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Phylogenetic Analyses and Comparative Genomics of Vitamin B6 (Pyridoxine) and Pyridoxal Phosphate Biosynthesis Pathways

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J. Mol. Microbiol. Biotechnol. (2001) 3(1): 1-20. Different Pyridoxine and Pyridoxal Phosphate BiosynthesisJMMB Pathways Review 1 Phylogenetic Analyses and Comparative Genomics of Vitamin B6 (Pyridoxine) and Pyridoxal Phosphate Biosynthesis Pathways Gerhard Mittenhuber* bacterial lineage. This proposal might help to explain why the PdxA/PdxJ pathway is largely restricted to this Institut für Mikrobiologie und Molekularbiologie, Ernst- subdivision. Moritz-Arndt-Universität, F.-L. Jahnstr. 15, D-17487 Greifswald, Germany Introduction Pyridoxal 5'-phosphate (PLP), the active form of vitamin Abstract B6, is an essential cofactor of many enzymes involved in amino acid metabolism in all cells (for reviews see Dolphin Vitamin B6 in its active form pyridoxal phosphate is et al., 1986; Dakshinamurti, 1990). The most common an essential coenzyme of many diverse enzymes. reactions involve (1) transaminases catalyzing the Biochemistry, enzymology and genetics of de novo conversion of α-ketoacids to amino acids, and (2) amino vitamin B6 biosynthesis have been primarily acid racemases producing D-amino acids originating from investigated in Escherichia coli. Database searches L-amino acids (Grogan, 1988). But PLP is also a coenzyme revealed that the key enzymes involved in ring closure of (3) sulfinate desulfinase catalyzing the removal of of the aromatic pyridoxin ring (PdxA; PdxJ) are present elemental sulfur and selenium atoms from L-cysteine, L- mainly in genomes of bacteria constituting the γ cystine, L-selenocysteine, and L-selenocystine to produce subdivision of proteobacteria. The distribution of DXS, L-alanine (Mihara et al., 1997), (4) of glycogen a transketolase-like enzyme involved in vitamin B6 phosphorylases (Helmreich, 1992), (5) of biosynthesis as well as in thiamine and isoprenoid diaminopelargonic acid synthase, an enzyme involved in biosynthesis and the distribution of vitamin B6 biotin synthesis (Kack et al., 1999) and (6) of 1- modifying enzymes (PdxH: oxidase; PdxK: kinase) was aminocyclopropane-1-carboxylate synthase (Rottmann et also analyzed. These enzymes are also present in the al., 1991) synthesizing 1-aminocyclopropane-1-carboxylic genomes of animals. Two recent papers (Ehrenshaft acid (ACC) - the precursor of the plant hormone ethylene - et al., 1999, Proc. Natl. Acad. Sci. USA. 96 : 9374-9378; from S-adenosylmethionine. Despite these vast differences Osmani et al., 1999, J. Biol. Chem. 274 : 23565-23569) in the nature of the reactions catalyzed by PLP-dependent show the involvement of an extremely conserved enzymes, their three-dimensional structures share common protein (a member of the UPF0019 or SNZ family) found structural elements (Capitani et al., 1999, Denessiouk et in all three domains of life (bacteria, archaea, eukarya) al., 1999, Kack et al., 1999, Schneider et al., 2000). in an alternative vitamin B6 biosynthesis pathway. The biochemistry of de novo PLP biosynthesis has Members of this family were previously identified as a been studied in the gramnegative model organism stationary phase inducible protein in yeast, as an Escherichia coli (Hill and Spenser, 1996). Also, molecular ethylene responsible protein in plants and in a marine cloning and characterization of genes coding for enzymes sponge, as a singlet oxygen resistance protein in involved in PLP biosynthesis was performed using this Cercospora nicotianae and as a cumene organism, mainly by Malcolm E. Winkler and coworkers: hydroperoxide and H2O2 inducible protein in Bacillus The PLP precursor pyridoxine 5'-phosphate (PNP) is subtilis. In yeast, the SNZ protein interacts with another synthesized by the PdxA and PdxJ enzymes using 4- protein called SNO which also represents a member phosphohydroxy-L-threonine (4PHT; synonym: 3- of a highly conserved protein family (called UPF0030 hydroxyhomoserine) and 1-deoxy-D-xylulose 5-phosphate or SNO family). Phylogenetic trees for the DXS, PdxA, (DXP) as substrates (Lam et al., 1992; Zhao and Winkler, PdxJ, PdxH, PdxK, SNZ and SNO protein families are 1996; Cane et al., 1998; Laber et al, 1999). PNP is oxidized presented and possible implications of the two to the active coenzyme PLP by the action of PdxH oxidase, different vitamin B6 biosynthesis pathways in cellular a flavoprotein (Lam and Winkler, 1992; Zhao and Winkler, metabolism are discussed. A radically different view 1995; Notheis et al., 1995). of bacterial evolution (Gupta, 2000, Crit. Rev. Microbiol. The two substrates DXP and 4PHT are supplied by 26: 111-131) which proposes a linear rather than a two independent pathways (Figure 1), which are both linked treelike evolutionary relationship between procaryotic to carbohydrate metabolism, i.e. glycolysis and the pentose species indicates that the γ subdivision of phosphate cyle: DXP, which is also a precursor in proteobacteria represents the most recently evolved isoprenoid and thiamine (vitamin B1) biosynthesis (Begley et al., 1999) is synthesized by the transketolase-like Received August 2, 2000; accepted September 4, 2000. *For correspondence. Email [email protected] enzyme DXP-synthase (DXS) (Sprenger et al., 1997; Lois greifswald.de; Tel. +49-3834-864218; Fax. +49-3834-864202. et al., 1998) using pyruvate and D-glyceraldehyde-3- © 2001 Horizon Scientific Press Further Reading Caister Academic Press is a leading academic publisher of advanced texts in microbiology, molecular biology and medical research. 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The key enzymes PdxA and PdxJ catalyze synthesis of the pyridine ring. The precursors 4PHT and DXP can be readily produced from intermediates of the pentose phosphate cycle and of glycolysis, respectively. Table 1. A comparison of the genes encoding pyridoxal 5'-phosphate biosynthesis enzymes of E. coli and orthologous open reading frames found in the B. subtilis genome. E. coli genes Enzymatic function of gene product References Similarities Predicted enzymatic function of gene product Expectation value coding for in B. subtilis enzymes involved in pyridoxine biosynthesis gapA Glyceraldehyde 3-P dehydrogenase
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  • Complete Genome Sequence of Ferroglobus Placidus AEDII12DO

