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Information on EC 1.3.1.111 - geranylgeranyl-bacteriochlorophyllide a reductase
for references in articles please use BRENDA:EC1.3.1.111
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.111 geranylgeranyl-bacteriochlorophyllide a reductase
IUBMB Comments
The enzyme catalyses the successive reduction of the geranylgeraniol esterifying group to phytol, reducing three out of four double bonds, and transforming geranylgeranyl bacteriochlorophyllide a via dihydrogeranylgeranyl bacteriochlorophyllide a and tetrahydrogeranylgeranyl bacteriochlorophyllide a to bacteriochlorophyll a. The enzyme can also accept the pheophytin derivative geranylgeranyl bacteriopheophytin, converting it to bacteriopheophytin a.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
showSynonyms
gg-bphe reductase, geranylgeranyl-bacteriochlorophyll reductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BchP
geranylgeranyl-bacteriopheophytin reductase
GG-Bphe reductase
BchP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
bacteriochlorophyll a + 3 NADP+ = geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
bacteriochlorophyll a:NADP+ oxidoreductase (geranylgeranyl-reducing)
The enzyme catalyses the successive reduction of the geranylgeraniol esterifying group to phytol, reducing three out of four double bonds, and transforming geranylgeranyl bacteriochlorophyllide a via dihydrogeranylgeranyl bacteriochlorophyllide a and tetrahydrogeranylgeranyl bacteriochlorophyllide a to bacteriochlorophyll a. The enzyme can also accept the pheophytin derivative geranylgeranyl bacteriopheophytin, converting it to bacteriopheophytin a.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
phytyl-bacteriochlorophyll a + 3 NADP+
geranylgeranyl-bacteriopheophytin a + NADPH + H+
phytyl-bacteriopheophytin a + NADP+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: activity assay is performed in the dark
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Cereibacter sphaeroides NCIB 8253
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: three reductive steps, overview
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: three reductive steps, overview
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriopheophytin a + 3 NADP+
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriopheophytin a + 3 NADP+
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
phytyl-bacteriochlorophyll a + 3 NADP+
Substrates: -
Products: -
Products: -
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
phytyl-bacteriochlorophyll a + 3 NADP+
-
Substrates: -
Products: -
Products: -
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
phytyl-bacteriochlorophyll a + 3 NADP+
Substrates: the enzyme is involved in phythylation of bacteriochlorophyll a
Products: -
Products: -
?
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
phytyl-bacteriochlorophyll a + 3 NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with geranylgeranyl-bacteriopheophytin a
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with geranylgeranyl-bacteriopheophytin a
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with bacteriochlorophyll a
Products: -
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?
additional information
?
-
-
Substrates: no activity with bacteriochlorophyll a
Products: -
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
geranylgeranyl-bacteriochlorophyll a + 3 NADPH + 3 H+
phytyl-bacteriochlorophyll a + 3 NADP+
Substrates: the enzyme is involved in phythylation of bacteriochlorophyll a
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Cereibacter sphaeroides NCIB 8253
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriochlorophyll a + 3 NADP+
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriopheophytin a + 3 NADP+
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
bacteriopheophytin a + 3 NADP+
geranylgeranyl bacteriopheophytin a + 3 NADPH + 3 H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
a mutant in orf391 synthesizes bacteriochlorophyll a that is esterified with geranylgeraniol rather than the normal phytol. Strains that accumulate geranylgeraniol-esterified bacteriochlorophyll a exhibit reduced photosynthetic growth capability compared to that observed with the parent strain which synthesizes bacteriochlorophyll a that is esterified with phytol. But synthesis of geranylgeranyl bacteriochlorophyllide a does not per se impair function of the reaction center complex nor energy transfer from the light harvesting complex
malfunction
a transposon mutant of gene bchP encoding geranylgeranyl-bacteriochlorophyll reductase possesses a structurally modified photosystem assembled with bacteriochlorophyll esterified with geranylgeraniol, rather than with phytol
malfunction
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex
malfunction
the CT2256-deleted mutant shows accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence, phenotype, overview
malfunction
the enzyme only catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin. It might be a naturally occurring bchP mutant with an insertion mutation that may have been the initial cause of a partial loss of function
malfunction
-
