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Information on EC 1.21.98.3 - anaerobic magnesium-protoporphyrin IX monomethyl ester cyclase
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1.21.98.3 anaerobic magnesium-protoporphyrin IX monomethyl ester cyclaseIUBMB Comments
This radical AdoMet enzyme participates in the biosynthesis of chlorophyllide a in anaerobic bacteria, catalysing the formation of an isocyclic ring. Contains a [4Fe-4S] cluster and a cobalamin cofactor. The same transformation is achieved in aerobic organisms by the oxygen-dependent EC 1.14.13.81, magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase. Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
BChE, chlE, Cyan7425_4778, Cyan7822_3999, F_1025, Mg-protoporphyrin IX monomethyl ester cyclase, MPE cyclase, oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BChE
chlE
F_1025
Mg-protoporphyrin IX monomethyl ester cyclase
MPE cyclase
oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase
BChE
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MPE cyclase
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ambiguous
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oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase
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oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase
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oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase
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oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine = 131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
(1b)
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131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine = 3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
(1c)
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magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O = 131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
(1a)
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magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
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magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis
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magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis
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magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O = 3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
magnesium-protoporphyrin-IX 13-monomethyl ester,S-adenosyl-L-methionine:H2O oxidoreductase (hydroxylating)
This radical AdoMet enzyme participates in the biosynthesis of chlorophyllide a in anaerobic bacteria, catalysing the formation of an isocyclic ring. Contains a [4Fe-4S] cluster and a cobalamin cofactor. The same transformation is achieved in aerobic organisms by the oxygen-dependent EC 1.14.13.81, magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase. Some facultative phototrophic bacteria, such as Rubrivivax gelatinosus, possess both enzymes.
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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
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
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-
-
?
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
-
-
-
?
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
-
-
-
?
131-oxo-magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine
3,8-divinyl protochlorophyllide a + 5'-deoxyadenosine + L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
overall reaction
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-methionine + H2O
131-hydroxy-magnesium-protoporphyrin IX 13-monomethyl ester + 5'-deoxyadenosine + L-methionine
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-
?
additional information
?
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establishment of in vitro biosynthesis of the isocyclic ring moiety of bacteriochlorophyll using purified recombinant BchE, method development, overview
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additional information
?
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establishment of in vitro biosynthesis of the isocyclic ring moiety of bacteriochlorophyll using purified recombinant BchE, method development, overview
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additional information
?
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establishment of in vitro biosynthesis of the isocyclic ring moiety of bacteriochlorophyll using purified recombinant BchE, method development, overview
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additional information
?
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establishment of in vitro biosynthesis of the isocyclic ring moiety of bacteriochlorophyll using purified recombinant BchE, method development, overview
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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
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
-
-
-
?
magnesium-protoporphyrin IX 13-monomethyl ester + 3 S-adenosyl-L-methionine + H2O
3,8-divinyl protochlorophyllide a + 3 5'-deoxyadenosine + 3 L-methionine
overall reaction
