Premium
Diversity and evolutionary analysis of iron‐containing (Type‐III) alcohol dehydrogenases in the three domains of life
Author(s) -
JuliánSánchez Adriana,
GaonaLópez Carlos,
RiverosRosas Héctor
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.lb91
Subject(s) - subfamily , biology , archaea , alcohol dehydrogenase , phylogenetic tree , genetics , protein family , bacteria , evolutionary biology , biochemistry , enzyme , gene
Alcohol dehydrogenase (ADH) activity is widely distributed in the three domains of life. Currently, there are three non‐homologous NAD(P) + ‐dependent ADH families reported: Type I ADH comprises Zn‐dependent ADHs; type II ADH comprises short‐chain ADHs described first in Drosophila; and, type III ADH comprises iron‐containing ADHs (FeADHs). These three families arose independently throughout evolution and possess different structures and mechanisms of reaction. While types I and II ADHs have been extensively studied, type III (iron‐activated) ADHs have been scarcely analyzed. Therefore in this work, a global phylogenetic analysis of iron‐activated ADHs was performed to get insights into the evolution of this protein family. Results showed that FeADHs are distributed in twenty two protein subfamilies, eight of them possessing protein sequences distributed in the three domains of life. Protein sequences from bacteria are present in all FeADH subfamilies, but protein sequences from archaea and eukarya are present in fourteen and thirteen subfamilies, respectively. Interestingly, none of these protein subfamilies possess protein sequences found simultaneously in the three main eukaryotic kingdoms (i.e., animals, plants and fungi). Animal FeADHs are found in just one protein subfamily, the hydroxyacid‐oxoacid transhydrogenase (HOT) subfamily, which includes protein sequences widely distributed in fungi, but not in plants), and in several taxa from lower eukaryotes, bacteria and archaea. Fungi FeADHs are found mainly in two subfamilies: HOT and maleylacetate reductase (MAR), but some can be found also in other three different protein subfamilies. Plant FeADHs are found only in chlorophyta but not in higher plants, and are distributed in three different protein subfamilies. In conclusion, FeADH is an ancient protein family that probably was present in the last common ancestor, and comprises a diversity of subfamilies that shares a common 3D scaffold that resulted with a patchy distribution in eukaryotes. Support or Funding Information Supported by DGAPA‐UNAM grant IN225016.