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Information on EC 4.99.1.4 - sirohydrochlorin ferrochelatase
for references in articles please use BRENDA:EC4.99.1.4
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EC Tree 4 Lyases
4.99 Other lyases
4.99.1 Sole sub-subclass for lyases that do not belong in the other subclasses
4.99.1.4 sirohydrochlorin ferrochelatase
IUBMB Comments
This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 4.99.1.4
- uroporphyrinogen
- tetrapyrrole
- methyltransferase
-
sirohaem
-
prosthetic
- epr
-
ferrochelation
- precorrin-2
- reductases
- fe-s
- nitrite
showSynonyms
sirohydrochlorin ferrochelatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CysG
Met8p
SirB
additional information
CysG
-
-
-
-
Met8p
-
-
-
-
SirB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
siroheme + 2 H+ = sirohydrochlorin + Fe2+
-
-
-
-
siroheme + 2 H+ = sirohydrochlorin + Fe2+
the enzyme from Pseudomonas chloroaphis contains Ca2+ and protoheme IX, the iron of which must be in the form Fe2+ for activity, the enzyme exhibits a strong preference for aliphatic aldoximes, such as butyraldoxime and acetaldoxime, over aromatic aldoximes, such as pyridine-2-aldoxime, which is a poor substrate, no activity was found with the aromatic aldoximes benzaldoxime and pyridine-4-aldoxime, mechanism
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
siroheme biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
siroheme ferro-lyase (sirohydrochlorin-forming)
This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction.
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CAS REGISTRY NUMBER
COMMENTARY
9012-93-5
-
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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
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + H+
-
Substrates: pH 8.0
Products: -
Products: -
?
sirohydrochlorin + Ni2+
Ni-sirohydrochlorin + 2 H+
Substrates: reaction of EC 4.99.1.11
Products: -
Products: -
?
precorrin-2 + Co2+
cobalt-precorrin-2 + 2 H+
-
Substrates: SirB, much lower specific activity than with sirohydrochlorin
Products: -
Products: -
?
precorrin-2 + Co2+
cobalt-precorrin-2 + 2 H+
Priestia megaterium DSM 509
-
Substrates: SirB, much lower specific activity than with sirohydrochlorin
Products: -
Products: -
?
sirohydrochlorin + Co2+
Co-sirohydrochlorin + 2 H+
Substrates: reaction of EC 4.99.1.3
Products: -
Products: -
?
sirohydrochlorin + Co2+
Co-sirohydrochlorin + 2 H+
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
-
Substrates: SirB, lower specificity for cobalt than for iron
Products: -
Products: -
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
Priestia megaterium DSM 509
-
Substrates: SirB, lower specificity for cobalt than for iron
Products: -
Products: -
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Co2+
cobalt-sirohydrochlorin + 2 H+
-
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: SirB, monofunctional ferrochelatase, higher specificity for iron over cobalt
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: SirB is responsible for the final step in siroheme synthesis
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Priestia megaterium DSM 509
-
Substrates: SirB, monofunctional ferrochelatase, higher specificity for iron over cobalt
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Priestia megaterium DSM 509
-
Substrates: SirB is responsible for the final step in siroheme synthesis
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: Met8p catalyzes ferrochelation during the synthesis of siroheme, both ferrochelation and NAD+-dependent dehydrogenation of preccorin-2 to produce sirohydrochlorin take place in a single bifunctional active site, Asp-141 participates in both catalytic reactions, which are not linked mechanistically, mechanism
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Substrates: Met8p structure, bifunctional Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme, both catalytic activities share a single active site, Asp-141 functions as a general base and plays an essential role in both dehydrogenase and chelatase processes
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: Met8p catalyzes ferrochelation during the biosynthesis of siroheme
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Substrates: Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: 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
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: CysG, siroheme biosynthesis
Products: sulfur metabolism depends on siroheme
Products: sulfur metabolism depends on siroheme
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + H+
-
Substrates: pH 8.0
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + H+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with protoporphyrin IX. Sirohydrochlorin and uroporphyrin I are suitably bound beside the Co2+ ion-binding site at the active site cavity, protoporphyrin IX is also docked to the active site but its orientation is different from those of the other two tetrapyrroles
Products: -
Products: -
-
additional information
?