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[4Fe-4S]-center
BchE sequence displays the conserved CXXXCXXC sequence essential for 4Fe-4S cluster formation and an active 4Fe-4S cluster is present in the protein. Isolated protein is yellow-brown in colour with an absorption peak around 410 nm
additional information
membrane-localized BchE requires an additional, heat-sensitive cytosolic cobalamin component for activity, BchE catalysis is not sustained in chimeric experiments when a cytosolic extract from Escherichia coli is used as a substitute
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Cobalamin
vitamin B12-requiring mutants of the bluE and bluB genes of Rhodobacter capsulatus, grown without B12, accumulate Mg-protoporphyrin monomethyl ester and its 3-vinyl-8-ethyl derivative. Cyclase activity in the B12-dependent mutants requires vitamin B12 but not protein synthesis
Cobalamin
dependent on, ligated via Asp248, Glu249, Leu29, Thr71, Val97
S-adenosyl-L-methionine
dependent on, ligated via Phe210, Glu308 and Lys320
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
BchE activity is stimulated by increasing concentrations of NADPH or SAM
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
evolution
BchE and ChlA/AcsF are mainly identified in anoxygenic photosynthetic bacteria and plants, respectively. Some photosynthetic bacteria have either both or one of the two enzymes. The phylogenetic relationships imply that both chlE/bchE and chlA/acsF genes had been the MPE cyclase genes inherited by a cyanobacterial common ancestor, and chlE has been later lost in several lineages. The chlA gene has persisted in all cyanobacterial lineages. A gene duplication of chlA to form chlAI and chlAII appears to have occurred in an early phase of evolution of cyanobacteria. Phylogenetic trees of ChlE/BchE and ChlA/AcsF, cyanobacteria and photosynthetic bacteria
evolution
BchE and ChlA/AcsF are mainly identified in anoxygenic photosynthetic bacteria and plants, respectively. Some photosynthetic bacteria have either both or one of the two enzymes. The phylogenetic relationships imply that both chlE/bchE and chlA/acsF genes had been the MPE cyclase genes inherited by a cyanobacterial common ancestor, and chlE has been later lost in several lineages. The chlA gene has persisted in all cyanobacterial lineages. A gene duplication of chlA to form chlAI and chlAII appears to have occurred in an early phase of evolution of cyanobacteria. Phylogenetic trees of ChlE/BchE and ChlA/AcsF, cyanobacteria and photosynthetic bacteria
evolution
BchE and ChlA/AcsF are mainly identified in anoxygenic photosynthetic bacteria and plants, respectively. Some photosynthetic bacteria have either both or one of the two enzymes. The phylogenetic relationships imply that both chlE/bchE and chlA/acsF genes had been the MPE cyclase genes inherited by a cyanobacterial common ancestor, and chlE has been later lost in several lineages. The chlA gene has persisted in all cyanobacterial lineages. A gene duplication of chlA to form chlAI and chlAII appears to have occurred in an early phase of evolution of cyanobacteria. Phylogenetic trees of ChlE/BchE and ChlA/AcsF, cyanobacteria and photosynthetic bacteria
evolution
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BchE and ChlA/AcsF are mainly identified in anoxygenic photosynthetic bacteria and plants, respectively. Some photosynthetic bacteria have either both or one of the two enzymes. The phylogenetic relationships imply that both chlE/bchE and chlA/acsF genes had been the MPE cyclase genes inherited by a cyanobacterial common ancestor, and chlE has been later lost in several lineages. The chlA gene has persisted in all cyanobacterial lineages. A gene duplication of chlA to form chlAI and chlAII appears to have occurred in an early phase of evolution of cyanobacteria. Phylogenetic trees of ChlE/BchE and ChlA/AcsF, cyanobacteria and photosynthetic bacteria
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malfunction
bchE genes from Cyanothece strains PCC 7425 and PCC 7822 restore the photosynthetic growth and bacteriochlorophyll production in the bchE-lacking mutant of Rhodobacter capsulatus
malfunction
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bchE genes from Cyanothece strains PCC 7425 and PCC 7822 restore the photosynthetic growth and bacteriochlorophyll production in the bchE-lacking mutant of Rhodobacter capsulatus
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metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
metabolism
proposed reaction mechanism for the Mg-protoporphyrin monomethyl ester-cyclase reaction starts with adenosylcobalamin forming the adenosyl radical, which leads to withdrawal of a hydrogen atom and formation of the benzylic-type 131-radical of Mg-protoporphyrin monomethyl ester. Withdrawal of an electron gives the 131-cation of Mg-protoporphyrin monomethyl ester. Hydroxyl ion attack on the cation gives 131-hydroxy-Mg-protoporphyrin monomethyl ester. Withdrawal of three hydrogen atoms leads successively to 131-keto-Mg-protoporphyrin monomethyl ester, its 132-Mg-protoporphyrin monomethyl ester, and cyclization to protochlorophyllide
metabolism
