Figure 2

Multiple sequence alignment of amino acid sequences of ACS from all three domains of life: Bacteria, Archaea and Eukaryota.

The alignment was generated with ClustalX 2.1. The ten conserved regions were highlighted by blue boxes. The three signature motifs (I–III) were highlighted in blue box. The red arrow indicated the lysine residue (K) essential for catalysis and posttranslational regulation. The black arrow indicated the aspartic acid residue (D) for the hinge of the N-terminus and the C-terminus. Name, NCBI accession numbers: for green algae: DtACS (in this study), D. tertiolecta, KT692941; CrACS, Chlamydomonas reinhardtii, XP_001700230.1; VcACS, Volvox carteri f. nagariensis, XP_002948463.1; T.ACS, Tetraselmis sp. GSL018, JAC81178.1; for Cyanobacteria: AvACS, Anabaena variabilis ATCC 29413, YP_321725.1; for archaebacteria: HmACS, Haloarcula marismortui, WP_011224682.1; AfACS, Archaeoglobus fulgidus DSM 4304, NP_069202.1; for higher plants: AtACS, Arabidopsis thaliana, NP_198504.1; GsACS, Glycine soja, KHN46374.1; S.ACS, Saccharum hybrid cultivar R570, AGT17010.1; for animals, HsACS, Homo sapiens, AAF75064.1; RnACS, Rattus norvegicus, NP_001101263.1; DrACS, Danio rerio, NP_001264046.1; for Bacteria: EcACS, Escherichia coli, WP_000078222.1; SeACS, Salmonella enterica, WP_031615207.1; MtACS, Mycobacterium tuberculosis, KHG66861.1; For fungi, AoACS, Aspergillus oryzae RIB40, XP_001820206.1; ScACS, Saccharomyces cerevisiae YJM789, EDN59709.1; for protists: CpACS, Cryptosporidium parvum, AAC47128.1; EmACS, Eimeria maxima, CDJ60264.1.