BRENDA - Enzyme Database
show all sequences of 1.3.1.111

Cloning, sequencing and functional assignment of the chlorophyll biosynthesis gene, chlP, of Synechocystis sp. PCC 6803

Addlesee, H.A.; Gibson, L.C.; Jensen, P.E.; Hunter, C.N.; FEBS Lett. 389, 126-130 (1996)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene bchP, sequence comparison with gene chlP from Synechocystis sp. strain PCC 6803
Rhodobacter sphaeroides
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
Synechocystis sp.
Engineering
Amino acid exchange
Commentary
Organism
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
Rhodobacter sphaeroides
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44869
-
x * 44869, sequence calculation
Synechocystis sp.
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
bacteriochlorophyll a + 3 NADP+
Rhodobacter sphaeroides
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
bacteriochlorophyll a + 3 NADP+
Synechocystis sp.
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
bacteriochlorophyll a + 3 NADP+
Rhodobacter sphaeroides NCIB 8253
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rhodobacter sphaeroides
Q9Z5D4
gene bchP
-
Rhodobacter sphaeroides NCIB 8253
Q9Z5D4
gene bchP
-
Synechocystis sp.
Q55087
gene chlP; gene chlP
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
bacteriochlorophyll a + 3 NADP+
-
736098
Rhodobacter sphaeroides
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
bacteriochlorophyll a + 3 NADP+
-
736098
Synechocystis sp.
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
bacteriochlorophyll a + 3 NADP+
-
736098
Rhodobacter sphaeroides NCIB 8253
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 44869, sequence calculation
Synechocystis sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
-
Rhodobacter sphaeroides
NADP+
-
Synechocystis sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
gene bchP, sequence comparison with gene chlP from Synechocystis sp. strain PCC 6803
Rhodobacter sphaeroides
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
Synechocystis sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
-
Rhodobacter sphaeroides
NADP+
-
Synechocystis sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
Rhodobacter sphaeroides
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
44869
-
x * 44869, sequence calculation
Synechocystis sp.
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
bacteriochlorophyll a + 3 NADP+
Rhodobacter sphaeroides
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
bacteriochlorophyll a + 3 NADP+
Synechocystis sp.
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
bacteriochlorophyll a + 3 NADP+
Rhodobacter sphaeroides NCIB 8253
-
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
bacteriochlorophyll a + 3 NADP+
-
736098
Rhodobacter sphaeroides
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
bacteriochlorophyll a + 3 NADP+
-
736098
Synechocystis sp.
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
bacteriochlorophyll a + 3 NADP+
-
736098
Rhodobacter sphaeroides NCIB 8253
geranylgeranyl bacteriochlorophyllide a + 3 NADPH + 3 H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 44869, sequence calculation
Synechocystis sp.
General Information
General Information
Commentary
Organism
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
Rhodobacter sphaeroides
metabolism
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
Synechocystis sp.
physiological function
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
Synechocystis sp.
General Information (protein specific)
General Information
Commentary
Organism
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
Rhodobacter sphaeroides
metabolism
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
Synechocystis sp.
physiological function
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis
Synechocystis sp.
Other publictions for EC 1.3.1.111
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
736948
Harada
Accumulation of chlorophyllous ...
Chlorobaculum tepidum, Chlorobaculum tepidum WT2321
Photochem. Photobiol. Sci.
7
1179-1187
2008
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1
-
1
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1
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-
2
-
2
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-
-
-
-
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2
-
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-
1
-
-
1
-
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-
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-
1
1
-
1
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1
-
-
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2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
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-
2
2
-
-
-
692822
Addlesee
Rhodospirillum rubrum possesse ...
Rhodobacter sphaeroides, Rhodospirillum rubrum
J. Bacteriol.
184
1578-1586
2002
-
-
1
-
2
-
-
-
-
-
-
3
-
6
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
4
-
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-
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-
1
4
-
2
-
-
-
-
-
-
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3
-
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-
-
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-
-
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8
-
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-
-
-
-
-
-
-
-
3
3
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-
692821
Addlesee
Physical mapping and functiona ...
Rhodobacter sphaeroides
J. Bacteriol.
181
7248-7255
1999
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-
1
-
1
-
-
-
-
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2
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4
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-
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-
-
-
-
-
4
-
1
-
-
-
1
-
-
2
-
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-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
736098
Addlesee
Cloning, sequencing and functi ...
Rhodobacter sphaeroides, Rhodobacter sphaeroides NCIB 8253, Synechocystis sp.
FEBS Lett.
389
126-130
1996
-
-
2
-
1
-
-
-
-
-
1
3
-
3
-
-
-
-
-
-
-
-
3
1
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-
-
-
-
-
-
2
-
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2
2
-
1
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1
3
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3
1
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-
-
-
-
-
-
-
-
3
3
-
-
-
735661
Bollivar
Molecular genetic analysis of ...
Rhodobacter capsulatus, Rhodobacter capsulatus SB1003
Biochemistry
33
12763-12768
1994
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1
-
1
-
-
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-
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2
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2
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-
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-
-
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4
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1
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1
1
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1
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2
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4
-
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-
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2
2
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