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PROSITE documentation PDOC00949 |
The term vitamin B6 is used to refer collectively to the compound pyridoxine and its vitameric forms, pyridoxal, pyridoxamine, and their phosphorylated derivatives. Vitamin B6 is required by all organisms and plays an essential role as a co-factor for enzymatic reactions. Plants, fungi, bacteria, archaebacteria, and protists synthetize vitamin B6. Animals and some highly specialized obligate pathogens obtain it nutritionally. Vitamin B6 has two distinct biosynthetic pathways, which do not coexist in any organism. The pdxA/pdxJ pathway, that has been extensively characterized in Escherichia coli, is found in the γ subdivision of the proteobacteria. A second pathway of vitamin B6 synthesis involving the pdxS/SNZ and pdxT/SNO (see <PDOC00950>) protein families, which are completely unrelated in sequence to the pdxA/pdxJ proteins, is found in plants, fungi, protists, archaebacteria, and most bacteria.
PdxS/SNZ and pdxT/SNO proteins form a complex which serves as a glutamine amidotransferase to supply ammonia as a source of the ring nitrogen of vitamin B6 [1]. PdxT/SNO and pdxS/SNZ appear to encode respectively the glutaminase subunit, which produces ammonia from glutamine, and the synthase subunit, which combines ammonia with five- and three-carbon phosphosugars to form vitamin B6 [2].
Proteins belonging to the pdxS/SNZ family occur in organisms in four kingdoms and form one of the most highly conserved family [3]. PdxS/SNZ proteins have a classic (β/α)8-barrel fold, consisting of eight parallel β-strands alternating with eight α helices (see <PDB:1ZNN>) [4].
Some proteins belonging to the pdxS/SNZ family are listed below:
These are hydrophilic proteins of about 32 Kd. They can be picked up in the database by the following pattern. We also developed a profile for the pdxS/ SNZ family.
Last update:June 2005 / Text revised; profile added.
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PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Dong Y.-X. Sueda S. Nikawa J.-I. Kondo H. |
Title | Characterization of the products of the genes SNO1 and SNZ1 involved in pyridoxine synthesis in Saccharomyces cerevisiae. | |
Source | Eur. J. Biochem. 271:745-752(2004). | |
PubMed ID | 14764090 |
2 | Authors | Belitsky B.R. |
Title | Physical and enzymological interaction of Bacillus subtilis proteins required for de novo pyridoxal 5'-phosphate biosynthesis. | |
Source | J. Bacteriol. 186:1191-1196(2004). | |
PubMed ID | 14762015 |
3 | Authors | Ehrenshaft M. Bilski P. Li M.Y. Chignell C.F. Daub M.E. |
Title | A highly conserved sequence is a novel gene involved in de novo vitamin B6 biosynthesis. | |
Source | Proc. Natl. Acad. Sci. U.S.A. 96:9374-9378(1999). | |
PubMed ID | 10430950 |
4 | Authors | Zhu J. Burgner J.W. Harms E. Belitsky B.R. Smith J.L. |
Title | A new arrangement of (beta /alpha )8 barrels in the synthase subunit of PLP synthase. | |
Source | J. Biol. Chem. 280:0-0(2005). | |
PubMed ID | 15911615 | |
DOI | 10.1074/jbc.M503642200 |