Evidence map›Paper›PMID 40082627›Full record

ArticleScientific reports2025

Homologous relationship between FabG involved in fatty acid biosynthesis and SDR on chromosome II in the multi-chromosome pathogen Vibrio anguillarum.

Dong-Gyun Kim, So Young Park, S M Rafiquzzaman, Jong Min Lee

Abstract read
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Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

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2citing papers in PubMed
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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Live and heat-treatediScience · 2026
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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Dong-Gyun Kim *Biotechnology Research Division, National Institute of Fisheries Science, Busan, Republic of Korea.
So Young Park *Department of Biotechnology, Pukyong National University, Busan, 48513, Republic of Korea.
S M RafiquzzamanDepartment of Fisheries Biology and Aquatic Environment, BSMRAU, Gazipur, Bangladesh.
Jong Min LeeDepartment of Biotechnology, Pukyong National University, Busan, 48513, Republic of Korea. jmlee84@pknu.ac.kr.

Funding

National Institute of Fisheries Science, Ministry of Oceans and Fisheries, Korea R2024053
6 · The paper itself

Abstract

Vibrio anguillarum threatens fish and larval farming industries and human health worldwide. The identification of bacterial adaptation and responses to stress due to environmental changes is vital for establishing a response strategy for pathogenic Vibrio. Previously, short-chain dehydrogenase/reductase (SDR) was identified on chromosome II of the multichromosomal V. anguillarum. In this study, a comparison of SDR and the enzyme FabG-1b (encoded on chromosome I and responsible for the β-ketoacyl acyl carrier protein (ACP) reductase in fatty acid biosynthesis (FAS II)) showed that the amino acid sequence homology was only 33.2%; however, the core of functionality, which includes the NAD(P)-binding domain and the conserved region of the active site, the topologies predicted using sequence-based homology modeling, and the quaternary homotetramer-type structures showed a significant similarity. FabG-1b was specific to the substrates fluorinated and halogenated aliphatic ketones, aromatic ketones, and aromatic β-ketoesters and SDR toward non-fluorinated and non-halogenated aliphatic ketones, aromatic ketones, and non-aromatic β-ketoesters. This complementary catalytic efficiencies of the two enzymes on various substrates conclusively supports the hypothesis that the two enzymes are likely homologs. This is the first study to report potential paralogous enzymes FabG-1b and SDR in Vibrio. This information improves our understanding of bacterial FAS for establishing strategies to overcome infectious diseases caused by pathogenic strains and identify targets for developing new antibacterial agents.

Indexed as

Bacterial ProteinsChromosomes, BacterialFatty AcidsVibrioAmino Acid SequenceModels, MolecularSubstrate SpecificityBacterial ProteinsFatty AcidsFabGFatty acid biosynthesisParalogsShort-chain dehydrogenase/reductase (SDR)Vibrio anguillarumβ-ketoacyl acyl carrier protein (ACP) reductase

Identifiers

PMID40082627
PMCPMC11906770

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.