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Mucilaginibacter florum sp. nov., isolated from the flower of Coreopsis grandiflora and Mucilaginibacter oryzagri sp. nov., isolated from rice paddy soil in Korea
Parthiban Subramanian, Jun Heo, Daseul Lee, Seunghwan Kim, Hyorim Choi, Yunhee Choi, Yiseul Kim
J. Microbiol. 2025;63(12):e2509014.   Published online December 31, 2025
DOI: https://doi.org/10.71150/jm.2509014
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AbstractAbstract PDFSupplementary Material

Two aerobic, Gram-stain-negative, non-motile and rod-shaped bacterial strains designated GGG-R5T and M4-18T were isolated from flowers of golden wave (Coreopsis grandiflora) and rice paddy soil, respectively in the Republic of Korea. Both strains were pigmented and produced flexirubin-type pigments. Based on phylogenetic analysis using 16S rRNA gene sequence, both strains were placed within the genus Mucilaginibacter with M. agri R11T and M. jinjuensis YC7004T both being the closest relatives to GGG-R5T (97.7%) and in case of M4-18T, M. ginsenosidivorax KHI28T (98.5%) was the nearest neighbor. Characteristic to genus Mucilaginibacter, the major cellular fatty acids in both strains were iso-C15:0, iso-C17:0 3-OH, summed feature 3 (C16:1 ω7c and/or C16:1 ω6c); menaquinone-7 was the major menaquinone and phosphatidylethanolamine was the major polar lipid observed. Comparison of genome sequences with the other members of Mucilaginibacter indicated orthologous average nucleotide identity (orthoANI) at 73.3–73.5% for GGG-R5T and 78.9–88.5% for M4-18T. Digital DNA-DNA hybridization (dDDH) values ranged at 19.1–19.7% between GGG-R5T and its neighbor species. In case of M4-18T, the observed range was at 21.9–36.6%. Considering the 16S rRNA similarity, orthoANI and dDDH values as well as comparison of phenotypic and chemotaxonomic characteristics indicated that both strains belonged to genus Mucilaginibacter but were distinctly distinguishable from previously described species. The strains GGG-R5T and M4-18T, therefore represent distinct novel species for which names Mucilaginibacter florum GGG-R5T and Mucilaginibacter oryzagri M4-18T are proposed. The type strains are GGG-R5T (= KACC 22063T = JCM 36590T) and M4-18T (= KACC 22773T = JCM 35894T).

Journal Article
Regulatory role of cysteines in (2R, 3R)-butanediol dehydrogenase BdhA of Bacillus velezensis strain GH1-13
Yunhee Choi , Yong-Hak Kim
J. Microbiol. 2022;60(4):411-418.   Published online March 14, 2022
DOI: https://doi.org/10.1007/s12275-022-2018-y
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AbstractAbstract PDF
Bacillus velezensis strain GH1-13 contains a (2R,3R)-butanediol dehydrogenase (R-BDH) BdhA which converts acetoin to R-BD reversibly, however, little is known about its regulatory cysteine and biological significance. We performed sitedirected mutation of three cysteines in BdhA. The C37S mutant had no enzyme activity and the C34S and C177S mutants differed from each other and wild type (WT). After zinc affinity chromatography, 1 mM ZnCl2 treatment resulted in a 3-fold enhancement of the WT activity, but reduced activity of the C34S mutant by more than 2 folds compared to the untreated ones. However, ZnCl2 treatment did not affect the activity of the C177S mutant. Most of the double and triple mutant proteins (C34S/C37S, C34S/C177S, C37S/C177S, and C34S/C37S/C177S) were aggregated in zinc resins, likely due to the decreased protein stability. All of the purified WT and single mutant proteins increased multiple intermolecular disulfide bonds in the presence of H2O2 as the buffer pH decreased from 7.5 to 5.5, whereas an intramolecular disulfide bond of cysteine 177 and another cysteine in the CGIC motif region was likely formed at pH higher than pKa of 7.5. When pH varied, WT and its C34S or C177S mutants reduced acetoin to R-BD at the optimum pH 5.5 and oxidized R-BD to acetoin at the optimum pH 10. This study demonstrated that cysteine residues in BdhA play a regulatory role for the production of acetoin and R-BD depending on pH as well as metal binding and oxidative stress.

Citations

Citations to this article as recorded by  
  • Significantly enhanced specific activity of Bacillus subtilis (2,3)-butanediol dehydrogenase through computer-aided refinement of its substrate-binding pocket
    Bochun Hu, Xiaoqi Xi, Fugang Xiao, Xiaomeng Bai, Yuanyuan Gong, Yifan Li, Xueqin Qiao, Cunduo Tang, Jihong Huang
    International Journal of Biological Macromolecules.2024; 281: 136443.     CrossRef
  • Structural and enzymatic characterization of Bacillus subtilis R,R-2,3-butanediol dehydrogenase
    Xiaofei Wang, Lingyun Jia, Fangling Ji
    Biochimica et Biophysica Acta (BBA) - General Subjects.2023; 1867(4): 130326.     CrossRef
  • Engineering a BsBDHA substrate-binding pocket entrance for the improvement in catalytic performance toward (R)-phenyl-1,2-ethanediol based on the computer-aided design
    Bo-Chun Hu, Meng-Ran Li, Ying-Ying Li, Xin-Shuang Yuan, Yu-Ye Hu, Fu-Gang Xiao
    Biochemical Engineering Journal.2023; 194: 108907.     CrossRef

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