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comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
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metabolism
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proposed reaction mechanism for the Mg-protoporphyrin monomethyl ester-cyclase reaction starts with adenosylcobalamin forming the adenosyl radical, which leads to withdrawal of a hydrogen atom and formation of the benzylic-type 131-radical of Mg-protoporphyrin monomethyl ester. Withdrawal of an electron gives the 131-cation of Mg-protoporphyrin monomethyl ester. Hydroxyl ion attack on the cation gives 131-hydroxy-Mg-protoporphyrin monomethyl ester. Withdrawal of three hydrogen atoms leads successively to 131-keto-Mg-protoporphyrin monomethyl ester, its 132-Mg-protoporphyrin monomethyl ester, and cyclization to protochlorophyllide
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metabolism
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comparison of the presence of BchE and AcsF genes encoding oxygen-independent and oxygen-dependent magnesium-protoporphyrin IX monomethylester cyclase, EC 1.21.98.3 and EC 1.14.13.81, respectively, in Proteobacteria. All tested species of aerobic anoxygenic phototrophs contain acsF genes, but some of them also retain the bchE gene. In contrast to bchE phylogeny, the AcsF phylogeny is in good agreement with 16S inferred phylogeny. The AcsF gene occupies a conserved position inside the photosynthesis gene cluster, whereas the BchE location in the genome varies largely between the species
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physiological function
a BchE mutant is photosynthesis-deficient, produces bacteriochlorophyll only under high oxygenation and accumulates Mg-protoporphyrin monomethyl ester under low oxygenation and anaerobiosis. A double knockout mutant lacking both Bche and aerobic magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase AcsF is devoid of photosystem and accumulates Mg-protoporphyrin monomethyl ester under both conditions indicating the involvement of the two enzymes at the same step of the biosynthesis pathway. AcsF acts strictly under high oxygenation conditions, whereas BchE is involved when the oxygen tension drops
physiological function
expression of the gene restores the photosynthetic growth and bacteriochlorophyll production in a bchE lacking mutant of Rhodobacter capsulatus. Significant amounts of Mg-protoporphyrin IX monomethyl ester and 3,8-divinyl protochlorophyllide and monovinyl protochlorophyllide are identified in the transconjugant
physiological function
expression of the gene restores the photosynthetic growth and bacteriochlorophyll production in a bchE lacking mutant of Rhodobacter capsulatus. Significant amounts of Mg-protoporphyrin IX monomethyl ester and 3,8-divinyl protochlorophyllide and monovinyl protochlorophyllide are identified in the transconjugant
physiological function
insertion mutant are defective in converting magnesium-protoporphyrin monomethyl ester to protochlorophyllide
physiological function
expression of the bchE genes from Cyanothece strain PCC 7425 restores the photosynthetic growth and bacteriochlorophyll production in a bchE-lacking mutant of Rhodobacter capsulatus
physiological function
expression of the bchE genes from Cyanothece strain PCC 7822 restores the photosynthetic growth and bacteriochlorophyll production in a bchE-lacking mutant of Rhodobacter capsulatus
physiological function
during bacteriochlorophyll a biosynthesis, the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis. Membrane-localized BchE requires an additional, heat-sensitive cytosolic component for activity
physiological function
-
during bacteriochlorophyll a biosynthesis, the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis. Membrane-localized BchE requires an additional, heat-sensitive cytosolic component for activity
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physiological function
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insertion mutant are defective in converting magnesium-protoporphyrin monomethyl ester to protochlorophyllide
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physiological function
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during bacteriochlorophyll a biosynthesis, the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis. Membrane-localized BchE requires an additional, heat-sensitive cytosolic component for activity
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physiological function
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during bacteriochlorophyll a biosynthesis, the oxygen-independent conversion of Mg-protoporphyrin IX monomethyl ester (Mg-PME) to protochlorophyllide (Pchlide) is catalyzed by the anaerobic Mg-PME cyclase termed BchE, via an unusual radical S-adenosylmethionine (SAM) and cobalamin-dependent BchE catalysis. Membrane-localized BchE requires an additional, heat-sensitive cytosolic component for activity
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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). BCHE_CERS4
Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)
612
0
69219
Swiss-Prot
-
BCHE_RHOCB
Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
575
0
65866
Swiss-Prot
