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Literature summary extracted from

  • Tavares, N.K.; VanDrisse, C.M.; Escalante-Semerena, J.C.
    Rhodobacterales use a unique L-threonine kinase for the assembly of the nucleotide loop of coenzyme B12 (2018), Mol. Microbiol., 110, 239-261 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.177 gene blueE, encded in the bluFEDCB operon, phylogenetic analysis, recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain, functional complementation of a Rhodobacter sphaeroides DELTAcobB strain, recombinant overproduction of RsBluE results in the production of substantial quantities of insoluble protein in Escherichia coli Cereibacter sphaeroides

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.177 additional information recombinant expression of Rhodobacter sphaeroides BluE restores AdoCbl-dependent growth of a Salmonella enterica DELTApduX strain. Cultures of strains producing RsBluE or SePduX display a much shorter lag time (12 and 16 h, respectively) than cultures of the wild-type strain carrying the empty cloning vector, or the strain producing RcBluE (26 h). Inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium Cereibacter sphaeroides

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.177 Ca2+ activates at low concentration, but inhibits 75% at 100 mM Cereibacter sphaeroides
2.7.1.177 L-Ser at higher concentrations Cereibacter sphaeroides

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.177 Ca2+ activates at low concentration, but inhibits 75% at 100 mM Cereibacter sphaeroides
2.7.1.177 Co2+ very low acctivation Cereibacter sphaeroides
2.7.1.177 Mg2+ activates Cereibacter sphaeroides
2.7.1.177 Mn2+ required, activates Cereibacter sphaeroides
2.7.1.177 additional information a divalent metal ion (1 mM) is required for RsBluE ATPase activity, with optimal activity observed with MnCl2 Cereibacter sphaeroides
2.7.1.177 Ni2+ activates Cereibacter sphaeroides
2.7.1.177 Zn2+ activates Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.177 ATP + L-threonine Cereibacter sphaeroides
-
 ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine Cereibacter sphaeroides ATCC 17023
-
 ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine Cereibacter sphaeroides NCIB 8253
-
 ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine Cereibacter sphaeroides DSM 158
-
 ADP + O-phospho-L-threonine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.177 Cereibacter sphaeroides Q3IZR9
-
-
2.7.1.177 Cereibacter sphaeroides ATCC 17023 Q3IZR9
-
-
2.7.1.177 Cereibacter sphaeroides DSM 158 Q3IZR9
-
-
2.7.1.177 Cereibacter sphaeroides NCIB 8253 Q3IZR9
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.177 ATP + L-threonine
-
 Cereibacter sphaeroides ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine
-
 Cereibacter sphaeroides ATCC 17023 ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine
-
 Cereibacter sphaeroides NCIB 8253 ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 ATP + L-threonine
-
 Cereibacter sphaeroides DSM 158 ADP + O-phospho-L-threonine
-
 ?
2.7.1.177 additional information RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate Cereibacter sphaeroides ?
-
-
2.7.1.177 additional information RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate Cereibacter sphaeroides ATCC 17023 ?
-
-
2.7.1.177 additional information RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate Cereibacter sphaeroides NCIB 8253 ?
-
-
2.7.1.177 additional information RsBluE has L-Thr kinase activity in vitro, no or poor activity with L-serine, L-tyrosine, D-serine, D-threonine, or L-valine. RsBluE hydrolyzed ATP in the absence of L-Thr, the RsBluE ATPase activity is independent of potential amino acid substrate Cereibacter sphaeroides DSM 158 ?
-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.1.177 bluE
-
 Cereibacter sphaeroides
2.7.1.177 RsBluE
-
 Cereibacter sphaeroides
2.7.1.177 RSP_0788 locus name Cereibacter sphaeroides

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.177 25
-
-
 Cereibacter sphaeroides

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.177 ATP
-
 Cereibacter sphaeroides

General Information

EC Number General Information Comment Organism
2.7.1.177 evolution Rhodobacterales lack pduX, instead they have the non-orthologous bluE gene that encodes an enzyme that, unlike PduX, is specific for L-Thr and cannot use L-Ser. Phylogenetic analysis. The RsBluE enzyme is found to be restricted to a subclass of Rhodobacterales with genetic attributes that indicate they have a strong preference for AdoCbl. That is to say, these Rhodobacter species prefer and synthesize only a cobamide (Cba) with DMB as the lower ligand base and AP-P as the nucleotide linker, Coalpha-(alpha-5,6-dimethylbenzimidazolyl-Cobeta-adenosylcobamide) (a.k.a. adenosylcobalamin, AdoCbl, coenzyme B12, CoB12). Cells with incomplete AdoCbl production have a pigmentation phenotype Cereibacter sphaeroides
2.7.1.177 malfunction inactivation of gene bluE in Rhodobacter sphaeroides causes AdoCbl-dependent growth phenotypes, DELTAbluE strains fail to grow compared to bluE+ controls. A blush phenotype for the DELTAbluE strain is observed and the amount of light-harvesting complex 1 (LH1 B875) reaction center pigments of this strain are reduced relative to those in cultures of the DELTAbluE strain growing in the presence of AdoCbl after measurements are normalized for the cell density of each culture. The blush phenotype is also corrected by the addition of CNCbl to the medium Cereibacter sphaeroides
2.7.1.177 metabolism enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales Cereibacter sphaeroides