    Complete Genome Sequence of Ferroglobus Placidus AEDII12DO

    Standards in Genomic Sciences (2011) 5:50-60 DOI:10.4056/sigs.2225018 Complete genome sequence of Ferroglobus placidus AEDII12DO Iain Anderson,1* Carla Risso,2 Dawn Holmes,2 Susan Lucas,1 Alex Copeland,1 Alla Lapidus,1 Jan-Fang Cheng,1 David Bruce,1,3 Lynne Goodwin,1,3 Samuel Pitluck,1 Elizabeth Saunders,1,3 Thomas Brettin,1,3 John C. Detter,1,3 Cliff Han,1,3 Roxanne Tapia,1,3 Frank Larimer,4 Miriam Land,4 Loren Hauser,4 Tanja Woyke,1 Derek Lovley,2 Nikos Kyrpides,1 and Natalia Ivanova1 1DOE Joint Genome Institute, Walnut Creek, California, USA 2Microbiology Department, University of Massachusetts, Amherst, Massachusetts, USA 3Los Alamos National Laboratory, Los Alamos, New Mexico, USA 4Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA *Corresponding author: [email protected] Keywords: Archaea, Euryarchaeota, Archaeoglobales, hydrothermal vent, hyperthermophile, anaerobe Ferroglobus placidus belongs to the order Archaeoglobales within the archaeal phylum Euryar- chaeota. Strain AEDII12DO is the type strain of the species and was isolated from a shallow marine hydrothermal system at Vulcano, Italy. It is a hyperthermophilic, anaerobic chemoli- thoautotroph, but it can also use a variety of aromatic compounds as electron donors. Here we describe the features of this organism together with the complete genome sequence and anno- tation. The 2,196,266 bp genome with its 2,567 protein-coding and 55 RNA genes was se- quenced as part of a DOE Joint Genome Institute Laboratory Sequencing Program (LSP) project. Introduction Strain AEDII12DO (=DSM 10642) is the type strain Organism information of the species Ferroglobus placidus.
  • Metabolic Roles of Uncultivated Bacterioplankton Lineages in the Northern Gulf of Mexico 2 “Dead Zone” 3 4 J

    Metabolic Roles of Uncultivated Bacterioplankton Lineages in the Northern Gulf of Mexico 2 “Dead Zone” 3 4 J

    bioRxiv preprint doi: https://doi.org/10.1101/095471; this version posted June 12, 2017. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. 1 Metabolic roles of uncultivated bacterioplankton lineages in the northern Gulf of Mexico 2 “Dead Zone” 3 4 J. Cameron Thrash1*, Kiley W. Seitz2, Brett J. Baker2*, Ben Temperton3, Lauren E. Gillies4, 5 Nancy N. Rabalais5,6, Bernard Henrissat7,8,9, and Olivia U. Mason4 6 7 8 1. Department of Biological Sciences, Louisiana State University, Baton Rouge, LA, USA 9 2. Department of Marine Science, Marine Science Institute, University of Texas at Austin, Port 10 Aransas, TX, USA 11 3. School of Biosciences, University of Exeter, Exeter, UK 12 4. Department of Earth, Ocean, and Atmospheric Science, Florida State University, Tallahassee, 13 FL, USA 14 5. Department of Oceanography and Coastal Sciences, Louisiana State University, Baton Rouge, 15 LA, USA 16 6. Louisiana Universities Marine Consortium, Chauvin, LA USA 17 7. Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, 18 13288 Marseille, France 19 8. INRA, USC 1408 AFMB, F-13288 Marseille, France 20 9. Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia 21 22 *Correspondence: 23 JCT [email protected] 24 BJB [email protected] 25 26 27 28 Running title: Decoding microbes of the Dead Zone 29 30 31 Abstract word count: 250 32 Text word count: XXXX 33 34 Page 1 of 31 bioRxiv preprint doi: https://doi.org/10.1101/095471; this version posted June 12, 2017.