-
Substrates: enzyme CfbA also functions as a nickel-chelatase. The catalytic mechanism of Co2+ insertion by CfbA is likely similar to that of Ni2+ insertion. However, the rate of Co2+-insertion is much faster than that of Ni2+-insertion as observed via activity assays
Products: -
Products: -
-
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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
sirohydrochlorin + Co2+
Co-sirohydrochlorin + 2 H+
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Ni2+
Ni-sirohydrochlorin + 2 H+
Substrates: reaction of EC 4.99.1.11
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: SirB is responsible for the final step in siroheme synthesis
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Priestia megaterium DSM 509
-
Substrates: SirB is responsible for the final step in siroheme synthesis
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: Met8p catalyzes ferrochelation during the biosynthesis of siroheme
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Substrates: Met8p catalyzes the final two steps in the biosynthesis of siroheme involving a beta-NAD+-dependent dehydrogenation of precorrin-2 to generate sirohydrochlorin followed by ferrochelation to yield siroheme
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
-
Substrates: CysG, siroheme biosynthesis
Products: sulfur metabolism depends on siroheme
Products: sulfur metabolism depends on siroheme
?
sirohydrochlorin + Fe2+
siroheme + 2 H+
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + H+
-
Substrates: -
Products: -
Products: -
?
sirohydrochlorin + Fe2+
siroheme + H+
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
additional information
although H146 is located in the vicinity of the active centre, it is not expected to be involved in metal binding, which agrees with experimental data indicating that it is not a functionally important residue
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
it is not possible to measure an accurate KM value for the metals as at low concentration of metal the assay is not sensitive enough, whereas at higher metal ion concentrations the enzyme is inactivated
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.055
Co2+
chimeric mutant enzyme, pH and temperature not specified in the publication
0.06
Co2+
wild-type enzyme, pH and temperature not specified in the publication
0.055
sirohydrochlorin
chimeric mutant enzyme, with Co2+, pH and temperature not specified in the publication
0.06
sirohydrochlorin
wild-type enzyme, with Co2+, pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33.25
-
mutant enzyme C199A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23°C
36.08
-
mutant enzyme C213A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23°C
38.5
-
wild type enzyme, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23°C
43
-
mutant enzyme C219A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23°C
44.67
-
mutant enzyme C135A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23°C
55.17
-
mutant enzyme C210A, in 20 mM Tris/HCl (pH 8.0) and 10 mM NaCl, at 23°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression of both uroporphyrinogen III methyl transferase (UPM1) and sirohydrochlorin ferrochelatase is minimal in etiolated seedlings and is upregulated in light
brenda
additional information
gene expression is found in all tissues analyzed
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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
evolution
metabolism
siroheme is synthesized in bacteria from uroporphyrinogen III in a three-step reaction that includes methylation of uroporphyrinogen III, NAD+-dependent oxidation of precorrin-2, and insertion of iron into sirohydrochlorin. Siroheme biosynthetic pathway of Staphylococcus aureus, overview. NirR is a sirohydrochlorin ferrochelatase, and therefore, it is renamed as ShfC. Sirohydrochlorin ferrochelatase (ShfC) is essential for nitrite reduction
physiological function
additional information
evolution
class II chelatases are a family of enzymes catalyzing insertion of a divalent metal ion into modified tetrapyrroles to yield cobalamin, heme, siroheme, and coenzyme F430. Five different class II chelatases, CbiX, CbiK, SirB, HemH, and CbiXS, have been identified. Enzyme CfbA is an important ancestor of all the class II chelatase family of enzymes, including SirB and CbiK/CbiX, functioning not only as a nickel-chelatase, but also as a cobalt-chelatase in vitro. Thus, CfbA is a key enzyme in terms of diversity and evolution of the chelatases catalyzing formation of metal-SHC-type of cofactors. Phlogenetic analysis, CfbA contains a non-His-rich region, designated as type II CfbA, is closely related to CbiXS from Archaeoglobus fulgidus, compared to His-rich CfbA (designated as type I CfbA). A chimeric CfbA, containing a non-His-rich region derived from Methanosarcina barkeri CfbA in place of the His-rich region, is constructed. The X-ray crystal structure of the chimeric CfbA shows that the non-His-rich region has a structured form and is positioned as in the Archaeoglobus fulgidus CbiXS, which is also a non-His-rich ancestral chelatase. Therefore, the resulting structures of wild-type and chimeric CfbA demonstrate not only that the His-rich region is intrinsically flexible, but also that the non-His-rich CfbA is structurally similar to CbiXS from archaea with no coenzyme F430, rather than the His-rich CfbA
evolution
within bacteria, siroheme synthesis may occur via one, two or three enzymes, the correspondent pathways are named as types 1, 2 and 3, respectively. Phylogenetic analysis reveals that type 1 is the most used pathway in Gammaproteobacteria and Streptomycetales, type 2 predominates in Fibrobacteres and Vibrionales, and type 3 predominates in Firmicutes of the Bacillales order. The current distribution of siroheme pathways within bacteria, which changes at the genus or species level and within taxa, seems to be the result of evolutionary multiple fusion/fission events. Within the organisms that perform siroheme biosynthesis via the type 3 pathway, the chelatase operative in the last step may be performed by four different enzymes, namely SirB, CbiXL, CbiXS, and CbiK. The last three proteins have been described as sirohydrochlorin cobaltochelatases (EC 4.99.1.3), but they also exhibit ferrochelatase activity
physiological function
Bacillus subtilis SirB catalyses the insertion of Fe2+ into the substrate sirohydrochlorin (SHC) in siroheme biosynthesis
physiological function
