Cloned (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates at low concentration, but inhibits 75% at 100 mM | Cereibacter sphaeroides | |
L-Ser | at higher concentrations | Cereibacter sphaeroides |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | activates at low concentration, but inhibits 75% at 100 mM | Cereibacter sphaeroides | |
Co2+ | very low acctivation | Cereibacter sphaeroides | |
Mg2+ | activates | Cereibacter sphaeroides | |
Mn2+ | required, activates | Cereibacter sphaeroides | |
additional information | a divalent metal ion (1 mM) is required for RsBluE ATPase activity, with optimal activity observed with MnCl2 | Cereibacter sphaeroides | |
Ni2+ | activates | Cereibacter sphaeroides | |
Zn2+ | activates | Cereibacter sphaeroides |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine | Cereibacter sphaeroides | - |
ADP + O-phospho-L-threonine | - |
? | |
ATP + L-threonine | Cereibacter sphaeroides ATCC 17023 | - |
ADP + O-phospho-L-threonine | - |
? | |
ATP + L-threonine | Cereibacter sphaeroides NCIB 8253 | - |
ADP + O-phospho-L-threonine | - |
? | |
ATP + L-threonine | Cereibacter sphaeroides DSM 158 | - |
ADP + O-phospho-L-threonine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Cereibacter sphaeroides | Q3IZR9 | - |
- |
Cereibacter sphaeroides ATCC 17023 | Q3IZR9 | - |
- |
Cereibacter sphaeroides DSM 158 | Q3IZR9 | - |
- |
Cereibacter sphaeroides NCIB 8253 | Q3IZR9 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-threonine | - |
Cereibacter sphaeroides | ADP + O-phospho-L-threonine | - |
? | |
ATP + L-threonine | - |
Cereibacter sphaeroides ATCC 17023 | ADP + O-phospho-L-threonine | - |
? | |
ATP + L-threonine | - |
Cereibacter sphaeroides NCIB 8253 | ADP + O-phospho-L-threonine | - |
? | |
ATP + L-threonine | - |
Cereibacter sphaeroides DSM 158 | ADP + O-phospho-L-threonine | - |
? | |
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 | ? | - |
- |
|
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 | ? | - |
- |
|
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 | ? | - |
- |
|
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 | Comment | Organism |
---|---|---|
bluE | - |
Cereibacter sphaeroides |
RsBluE | - |
Cereibacter sphaeroides |
RSP_0788 | locus name | Cereibacter sphaeroides |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
- |
Cereibacter sphaeroides |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Cereibacter sphaeroides |
General Information | Comment | Organism |
---|---|---|
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 |
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 |
metabolism | enzyme BluE is the L-Thr kinase involved in AdoCbl biosynthesis in Rhodobacterales | Cereibacter sphaeroides |