Comparative In Silico Profiling of Anthocyanin Biosynthetic Enzymes in Oryza Species: Evolutionary Conservation versus Functional Diversification

DOI

10.2991/978-94-6239-821-4_4How to use a DOI?

Keywords

Oryza sativa; anthocyanin biosynthesis; LOD1; glycosyl transferase; malonyl transferase; phylogenetic analysis

Abstract

Anthocyanins, a class of flavonoid pigments, underlie plant coloration, environmental stress resilience, and dietary value. Whether the enzymes governing anthocyanin formation are equally constrained across cultivated rice and its wild relatives, or diverge unevenly along the pathway, remains poorly resolved at the sequence level. We addressed this through a comparative bioinformatic evaluation of three enzymes central to the late stages of anthocyanin biosynthesis—leucoanthocyanidin dioxygenase 1 (LOD1/ANS), glycosyl transferase, and malonyl transferase—across four Oryza taxa: cultivated O. sativa aus N22 and the wild relatives O. nivara, O. rufipogon, and O. punctata. Multiple sequence alignment coupled with phylogenetic reconstruction placed glycosyl transferase as the most conserved of the three loci (92.08–100% identity) and showed its topology tracking genome-level relatedness (AA- versus BB-genome accessions) closely, while malonyl transferase displayed the widest divergence (56.48–95.25%) and, notably, departed from that same genome-relatedness structure in the O. rufipogon lineage. Physicochemical profiling indicated that LOD1 and glycosyl transferase are consistently stable, hydrophilic, acidic polypeptides, whereas malonyl transferase showed more variable stability indices and an isoelectric point range that crosses from acidic to basic across taxa, implying a shift in net charge at physiological pH not seen in the other two enzymes. Subcellular localization predictions placed LOD1 and malonyl transferase in the cytoplasm and glycosyl transferase in the chloroplast, a pattern conserved across all four taxa despite chloroplast targeting being atypical for this enzyme family. Mapping these enzymes onto the KEGG anthocyanin pathway situated this conservation gradient within a broader, chemically plausible logic: catalytically constrained, substrate-specific reactions (LOD1, glycosylation) are tightly conserved, while the terminal, acyl-donor-flexible modification step (malonylation) is comparatively free to diversify. Collectively, these results point to strong purifying constraint on the core biosynthetic machinery alongside more permissive, lineage-specific evolution of the terminal modification step, a pattern with implications for understanding pigment diversity across the genus Oryza.

Copyright

© 2026 The Author(s)

Open Access

Open Access This chapter is licensed under the terms of the Creative Commons Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/), which permits any noncommercial use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license and indicate if changes were made.

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TY  - CONF
AU  - R. Shravani
AU  - B. Swathi
AU  - G. Dhanalakshmi
PY  - 2026
DA  - 2026/10/31
TI  - Comparative In Silico Profiling of Anthocyanin Biosynthetic Enzymes in Oryza Species: Evolutionary Conservation versus Functional Diversification
BT  - Proceedings of the International Conference on Information Systems Design And Intelligent Applications (ICISDA 2026)
PB  - Atlantis Press
SP  - 27
EP  - 42
SN  - 1951-6851
UR  - https://doi.org/10.2991/978-94-6239-821-4_4
DO  - 10.2991/978-94-6239-821-4_4
ID  - Shravani2026
ER  -