the gene annotated as nirR in the genome of Staphylococcus aureus, and proposed to encode a nitrite reductase transcriptional regulator, is in fact a sirohydrochlorin ferrochelatase that performs the last step of the siroheme biosynthesis pathway, phylogenetic analysis
physiological function
-
Bacillus subtilis SirB catalyses the insertion of Fe2+ into the substrate sirohydrochlorin (SHC) in siroheme biosynthesis
-
additional information
the structure of SirB with Co2+ shows that the active site of SirB is located at the N-terminal domain with metal-binding amino acid residues His10, Glu43, and His76, which is also predicted for CbiX, but is distinct from the C-terminal active sites of CbiK and HemH. The key structural features for substrate recognition of SirB is the hydrophobic area at the active site as well as the substituents of the tetrapyrroles
additional information
residues H22 and H87, which are predicted by homology modelling to be located at the active site, control the ferrochelatase activity by binding of the metallated substrate. Homology-based structure modelling of ShfC using Salmonella enterica enzyme CbiK (PDB ID 2XWP) as template, which contains a metallated sirohydrochlorin at the active site
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
homodimer
-
each monomer is composed of three functional domains, domain structure
homodimer
three structural domains per monomer, domain structure
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
CysG, phosphorylation of Ser-128, plays a regulatory role
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using in 0.2 M imidazole malate pH 5.5, 24% (w/v) PEG 600 at a ratio of 50:50 ratio of protein : mother liquor and 10% ethylene glycol
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C135A
-
the mutant shows increased specific activity compared to the wild type enzyme
C199A
-
the mutant shows reduced specific activity compared to the wild type enzyme
C210A
-
the mutant shows increased specific activity compared to the wild type enzyme
C213A
-
the mutant shows reduced specific activity compared to the wild type enzyme
C219A
-
the mutant shows increased specific activity compared to the wild type enzyme
D141A
G22D
H237A
mutant of bifunctional Met8p is active as both dehydrogenase and ferrochelatase
S128A
-
mutant has higher cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
S128D
-
mutant has lower cobalt chelatase activity than wild-type CysG with sirohydrochlorin as substrate
H146L
site-directed mutagenesis, although H146 is highly conserved among sirohydrochlorin ferrochelatase-like proteins, replacement by leucine does not cause alterations on the phenotype
H22L
site-directed mutagenesis, the mutation does not revert the cysteine auxotrophy of the strain, which is consistent with the need of these residues are necessary for the function of the enzyme
H87L
site-directed mutagenesis, the mutation does not revert the cysteine auxotrophy of the strain, which is consistent with the need of these residues are necessary for the function of the enzyme
additional information
D141A
-
mutant of bifunctional Met8p is devoid of both dehydrogenase and ferrochelatase activities
D141A
mutant of bifunctional Met8p is completely inactive as both dehydrogenase and ferrochelatase
G22D
-
mutant of bifunctional Met8p is completely inactive as NAD+-dependent dehydrogenase, but functions as ferrochelatase
G22D
mutant of bifunctional Met8p is completely inactive as dehydrogenase, but functions as ferrochelatase
additional information
to study the structural flexibility of the His-rich region, a chimeric CfbA, containing a non-His-rich region derived from Methanosarcina barkeri CfbA in place of the His-rich region, is constructed. The X-ray crystal structure of the chimeric CfbA shows that the non-His-rich region has a structured form and is positioned as in the Archaeoglobus fulgidus CbiXS, which is also a non-His-rich ancestral chelatase. Therefore, the resulting structures of wild-type and chimeric CfbA demonstrate not only that the His-rich region is intrinsically flexible, but also that the non-His-rich CfbA is structurally similar to CbiXS from archaea with no coenzyme F430, rather than the His-rich CfbA
additional information
construction of a nirR mutant, the evaluation of the expression of nirB and cysG1 in the Staphylococcus aureus DELTAnirR mutant reveals that the expression of these genes shows negligible differences between wild-type and the mutant, which rules out the regulatory role of NirR. Under anaerobic conditions, the sirohydrochlorin ferrochelatase nirR mutant strain shows no nitrite consumption, which is consistent with the lack of siroheme formation. Co-expression of sirohydrochlorin ferrochelatase NirR, encoded by gene nirR, with Methanothermobacter thermautotrophicus sirC and Pseudomonas denitrificans cobA leads to complementation of Escherichia coli DELTA302a mutant. This strain lacks the Escherichia coli cysG gene, and because it is unable to synthesize siroheme, it only grows in medium supplemented with cysteine or sulfide, or when the strain expresses other proteins capable of producing siroheme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene nirR, sequence comparisons, the gene annotated as nirR in the genome of Staphylococcus aureus, and proposed to encode a nitrite reductase transcriptional regulator, is in fact a sirohydrochlorin ferrochelatase that performs the last step of the siroheme biosynthesis pathway, phylogenetic analysis. The siroheme genes of Staphylococcus spp. are located in the vicinity of the nitrite reductase operon. The nirR gene has 732 bp, and its initiation codon is annotated as GTG, which encodes a valine amino acid instead of methionine. After several attempts, this gene product cannot be expressed successfully. The most probable ATG start codon is located 39 bp upstream of the one annotated in the genome giving rise to a gene with 771 bp. This DNA segment is cloned into pET-23b, and a protein of 255 amino acids and a molecular mass of approximately 29 kDa is produced. Co-expression of sirohydrochlorin ferrochelatase NirR, encoded by gene nirR, with Methanothermobacter thermautotrophicus sirC and Pseudomonas denitrificans cobA leads to complementation of Escherichia coli DELTA302a mutant
sirB, expression in Escherichia coli BL21(DE3)pLysS, sirA,B,C operon, amino acid sequence
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of both uroporphyrinogen III methyl transferase (UPM1) and sirohydrochlorin ferrochelatase is minimal in etiolated seedlings and is upregulated in light
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schubert, H.L.; Raux, E.; Brindley, A.A.; Leech, H.K.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase
EMBO J.