the CT2256-deleted mutant shows accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence, phenotype, overview
-
malfunction
Cereibacter sphaeroides NCIB 8253
-
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex
-
malfunction
-
a mutant in orf391 synthesizes bacteriochlorophyll a that is esterified with geranylgeraniol rather than the normal phytol. Strains that accumulate geranylgeraniol-esterified bacteriochlorophyll a exhibit reduced photosynthetic growth capability compared to that observed with the parent strain which synthesizes bacteriochlorophyll a that is esterified with phytol. But synthesis of geranylgeranyl bacteriochlorophyllide a does not per se impair function of the reaction center complex nor energy transfer from the light harvesting complex
-
metabolism
esterification of bacteriochlorophyllide a initially involves the addition of a geranylgeraniol group followed by sequential reduction of the geranylgeraniol moiety tophytol which is the end product of the pathway. Synthesis of geranylgeraniol-esterified bacteriochlorophyll does not affect the energy transfer rate from light harvesting to reaction center complexes nor the electron transfer function as measured by the yield of electron transfer to the primary and secondary quinones, the charge recombination rate from the quinones, and the rate of cytochrome c2 oxidation. Pathway for synthesis of bacteriochlorophyll from bacteriochlorophyllide, overview
metabolism
requirement of Rhodospirillum rubrum for phytylated bacteriopheophytin, a potential link between the absence of light-harvesting complex 2 and of phytylated bacteriochlorophyll from the wild-type bacterium. In addition to bacteriochlorophyll, the reaction center of purple bacteria contains two bacteriopheophytin molecules, one of which is the first clearly resolved acceptor of electrons, following electron transfer from the bacteriochlorophyll dimer. Proposed pathway for reduction of geranylgeranyl bacteriopheophytin a in Rhodospirillum rubrum, reduction proceeds via dihydro-GG-esterified and tetrahydro-GG-esterified intermediates to the final product, phytylated bacteriopheophytin
metabolism
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
metabolism
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis, pathway for the phytylation of bacteriochlorophyll a, overview
metabolism
-
esterification of bacteriochlorophyllide a initially involves the addition of a geranylgeraniol group followed by sequential reduction of the geranylgeraniol moiety tophytol which is the end product of the pathway. Synthesis of geranylgeraniol-esterified bacteriochlorophyll does not affect the energy transfer rate from light harvesting to reaction center complexes nor the electron transfer function as measured by the yield of electron transfer to the primary and secondary quinones, the charge recombination rate from the quinones, and the rate of cytochrome c2 oxidation. Pathway for synthesis of bacteriochlorophyll from bacteriochlorophyllide, overview
-
physiological function
the bacteriochlorophyll of the purple photosynthetic bacterium Rhodobacter sphaeroides is esterified with phytol. The presence of this alcohol moiety is essential for the correct assembly of the photosynthetic apparatus. The enzyme is essential and responsible for the reduction of the alcohol moiety of (bacterio)chlorophyll to phytol
physiological function
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
physiological function
the enzyme is involved esterification of bacteriochlorophyll a with DELTA2,6-phytadienol and phytol, respectively, which is produced by reduction of the geranylgeranyl group at the C-17 propionate residue
physiological function
the enzyme is responsible for the reduction of the isoprenoid moiety of bacteriochlorophyll (Bchl) from geranylgeraniol (GG) to phytol, it also catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin
physiological function
-
the enzyme is involved esterification of bacteriochlorophyll a with DELTA2,6-phytadienol and phytol, respectively, which is produced by reduction of the geranylgeranyl group at the C-17 propionate residue
-
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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). A0A5B7BD70_DAVIN
395
0
43541
TrEMBL
other Location (Reliability: 3)
A0A5B7BNL5_DAVIN
110
0
12335
TrEMBL
other Location (Reliability: 2)
A0A5B7A3T1_DAVIN
370
1
40474
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B6ZLH6_DAVIN
293
0
32024
TrEMBL
Secretory Pathway (Reliability: 5)
A0A5B6YP77_DAVIN
378
1
41403
TrEMBL
other Location (Reliability: 4)
A0A5B7A1M8_DAVIN
368
1
40166
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5B7A8K1_DAVIN
312
0
33965
TrEMBL
Mitochondrion (Reliability: 1)
CHLP_SYNY3
Synechocystis sp. (strain PCC 6803 / Kazusa)
407
0
44883
Swiss-Prot
-
Q8KAB0_CHLTE
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
383
0
43090
TrEMBL
-
Q9Z5D4_CERSP
394
0
43445
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a transposon mutant of gene bchP encoding geranylgeranyl-bacteriochlorophyll reductase possesses a structurally modified photosystem assembled with bacteriochlorophyll esterified with geranylgeraniol, rather than with phytol
additional information
-
