pdxT
168
pyridoxal-5-phosphate synthase (glutaminase domain)
Locus
BSU_00120
Molecular weight
21.30 kDa
Isoelectric point
4.98
Function
pyridoxal-5-phosphate biosynthesis
Product
pyridoxal-5-phosphate synthase (glutaminase domain)
Essential
no
E.C.
4.3.3.6
Synonyms
pdxT, yaaE
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0311 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
19,968 20,558
Phenotypes of a mutant
the mutant tends to acquire suppressor mutations that result in improved growth and colony morphology PubMed
auxotrophic for pyridoxal-5-phosphate at low external ammonium concentration PubMed, this can be suppressed by overexpression of pdxS or the ammonium transporter NrgA PubMed
inactivation of pdxT reduces sporulation efficiency to 1.2% that of wild type cells; delayed entry into sporulation PubMed
poor growth PubMed
non-transformable PubMed
The protein
Catalyzed reaction/ biological activity
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (according to UniProt)
aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine --> H+ + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-phosphate (according to UniProt)
Protein family
Glutaminase PdxT/SNO family (single member, according to UniProt)
Structure
cytosol (according to UniProt)
Expression and Regulation
Operons
Description
Regulation
expression is reduced in motile cells as compared to non-motile cells PubMed
Regulatory mechanism
Open in new tab
Biological materials
Mutant
BKE00120 (pdxT::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATGTCAGCAGCGCTCCTAT, downstream forward: _UP4_TAAAACAGTTGAAAGCTGTG
BKK00120 (pdxT::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATGTCAGCAGCGCTCCTAT, downstream forward: _UP4_TAAAACAGTTGAAAGCTGTG
GP4754 (trpC2 ΔpdxT::cat), available in Jörg Stülke's lab
References
Reviews
Underground metabolism facilitates the evolution of novel pathways for vitamin B6 biosynthesis.Applied microbiology and biotechnology. 2021 Mar 4; . PMID: 33665688
Original Publications
Structure and identification of the native PLP synthase complex from Methanosarcina acetivorans lysate.mBio. 2024 Nov 26; :e0309024. PMID: 39589128
A Bacillus subtilis ΔpdxT mutant suppresses vitamin B6 limitation by acquiring mutations enhancing pdxS gene dosage and ammonium assimilation.Environmental microbiology reports. 2021 Feb 8; . PMID: 33559288
Construction and Analysis of Two Genome-Scale Deletion Libraries for Bacillus subtilis.
Cell systems. 2017 Mar 22; 4(3):291-305.e7. pii:S2405-4712(16)30447-1. doi:10.1016/j.cels.2016.12.013. PMID:28189581
High-Throughput Genetic Screens Identify a Large and Diverse Collection of New Sporulation Genes in Bacillus subtilis.
PLoS biology. 2016 Jan; 14(1):e1002341. doi:10.1371/journal.pbio.1002341. PMID:26735940
Engineering a pyridoxal 5'-phosphate supply for cadaverine production by using Escherichia coli whole-cell biocatalysis.
Scientific reports. 2015 Oct 22; 5:15630. doi:10.1038/srep15630. PMID:26490441
Crystal structures capture three states in the catalytic cycle of a pyridoxal phosphate (PLP) synthase.
The Journal of biological chemistry. 2015 Feb 27; 290(9):5226-39. doi:10.1074/jbc.M114.626382. PMID:25568319
A novel engineering tool in the Bacillus subtilis toolbox: inducer-free activation of gene expression by selection-driven promoter decryptification.
Microbiology (Reading, England). 2015 Feb; 161(Pt 2):354-61. doi:10.1099/mic.0.000001. PMID:25473090
Differences in the roles of a glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase between Bacillus circulans and Bacillus subtilis.
Bioscience, biotechnology, and biochemistry. 2013; 77(7):1481-5. . PMID:23832367
Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis.
Biochemistry. 2009 Mar 10; 48(9):1928-35. doi:10.1021/bi801887r. PMID:19152323
Structure of a bacterial pyridoxal 5'-phosphate synthase complex.
Proceedings of the National Academy of Sciences of the United States of America. 2006 Dec 19; 103(51):19284-9. . PMID:17159152
yaaD and yaaE are involved in vitamin B6 biosynthesis in Bacillus subtilis.
Journal of bioscience and bioengineering. 2002; 93(3):309-12. . PMID:16233205
On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis.
The Journal of biological chemistry. 2005 Sep 16; 280(37):32291-300. . PMID:16030023
A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase.
The Journal of biological chemistry. 2005 Jul 29; 280(30):27914-23. . PMID:15911615
Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis.
Journal of bacteriology. 2004 Feb; 186(4):1191-6. . PMID:14762015
The Spo0A regulon of Bacillus subtilis.
Molecular microbiology. 2003 Dec; 50(5):1683-701. . PMID:14651647
Three-dimensional structure of YaaE from Bacillus subtilis, a glutaminase implicated in pyridoxal-5'-phosphate biosynthesis.
The Journal of biological chemistry. 2004 Jan 23; 279(4):2704-11. . PMID:14585832
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Time of last update: 2025-04-07 11:00:33
Author of last update: Jstuelk