BRENDA - Enzyme Database show
show all sequences of 4.99.1.4

CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis

Stroupe, M.E.; Leech, H.K.; Daniels, D.S.; Warren, M.J.; Getzoff, E.D.; Nat. Struct. Biol. 10, 1064-1073 (2003)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Salmonella enterica
Crystallization (Commentary)
Crystallization
Organism
X-ray crystal structure of CysG
Salmonella enterica
Engineering
Amino acid exchange
Commentary
Organism
S128A
mutant has higher cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
Salmonella enterica
S128D
mutant has lower cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
Salmonella enterica
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sirohydrochlorin + Fe2+
Salmonella enterica
CysG, siroheme biosynthesis
siroheme + 2 H+
sulfur metabolism depends on siroheme
Salmonella enterica
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Salmonella enterica
-
-
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
phosphoprotein
CysG, phosphorylation of Ser-128, plays a regulatory role
Salmonella enterica
Purification (Commentary)
Commentary
Organism
-
Salmonella enterica
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0138
-
S128D mutant CysG, cobalt chelation of sirohydrochlorin
Salmonella enterica
0.0656
-
wild-type CysG, cobalt chelation of sirohydrochlorin
Salmonella enterica
0.243
-
S128A mutant CysG, cobalt chelation of sirohydrochlorin
Salmonella enterica
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sirohydrochlorin + Co2+
-
653297
Salmonella enterica
cobalt-sirohydrochlorin + 2 H+
-
653297
Salmonella enterica
?
sirohydrochlorin + Fe2+
CysG structure, the multifunctional siroheme synthase CysG synthesizes siroheme from uroporphyrinogen III, CysG contains two structurally independent modules: a bismethyltransferase and a dual-function dehydrogenase-chelatase
653297
Salmonella enterica
siroheme + 2 H+
-
653297
Salmonella enterica
?
sirohydrochlorin + Fe2+
CysG, siroheme biosynthesis
653297
Salmonella enterica
siroheme + 2 H+
sulfur metabolism depends on siroheme
653297
Salmonella enterica
?
Subunits
Subunits
Commentary
Organism
homodimer
-
Salmonella enterica
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Salmonella enterica
Crystallization (Commentary) (protein specific)
Crystallization
Organism
X-ray crystal structure of CysG
Salmonella enterica
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
S128A
mutant has higher cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
Salmonella enterica
S128D
mutant has lower cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
Salmonella enterica
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
sirohydrochlorin + Fe2+
Salmonella enterica
CysG, siroheme biosynthesis
siroheme + 2 H+
sulfur metabolism depends on siroheme
Salmonella enterica
?
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
phosphoprotein
CysG, phosphorylation of Ser-128, plays a regulatory role
Salmonella enterica
Purification (Commentary) (protein specific)
Commentary
Organism
-
Salmonella enterica
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.0138
-
S128D mutant CysG, cobalt chelation of sirohydrochlorin
Salmonella enterica
0.0656
-
wild-type CysG, cobalt chelation of sirohydrochlorin
Salmonella enterica
0.243
-
S128A mutant CysG, cobalt chelation of sirohydrochlorin
Salmonella enterica
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
sirohydrochlorin + Co2+
-
653297
Salmonella enterica
cobalt-sirohydrochlorin + 2 H+
-
653297
Salmonella enterica
?
sirohydrochlorin + Fe2+
CysG structure, the multifunctional siroheme synthase CysG synthesizes siroheme from uroporphyrinogen III, CysG contains two structurally independent modules: a bismethyltransferase and a dual-function dehydrogenase-chelatase
653297
Salmonella enterica
siroheme + 2 H+
-
653297
Salmonella enterica
?
sirohydrochlorin + Fe2+
CysG, siroheme biosynthesis
653297
Salmonella enterica
siroheme + 2 H+
sulfur metabolism depends on siroheme
653297
Salmonella enterica
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
-
Salmonella enterica
Other publictions for EC 4.99.1.4
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)
748869
Garai
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2016
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1
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3
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3
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1
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1
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92
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1
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1
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1
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1
1
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1
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1
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1
1
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1
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1
1
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729160
Saha
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Biochem. J.
444
227-237
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6
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1
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1
1
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5
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1
1
2
1
-
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1
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1
6
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1
1
-
-
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-
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-
-
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716791
Romao
Evolution in a family of chela ...
Bacillus megaterium
Proc. Natl. Acad. Sci. USA
108
97-102
2011
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1
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1
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1
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1
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696120
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no activity in Desulfovibrio vulgaris
Biochem. J.
420
317-325
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665692
Raux-Deery
Identification and characteriz ...
Arabidopsis thaliana
J. Biol. Chem.
280
4713-4721
2005
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1
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2
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2
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1
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4
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-
1
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-
-
2
-
3
-
-
-
-
-
-
-
-
-
-
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-
1
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-
-
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2
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1
1
2
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1
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1
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2
-
3
-
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649745
Raux
Identification and functional ...
Bacillus megaterium, Bacillus megaterium DSM 509
Biochem. J.
370
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2003
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1
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-
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-
1
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1
2
-
4
-
-
1
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-
2
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8
1
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1
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1
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1
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1
2
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-
1
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-
2
-
8
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
653297
Stroupe
CysG structure reveals tetrapy ...
Salmonella enterica
Nat. Struct. Biol.
10
1064-1073
2003
-
-
1
1
2
-
-
-
-
-
-
1
-
1
-
1
1
-
-
-
3
-
3
1
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1
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1
2
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1
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1
1
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-
3
-
3
1
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-
644283
Schubert
The structure of Saccharomyces ...
Saccharomyces cerevisiae
EMBO J.
21
2068-2075
2002
-
-
1
1
3
-
-
-
-
-
-
2
-
2
-
-
1
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2
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4
1
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1
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1
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1
3
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2
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1
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2
-
4
1
-
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-
1
-
-
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-
-
-
-
-
649817
Schubert
Structural diversity in metal ...
Saccharomyces cerevisiae
Biochem. Soc. Trans.
30
595-600
2002
-
-
-
1
2
-
-
-
-
-
-
1
-
1
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1
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-
-
2
1
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1
2
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1
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2
1
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