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Information on EC 5.3.3.23 - S-methyl-5-thioribulose 1-phosphate isomerase
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5.3.3.23 S-methyl-5-thioribulose 1-phosphate isomeraseIUBMB Comments
The enzyme, characterized from the bacterium Rhodospirillum rubrum, participates in methionine salvage from S-methyl-5'-thioadenosine. It is a RubisCO-like protein (RLP) that is not capable of carbon fixation, and catalyses an isomerization reaction that converts S-methyl-5-thio-D-ribulose 1-phosphate to a 3:1 mixture of S-methyl-1-thioxylulose 5-phosphate and S-methyl-1-thioribulose 5-phosphate. The reaction is an overall 1,3-proton transfer, which likely consists of two 1,2-proton transfer events.
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The expected taxonomic range for this enzyme is: Rhodospirillum rubrum
Reaction Schemes
Synonyms
5-methylthioribulose-1-phosphate isomerase, ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein, RLP, rlp Rru_A1998, RuBisCO-like protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-methylthioribulose-1-phosphate isomerase
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incorrect
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ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein
RLP
rlp Rru_A1998
RuBisCO-like protein
ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein
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ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein
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ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein
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ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein
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ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein
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RLP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thio-D-ribulose 5-phosphate
(2)
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S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thio-D-ribulose 5-phosphate
(2), the enzyme from Rhodospirillum rubrum catalyzes an isomerization reaction (overall 1,3-proton transfer reaction, likely, two 1,2-proton transfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate
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S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thio-D-xylulose 5-phosphate
(1)
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-
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S-methyl-5-thio-D-ribulose 1-phosphate = S-methyl-1-thio-D-xylulose 5-phosphate
(1), the enzyme from Rhodospirillum rubrum catalyzes an isomerization reaction (overall 1,3-proton transfer reaction, likely, two 1,2-proton transfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-methyl-5-thio-D-ribulose 1-phosphate 1,3-isomerase
The enzyme, characterized from the bacterium Rhodospirillum rubrum, participates in methionine salvage from S-methyl-5'-thioadenosine. It is a RubisCO-like protein (RLP) that is not capable of carbon fixation, and catalyses an isomerization reaction that converts S-methyl-5-thio-D-ribulose 1-phosphate to a 3:1 mixture of S-methyl-1-thioxylulose 5-phosphate and S-methyl-1-thioribulose 5-phosphate. The reaction is an overall 1,3-proton transfer, which likely consists of two 1,2-proton transfer events.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
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-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-ribulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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-
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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-
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
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-
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r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
-
r
S-methyl-5-thio-D-ribulose 1-phosphate
S-methyl-1-thio-D-xylulose 5-phosphate
-
-
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r
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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the RLP can catalyze an overall 1,3-proton transfer reaction via two successive 1,2-proton transfer reactions initiated by abstraction of the 3-proton of the substrate, and the RLP catalyzes a second 1,2-proton transfer reaction initiated by abstraction of the 4-proton from the 3-oxo intermediate to generate a second 3,4-enediolate anion. A bidentate coordination with Mg2+ to stabilize both the 2,3- and 3,4-enediolate intermediates is expected to require movement of the Mg2+ and/or the substrate on the reaction coordinate, although the same base could catalyze abstraction of a proton from carbon-3 of the substrate and carbon-4 of the presumed 3-keto intermediate. Continuous monitoring of the reaction by 1H NMR does not reveal transient accumulation of the 3-keto intermediate, suggesting that it remains enzyme-bound during the course of the reaction
evolution
in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
evolution
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the enzyme is a member of the RuBisCO superfamily, RuBisCO catalyzes carboxylation and oxygenation, while the enzyme from Rhodospirillum rubrum catalyzes isomerizations, overview. Rhodospirillum rubrum encodes an RLP that is a member of an uncharacterized family of RLPs which contain a KDDH motif instead of the signature KDDE motif. Like the tautomerases, the sequences contain hydrophobic residues (Pro and Ile/Val) for the formation of a hydrophobic binding pocket for the distal portion of the substrate. The enzyme is able to utilize 5'-methythioadenosine (MTA) as a sulfur source
