphate (ADP) and guanosine 5'-diphosphate (GDP) PubMed
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU00510
- UniProt: P14193
- KEGG entry: [3]
- E.C. number: 2.7.6.1
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Natalia P Zakataeva, Dmitriy V Romanenkov, Victoria S Skripnikova, Maria V Vitushkina, Vitaliy A Livshits, Alexandr D Kivero, Anna E Novikova
Wild-type and feedback-resistant phosphoribosyl pyrophosphate synthetases from Bacillus amyloliquefaciens: purification, characterization, and application to increase purine nucleoside production.
Appl Microbiol Biotechnol: 2012, 93(5);2023-33
[PubMed:22083279]
[WorldCat.org]
[DOI]
(I p)
Shuobo Shi, Tao Chen, Zhigang Zhang, Xun Chen, Xueming Zhao
Transcriptome analysis guided metabolic engineering of Bacillus subtilis for riboflavin production.
Metab Eng: 2009, 11(4-5);243-52
[PubMed:19446032]
[WorldCat.org]
[DOI]
(I p)
Aloke Kumar Bera, Jianghai Zhu, Howard Zalkin, Janet L Smith
Functional dissection of the Bacillus subtilis pur operator site.
J Bacteriol: 2003, 185(14);4099-109
[PubMed:12837784]
[WorldCat.org]
[DOI]
(P p)
Sangita C Sinha, Joseph Krahn, Byung Sik Shin, Diana R Tomchick, Howard Zalkin, Janet L Smith
The purine repressor of Bacillus subtilis: a novel combination of domains adapted for transcription regulation.
J Bacteriol: 2003, 185(14);4087-98
[PubMed:12837783]
[WorldCat.org]
[DOI]
(P p)
I Hilden, B N Krath, B Hove-Jensen
Tricistronic operon expression of the genes gcaD (tms), which encodes N-acetylglucosamine 1-phosphate uridyltransferase, prs, which encodes phosphoribosyl diphosphate synthetase, and ctc in vegetative cells of Bacillus subtilis.
J Bacteriol: 1995, 177(24);7280-4
[PubMed:8522540]
[WorldCat.org]
[DOI]
(P p)
K Arnvig, B Hove-Jensen, R L Switzer
Purification and properties of phosphoribosyl-diphosphate synthetase from Bacillus subtilis.
Eur J Biochem: 1990, 192(1);195-200
[PubMed:2169413]
[WorldCat.org]
[DOI]
(P p)
