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Figure 3
Multiple sequence alignment of PsEst3 with eight homologs [Paenibacillus sp. 1_12 (UniProt accession No. A0A1I4E7Z0), P. thalictri (A0A4Q9DLG8), P. piri (A0A4R5KT22), P. whitsoniae (A0A430JH40), Paenibacillus sp. FSL H7-0357 (A0A089I8J6), Cohnella sp. CIP 111063 (A0A231R2L3), Alteribacillus persepolensis (A0A1G8AGB0) and Lihuaxuella thermophila (A0A1H8C781)] obtained from the BLAST results of PsEst3 using the UniProt database. The last two homologs (A0A1G8E3W4 and A0A1H8C781) that contain a GHSRG motif instead of GHSRA were added to the alignment. The secondary structure of PsEst3 is shown above the sequence. The pentapeptide sequence (GHSRA/G) and oxyanion hole-forming sequence (HGFR/K) are highlighted with blue and red rectangles, respectively. The catalytic triads and residues forming the acyl-binding pocket are indicated with black and red arrows, respectively.

IUCrJ
Volume 10| Part 2| March 2023| Pages 220-232
ISSN: 2052-2525
https://doi.org/10.1107/S2052252523001562