BRENDA - Enzyme Database show
show all sequences of 1.3.98.3

Coproporphyrin III excretion identifies the anaerobic coproporphyrinogen III oxidase HemN as a copper target in the Cu+-ATPase mutant copA- of Rubrivivax gelatinosus

Azzouzi, A.; Steunou, A.S.; Durand, A.; Khalfaoui-Hassani, B.; Bourbon, M.L.; Astier, C.; Bollivar, D.W.; Ouchane, S.; Mol. Microbiol. 88, 339-351 (2013)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
Cu2+
copper affects tetrapyrrole biosynthesis presumably at the level of the SAM and [4Fe-4S] containing HemN enzyme. Members of the radical SAM enzyme family are copper sensitive. The excess copper target in the tetrapyrrole pathway is the anaerobic coproporphyrinogen III oxidase [4Fe-4S] containing HemN
Rubrivivax gelatinosus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
Rubrivivax gelatinosus
-
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rubrivivax gelatinosus
I0HU37
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
-
745799
Rubrivivax gelatinosus
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
[4Fe-4S] cluster
-
Rubrivivax gelatinosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
[4Fe-4S] cluster
-
Rubrivivax gelatinosus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cu2+
copper affects tetrapyrrole biosynthesis presumably at the level of the SAM and [4Fe-4S] containing HemN enzyme. Members of the radical SAM enzyme family are copper sensitive. The excess copper target in the tetrapyrrole pathway is the anaerobic coproporphyrinogen III oxidase [4Fe-4S] containing HemN
Rubrivivax gelatinosus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
Rubrivivax gelatinosus
-
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
coproporphyrinogen III + 2 S-adenosyl-L-methionine
-
745799
Rubrivivax gelatinosus
protoporphyrinogen IX + 2 CO2 + 2 L-methionine + 2 5'-deoxyadenosine
-
-
-
?
Expression
Organism
Commentary
Expression
Rubrivivax gelatinosus
HemN expression or activity is affected in the copA- mutant under excess copper
down
General Information
General Information
Commentary
Organism
malfunction
excess copper in the copA- mutant, deficient for Cu+-ATPase CopA via transposon mutagenesis, results in a substantial decrease of the cytochrome c oxidase and the photosystem under microaerobic and anaerobic conditions together with the extrusion of coproporphyrin III. Enzyme CopA is required for the activity of cuproproteins in the purple bacterium Rubrivivax gelatinosus. CopA is not directly required for cytochrome c oxidase activity but is vital for copper tolerance. The Cu+-ATPase CtpA is required only for the activity of cuproproteins in the purple bacterium Rubrivivax gelatinosus
Rubrivivax gelatinosus
physiological function
coproporphyrinogen III is converted to protoporphyrinogen IX under anaerobiosis and low oxygen tension by the anaerobic coproporphyrinogen III oxidase HemN. The Cu+-ATPase CopA is not directly required for cytochrome c oxidase but is vital for copper tolerance. The physiological role of the copper P1B-type transporter CtpA, though homologous to CopA, differs from that of the effluxATPase CopA, because CtpA is dispensable for copper tolerance in contrast to CopA. HemN, a radical SAM and iron-sulfur containing protein, is a target enzyme in the tetrapyrrole biosynthesis pathway
Rubrivivax gelatinosus
General Information (protein specific)
General Information
Commentary
Organism
malfunction
excess copper in the copA- mutant, deficient for Cu+-ATPase CopA via transposon mutagenesis, results in a substantial decrease of the cytochrome c oxidase and the photosystem under microaerobic and anaerobic conditions together with the extrusion of coproporphyrin III. Enzyme CopA is required for the activity of cuproproteins in the purple bacterium Rubrivivax gelatinosus. CopA is not directly required for cytochrome c oxidase activity but is vital for copper tolerance. The Cu+-ATPase CtpA is required only for the activity of cuproproteins in the purple bacterium Rubrivivax gelatinosus
Rubrivivax gelatinosus
physiological function
coproporphyrinogen III is converted to protoporphyrinogen IX under anaerobiosis and low oxygen tension by the anaerobic coproporphyrinogen III oxidase HemN. The Cu+-ATPase CopA is not directly required for cytochrome c oxidase but is vital for copper tolerance. The physiological role of the copper P1B-type transporter CtpA, though homologous to CopA, differs from that of the effluxATPase CopA, because CtpA is dispensable for copper tolerance in contrast to CopA. HemN, a radical SAM and iron-sulfur containing protein, is a target enzyme in the tetrapyrrole biosynthesis pathway
Rubrivivax gelatinosus
Expression (protein specific)
Organism
Commentary
Expression
Rubrivivax gelatinosus
HemN expression or activity is affected in the copA- mutant under excess copper
down
Other publictions for EC 1.3.98.3
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)
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726009
Azzouzi
Coproporphyrin III excretion i ...
Rubrivivax gelatinosus
Mol. Microbiol.
88
339-351
2013
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745799
Azzouzi
Coproporphyrin III excretion ...
Rubrivivax gelatinosus
Mol. Microbiol.
88
339-351
2013
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724235
Abicht
Lactococcus lactis HemW (HemN) ...
Lactococcus lactis
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674567
Layer
The substrate radical of Esche ...
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672473
Layer
Structural and functional comp ...
Bacillus subtilis, Cupriavidus necator, Escherichia coli, Rhodobacter sphaeroides, Salmonella enterica subsp. enterica serovar Typhimurium
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386
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674462
Layer
Radical S-adenosylmethionine e ...
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658501
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Structure and function of radi ...
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655340
Layer
Crystal structure of coproporp ...
Escherichia coli
EMBO J.
22
6214-6224
2003
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656073
Layer
Oxygen-independent coproporphy ...
Escherichia coli
J. Biol. Chem.
277
34136-34142
2002
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