-
BCHE_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
499
0
57793
Swiss-Prot
-
A0A644W8U6_9ZZZZ
449
0
50717
TrEMBL
other Location (Reliability: 4)
A0A7R9R9H3_9EURY
426
0
48830
TrEMBL
-
A0A7R9N960_9EURY
256
0
29829
TrEMBL
-
A0A644T532_9ZZZZ
452
0
51528
TrEMBL
other Location (Reliability: 5)
A0A812A957_9EURY
88
0
10708
TrEMBL
-
A0A7R9RAK9_9EURY
486
0
56775
TrEMBL
-
A0A7R9NAV8_9EURY
488
0
56177
TrEMBL
-
A0A644UGX0_9ZZZZ
445
0
51110
TrEMBL
other Location (Reliability: 3)
A0A8A0RMX4_9FIRM
584
0
67042
TrEMBL
-
A0A644UGM1_9ZZZZ
532
0
61597
TrEMBL
Mitochondrion (Reliability: 5)
A0A7R9RCK4_9EURY
323
0
37600
TrEMBL
-
A0A644V0H3_9ZZZZ
512
0
58463
TrEMBL
other Location (Reliability: 2)
A0A644TRK9_9ZZZZ
466
0
53592
TrEMBL
other Location (Reliability: 4)
A0A7R9RAH9_9EURY
488
0
56175
TrEMBL
-
B8HM76_CYAP4
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
675
0
77119
TrEMBL
-
E0U5T3_GLOV7
Gloeothece verrucosa (strain PCC 7822)
744
0
84735
TrEMBL
-
J9JE44_9HYPH
203
0
23873
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
2 * 63000, calculated, 2 * 43000, SDS-PAGE of truncated protein of 384 residues
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
bchE genes from Cyanothece strains PCC 7425 and PCC 7822 restore the photosynthetic growth and bacteriochlorophyll production in the bchE-lacking mutant of Rhodobacter capsulatus
additional information
-
bchE genes from Cyanothece strains PCC 7425 and PCC 7822 restore the photosynthetic growth and bacteriochlorophyll production in the bchE-lacking mutant of Rhodobacter capsulatus
additional information
-
bchE genes from Cyanothece strains PCC 7425 and PCC 7822 restore the photosynthetic growth and bacteriochlorophyll production in the bchE-lacking mutant of Rhodobacter capsulatus
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein, preparation is yellow-brown in color. Only a small fraction can be solubilized with urea (6 M), and most of the iron-sulfur cluster is degraded upon solubilization of inclusion bodies
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Cyan7425_4778 or chlE, DNA and amino acid sequence determination and analysis, the chlE gene is located in a gene cluster, chlAII-ho2-hemN-chlE-desF, sequence comparisons and phylogenetic analysis, functional complementation of a bchE-lacking mutant of Rhodobacter capsulatus
gene Cyan7822_3999 or chlE, DNA and amino acid sequence determination and analysis, the chlE gene is located at some distance from the chlAII-ho2-hemN gene cluster, sequence comparisons and phylogenetic analysis, functional complementation of a bchE-lacking mutant of Rhodobacter capsulatus
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
simplified method to prepare Mg-protoporphyrin monomethyl ester from freeze dried BchE mutant Rhodobacter capsulatus DB575 cells by extraction with acetone/H2O/25% NH3. Isolated Mg-protoporphyrin monomethyl ester can be identified by absorption and fluorescence spectroscopy, and its purity analyzed by HPLC. The extracted Mg-protoporphyrin monomethyl ester can be dried and redissolved in buffered DMSO to be used as substrate. Mg-protoporphyrin monomethyl ester is in addition a substrate to magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase, EC 1.13.14.81
synthesis
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simplified method to prepare Mg-protoporphyrin monomethyl ester from freeze dried BchE mutant Rhodobacter capsulatus DB575 cells by extraction with acetone/H2O/25% NH3. Isolated Mg-protoporphyrin monomethyl ester can be identified by absorption and fluorescence spectroscopy, and its purity analyzed by HPLC. The extracted Mg-protoporphyrin monomethyl ester can be dried and redissolved in buffered DMSO to be used as substrate. Mg-protoporphyrin monomethyl ester is in addition a substrate to magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase, EC 1.13.14.81
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gough, S.P.; Rzeznicka, K.; Peterson Wulff, R.; Francisco, J.d.; Hansson, A.; Jensen, P.E.; Hansson, M.
A new method for isolating physiologically active Mg-protoporphyrin monomethyl ester, the substrate of the cyclase enzyme of the chlorophyll biosynthetic pathway
Plant Physiol. Biochem.
45
932-936
2007
Rhodobacter capsulatus (P26168), Rhodobacter capsulatus ATCC BAA-309 (P26168)
brenda
Boldareva-Nuianzina, E.N.; Blahova, Z.; Sobotka, R.; Koblizek, M.
Distribution and origin of oxygen-dependent and oxygen-independent forms of Mg-protoporphyrin monomethylester cyclase among phototrophic proteobacteria
Appl. Environ. Microbiol.
79
2596-2604
2013
Roseobacter sp. (G3GIW8), Citromicrobium sp. CV44 (G3GIX0), Rhodobacterales bacterium chep-kr (G3GIX2), Roseinatronobacter monicus (J7FAN3), Roseobacter sp. Zun_kholvo (J7FBD4), Roseinatronobacter sp. khil (J7FBP5), Methylobacteriaceae bacterium RM11-8-1 (J9JE44), Rhodobaca bogoriensis (J9JE46), Rhodobaca bogoriensis DSM 18756 (J9JE46), Roseobacter sp. B09 (G3GIW8)
brenda
Yamanashi, K.; Minamizaki, K.; Fujita, Y.
Identification of the chlE gene encoding oxygen-independent Mg-protoporphyrin IX monomethyl ester cyclase in cyanobacteria
Biochem. Biophys. Res. Commun.
463
1328-1333
2015
Cyanothece sp. PCC 7425 (B8HM76), Gloeothece verrucosa PCC 7822 (E0U5T3)
brenda