A New Class of Phosphoribosyltransferases Involved in Cobamide Biosynthesis Is Found in Methanogenic Archaea and Cyanobacteria

Jeter, Victoria L.; Mattes, Theodoric A.; Beattie, Nathaniel R.; Escalante-Semerena, Jorge C.

doi:10.1021/acs.biochem.8b01253

Cited by 15Porphyrin Metabolism and DisordersBiochemical and Molecular ResearchMetalloenzymes and iron-sulfur proteins

A New Class of Phosphoribosyltransferases Involved in Cobamide Biosynthesis Is Found in Methanogenic Archaea and Cyanobacteria

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Jeter, Victoria L., Mattes, Theodoric A., Beattie, Nathaniel R., Escalante-Semerena, Jorge C.·2019·Biochemistry

DOI 10.1021/acs.biochem.8b01253PMC PMC6380956

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Abstract

Cobamides are coenzymes used by cells from all domains of life but made de novo by only some bacteria and archaea. The last steps of the cobamide biosynthetic pathway activate the corrin ring and the lower ligand base, condense the activated intermediates, and dephosphorylate the product prior to the release of the biologically active coenzyme. In bacteria, a phosphoribosyltransferase (PRTase) enyzme activates the base into its α-mononucleotide. The enzyme from Salmonella enterica ( SeCobT) has been extensively biochemically and structurally characterized. The crystal structure of the putative PRTase from the archaeum Methanocaldococcus jannaschii ( MjCobT) is known, but its function has not been validated. Here we report the in vivo and in vitro characterization of MjCobT. In vivo, in vitro, and phylogenetic data reported here show that MjCobT belongs to a new class of NaMN-dependent PRTases. We also show that the Synechococcus sp. WH7803 CobT protein has PRTase activity in vivo. Lastly, results of isothermal titration calorimetry and analytical ultracentrifugation analysis show that the biologically active form of MjCobT is a dimer, not a trimer, as suggested by its crystal structure.

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Archaeal and bacterial CobT proteins are not homologous.
“Archaeal and bacterial CobT proteins are not homologous, as previously reported [119].”
From Evidence for corrin biosynthesis in the last universal common ancestor (2025) · cites this paper as [119]
The Introduction calls the archaeal proteins “SeCobT homologues” and reports 18% sequence identity between the archaeal and bacterial enzymes. The Concluding Remarks describe their CobT groups as highly divergent, not nonhomologous. Page numbers were not supplied in our copy. (LLM, conf=0.84)
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Authors: Jeter, V. L., Mattes, T. A., Beattie, N. R., & Escalante-Semerena, J. C.
Affiliations: University of Georgia (US)
ORCID: Jeter, Victoria L.
Mattes, Theodoric A.
Escalante-Semerena, Jorge C.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2019-01-14
Volume: 58
Issue: 7
Pages: 951-964
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/acs.biochem.8b01253
PMC: PMC6380956
OpenAlex: W2910920261
Cited by: 15
References: 45
Citations by year: 2025: 1 · 2024: 3 · 2023: 2 · 2022: 4 · 2021: 1 · 2020: 3 · 2019: 1
FWCI: 0.74
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-045 (stm-asf)
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of General Medical Sciences (R37-GM40313, R37-GM040313)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
Keywords: phosphoribosyltransferase, vitamin B12, vitamin B12 biosynthesis, Methanococcus jannaschii, methanogenic archaea, cyanobacteria, protein dimerization
MeSH terms: Cyanobacteria, Archaea, Bacterial Proteins, Cobamides, Hydrogen-Ion Concentration, Multienzyme Complexes, Nucleotidyltransferases, Osmolar Concentration, Pentosyltransferases, Phosphates, Phylogeny, Substrate Specificity, Methanococcus, Potassium Compounds, Salmonella enterica, Archaeal Proteins

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A New Class of Phosphoribosyltransferases Involved in Cobamide Biosynthesis Is Found in Methanogenic Archaea and Cyanobacteria

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