title: Potential Role of Acetyl-CoA Synthetase (acs) and Malate Dehydrogenase (mae) in the Evolution of the Acetate Switch in Bacteria and Archaea.
abstract: Although many Archaea have AMP-Acs (acetyl-coenzyme A synthetase) and ADP-Acs, the extant methanogenic genus Methanosarcina is the only identified Archaeal genus that can utilize acetate via acetate kinase (Ack) and phosphotransacetylase (Pta). Despite the importance of ack as the potential urkinase in the ASKHA phosphotransferase superfamily, an origin hypothesis does not exist for the acetate kinase in Bacteria, Archaea, or Eukarya. Here we demonstrate that Archaeal AMP-Acs and ADP-Acs contain paralogous ATPase motifs previously identified in Ack, which demonstrate a novel relation between these proteins in Archaea. The identification of ATPase motif conservation and resulting structural features in AMP- and ADP-acetyl-CoA synthetase proteins in this study expand the ASKHA superfamily to include acetyl-CoA synthetase. Additional phylogenetic analysis showed that Pta and MaeB sequences had a common ancestor, and that the Pta lineage within the halophilc archaea was an ancestral lineage. These results suggested that divergence of a duplicated maeB within an ancient halophilic, archaeal lineage formed a putative pta ancestor. These results provide a potential scenario for the establishment of the Ack/Pta pathway and provide novel insight into the evolution of acetate metabolism for all three domains of life.
authors.affiliation: 1] Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA [2] Center for Biofilm Engineering, Montana State University, Bozeman, MT, USA [3] US Geological Survey, Helena, MT, USA.
authors.forename: Elliott P
authors.initials: EP
authors.lastname: Barnhart
authors.affiliation: Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA.
authors.forename: Marcella A
authors.initials: MA
authors.lastname: McClure
authors.affiliation: Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA.
authors.forename: Kiki
authors.initials: K
authors.lastname: Johnson
authors.affiliation: Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA.
authors.forename: Sean
authors.initials: S
authors.lastname: Cleveland
authors.affiliation: 1] Center for Biofilm Engineering, Montana State University, Bozeman, MT, USA [2] Department of Chemical and Biological Engineering, Montana State University, Bozeman, MT, USA.
authors.forename: Kristopher A
authors.initials: KA
authors.lastname: Hunt
authors.affiliation: 1] Department of Microbiology and Immunology, Montana State University, Bozeman, MT, USA [2] Center for Biofilm Engineering, Montana State University, Bozeman, MT, USA [3] Energy Research Institute, Montana State University, Bozeman, MT, USA [4] ENIGMA, Lawrence Berkeley National Laboratory, Berkeley, CA, USA [5] National Center for Genome Resources, Santa Fe, NM, USA.
authors.forename: Matthew W
authors.initials: MW
authors.lastname: Fields
mesh_terms: D000084:Acetate Kinase / Q000737:chemistry / Q000378:metabolism; D000106:Acetate-CoA Ligase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000085:Acetates / Q000378:metabolism*; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005075:Biological Evolution; D017124:Conserved Sequence; D019143:Evolution, Molecular; D016931:Halobacteriales / Q000201:enzymology / Q000235:genetics; D008291:Malate Dehydrogenase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017020:Methanosarcina / Q000235:genetics / Q000378:metabolism; D010709:Phosphate Acetyltransferase / Q000737:chemistry / Q000378:metabolism; D010802:Phylogeny; D013379:Substrate Specificity
chemical_list: D000085:Acetates; D019843:Archaeal Proteins; D001426:Bacterial Proteins; D008291:Malate Dehydrogenase; D010709:Phosphate Acetyltransferase; D000084:Acetate Kinase; D000106:Acetate-CoA Ligase