a transposon mutant of gene bchP encoding geranylgeranyl-bacteriochlorophyll reductase possesses a structurally modified photosystem assembled with bacteriochlorophyll esterified with geranylgeraniol, rather than with phytol
additional information
construction of a a hybrid gene consisting of the 5'half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
additional information
-
construction of a a hybrid gene consisting of the 5'half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
additional information
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex. Upon heterologous expression of the Synechocystis bchP homologue encoded by gene chlP, not only are hydrogenated forms of geranylgeranyl bacteriochlorophyllide a (bchlaGG) detectable, but the level of LH2 is increased, phenotype, overview
additional information
Cereibacter sphaeroides NCIB 8253
-
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex. Upon heterologous expression of the Synechocystis bchP homologue encoded by gene chlP, not only are hydrogenated forms of geranylgeranyl bacteriochlorophyllide a (bchlaGG) detectable, but the level of LH2 is increased, phenotype, overview
-
additional information
generation of a gene CT2256 deletion mutant, which almost shows no apparent phenotype compared to the wild-type. The purple bacterium Rhodobacter capsulatus mutant strain DB391 defective in the bchP gene is partially complemented with the CT2256 gene, bacteriochlorophyllide a is synthesized in the mutant in addition to accumulating other intermediates, phenotype, overview
additional information
-
generation of a gene CT2256 deletion mutant, which almost shows no apparent phenotype compared to the wild-type. The purple bacterium Rhodobacter capsulatus mutant strain DB391 defective in the bchP gene is partially complemented with the CT2256 gene, bacteriochlorophyllide a is synthesized in the mutant in addition to accumulating other intermediates, phenotype, overview
-
additional information
construction of a chromosomal KmR insertion mutation of gene bchP performed by GTA-mediated homologous recombination
additional information
-
construction of a chromosomal KmR insertion mutation of gene bchP performed by GTA-mediated homologous recombination
-
additional information
construction of a hybrid gene consisting of the 5' half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
additional information
-
construction of a hybrid gene consisting of the 5' half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bchP, DNA and amino acid sequence determination and analysis, sequence comparison
gene bchP, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS. The recombinant enzyme complements the bchP insertion mutant T6G5
gene bchP, recombinant expression in Escherichia coli and in the plasmid-mobilizing Rhodobacter capsulatus strain TecS
gene bchP, sequence comparison with gene chlP from Synechocystis sp. strain PCC 6803
gene chfP, DNA and amino acid sequence determination and analysis, the enzyme partially complements a bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides, which is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex. Upon heterologous expression of the Synechocystis bchP homologue, not only are hydrogenated forms of geranylgeranyl bacteriochlorophyllide a (bchlaGG) detectable, but the level of LH2 is increased, sequence comparison with gene chP from Rhodobacter sphaeroides strain NCIB 8253
gene CT2256, recombinant expression in Rhodobacter capsulatus mutant strain DB391 defective in the bchP gene and partial complementation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Addlesee, H.A.; Hunter, C.N.
Physical mapping and functional assignment of the geranylgeranyl-bacteriochlorophyll reductase gene, bchP, of Rhodobacter sphaeroides
J. Bacteriol.
181
7248-7255
1999
Cereibacter sphaeroides (Q9Z5D4), Cereibacter sphaeroides
brenda
Addlesee, H.A.; Hunter, C.N.
Rhodospirillum rubrum possesses a variant of the bchP gene, encoding geranylgeranyl-bacteriopheophytin reductase
J. Bacteriol.
184
1578-1586
2002
Cereibacter sphaeroides (Q9Z5D4), Cereibacter sphaeroides, Rhodospirillum rubrum (Q936J5), Rhodospirillum rubrum
brenda
Bollivar, D.
Molecular genetic analysis of terminal steps in bacteriochlorophyll a biosynthesis: characterization of a Rhodobacter capsulatus strain that synthesizes geranylgeraniol-esterified bacteriochlorophyll a
Biochemistry
33
12763-12768
1994
Rhodobacter capsulatus (Q9Z5D4), Rhodobacter capsulatus SB1003 (Q9Z5D4)
brenda
Addlesee, H.A.; Gibson, L.C.; Jensen, P.E.; Hunter, C.N.
Cloning, sequencing and functional assignment of the chlorophyll biosynthesis gene, chlP, of Synechocystis sp. PCC 6803
FEBS Lett.
389
126-130
1996
Cereibacter sphaeroides (Q9Z5D4), Cereibacter sphaeroides NCIB 8253 (Q9Z5D4), Synechocystis sp. (Q55087)
brenda
Harada, J.; Miyago, S.; Mizoguchi, T.; Azai, C.; Inoue, K.; Tamiaki, H.; Oh-oka, H.
Accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence in the CT2256-deleted mutant of the green sulfur bacterium Chlorobium tepidum
Photochem. Photobiol. Sci.
7
1179-1187
2008
Chlorobaculum tepidum (Q8KAB0), Chlorobaculum tepidum WT2321 (Q8KAB0)
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.1.111)
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