evolution
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in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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evolution
-
in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
-
evolution
-
in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
-
evolution
-
in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
-
evolution
-
in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
-
evolution
-
in contrast to true D-ribulose-1,5-bisphosphate carboxylase/oxygenases (RubisCOs), ribulose-1,5-bisphosphate carboxylase/oxygenase-like protein s (RLPs) lack essential, conserved active site residues. Consequently, none of these proteins tested so far has been shown to catalyze the carboxylation of D-ribulose-1,5-bisphosphate. Based on phylogenetic analysis, active site differences and genome context, at least six different RLP-subfamilies are identified that are assumed to use different substrates and catalyze different reactions
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malfunction
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disruption of the gene encoding the RLP abolishes the ability of Rhodospirillum rubrum to utilize 5'-methylthioadenosine (MTA) as a sole sulfur source, implicating a distinct pathway for sulfur salvage
malfunction
disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
malfunction
-
disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
-
disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
-
disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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malfunction
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disruption of the RLP gene results in a 5'-methylthioadenosine (MTA)-deficient growth phenotype under aerobic conditions
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metabolism
the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
metabolism
-
the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
-
metabolism
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the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
-
metabolism
-
the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
-
metabolism
-
the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
-
metabolism
-
the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
-
metabolism
-
the Rhodospirillum rubrum genome lacks most of the canonical methionine salvage pathway genes and, therefore, might use an alternative strategy to utilize 5'-methylthioadenosine (MTA) aerobically as its sole sulfur source. Rhodospirillum rubrum RLP is involved in another central metabolic pathway, in which the polyamine biosynthesis dead-end product MTA is channelled into isoprenoid metabolism with concomitant release of the volatile gas methanethiol. The proposed MTA-isoprenoid pathway fits to the organism's physiology, and phylogenetic analysis indicate that a number of organisms make use of this metabolic shunt. Overview
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physiological function
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some homologues of D-ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) do not catalyze carboxylation and are designated RuBisCO-like proteins (RLPs). The RLP enzyme from Rhodospirillum rubrum catalyzes an isomerization reaction (overall 1,3-proton transfer reaction, likely, two 1,2-proton transfer reactions) that converts 5-methylthio-D-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate. Role of this RLP in a sulfur salvage pathway
physiological function
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
physiological function
-
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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physiological function
-
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
-
physiological function
-
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
-
physiological function
-
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
-
physiological function
-
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
-
physiological function
-
the Rhodospirillum rubrum RLP enzyme functions in 5'-methylthioadenosine (MTA) metabolism. Wild type Rhodospirillum rubrum can grow with MTA as sole source of sulfur. When incubated in vitro with 5-methylthio-D-ribulose-1-phosphate (MTRu-1P), an intermediate of the canonical methionine salvage pathway, recombinant Rhodospirillum rubrum RLP catalyzes a 1,3-isomerization reaction (presumably two successive 1,2-isomerization reactions) to yield a 1:3 mixture of 1-methylthio-ribulose-5-phosphate (MTRu-5P) and 1-methylthio-xylulose-5-phosphate (MTXu-5P)
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RLP_RHORT
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)
374
0
38880
Swiss-Prot
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Imker, H.; Singh, J.; Warlick, B.; Tabita, F.; Gerlt, J.
Mechanistic diversity in the RuBisCO superfamily a novel isomerization reaction catalyzed by the RuBisCO-like protein from Rhodospirillum rubrum
Biochemistry
47
11171-11173
2008
Rhodospirillum rubrum
brenda
Erb, T.; Evans, B.; Cho, K.; Warlick, B.; Sriram, J.; Wood, B.; Imker, H.; Sweedler, J.; Tabita, F.; Gerlt, J.
A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis
Nat. Chem. Biol.
8
926-932
2012
Rhodospirillum rubrum (Q2RSU7), Rhodospirillum rubrum S1 (Q2RSU7), Rhodospirillum rubrum NCIMB 8255 (Q2RSU7), Rhodospirillum rubrum ATH 1.1.1 (Q2RSU7), Rhodospirillum rubrum ATCC 11170 (Q2RSU7), Rhodospirillum rubrum LMG 4362 (Q2RSU7), Rhodospirillum rubrum DSM 467 (Q2RSU7)
brenda
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