21
2068-2075
2002
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P15807)
brenda
Raux, E.; Leech, H.K.; Beck, R.; Schubert, H.L.; Santander, P.J.; Roessner, C.A.; Scott, A.I.; Martens, J.H.; Jahn, D.; Thermes, C.; Rambach, A.; Warren, M.J.
Identification and functional analysis of enzymes required for precorrin-2 dehydrogenation and metal ion insertion in the biosynthesis of sirohaem and cobalamin in Bacillus megaterium
Biochem. J.
370
505-516
2003
Priestia megaterium, Priestia megaterium DSM 509
brenda
Schubert, H.L.; Raux, E.; Matthews, M.A.; Phillips, J.D.; Wilson, K.S.; Hill, C.P.; Warren, M.J.
Structural diversity in metal ion chelation and the structure of uroporphyrinogen III synthase
Biochem. Soc. Trans.
30
595-600
2002
Saccharomyces cerevisiae
brenda
Stroupe, M.E.; Leech, H.K.; Daniels, D.S.; Warren, M.J.; Getzoff, E.D.
CysG structure reveals tetrapyrrole-binding features and novel regulation of siroheme biosynthesis
Nat. Struct. Biol.
10
1064-1073
2003
Salmonella enterica
brenda
Raux-Deery, E.; Leech, H.K.; Nakrieko, K.A.; McLean, K.J.; Munro, A.W.; Heathcote, P.; Rigby, S.E.; Smith, A.G.; Warren, M.J.
Identification and characterization of the terminal enzyme of siroheme biosynthesis from Arabidopsis thaliana: a plastid-located sirohydrochlorin ferrochelatase containing a 2FE-2S center
J. Biol. Chem.
280
4713-4721
2005
Arabidopsis thaliana
brenda
Lobo, S.A.; Brindley, A.; Warren, M.J.; Saraiva, L.M.
Functional characterization of the early steps of tetrapyrrole biosynthesis and modification in Desulfovibrio vulgaris Hildenborough
Biochem. J.
420
317-325
2009
no activity in Desulfovibrio vulgaris
brenda
Romao, C.V.; Ladakis, D.; Lobo, S.A.; Carrondo, M.A.; Brindley, A.A.; Deery, E.; Matias, P.M.; Pickersgill, R.W.; Saraiva, L.M.; Warren, M.J.
Evolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerization
Proc. Natl. Acad. Sci. USA
108
97-102
2011
Priestia megaterium
brenda
Saha, K.; Webb, M.E.; Rigby, S.E.; Leech, H.K.; Warren, M.J.; Smith, A.G.
Characterization of the evolutionarily conserved iron-sulfur cluster of sirohydrochlorin ferrochelatase from Arabidopsis thaliana
Biochem. J.
444
227-237
2012
Arabidopsis thaliana
brenda
Bali, S.; Rollauer, S.; Roversi, P.; Raux-Deery, E.; Lea, S.M.; Warren, M.J.; Ferguson, S.J.
Identification and characterization of the missing terminal enzyme for siroheme biosynthesis in alpha-proteobacteria
Mol. Microbiol.
92
153-163
2014
Paracoccus pantotrophus
brenda
Garai, S.; Joshi, N.C.; Tripathy, B.C.
Phylogenetic analysis and photoregulation of siroheme biosynthesis genes uroporphyrinogen III methyltransferase and sirohydrochlorin ferrochelatase of Arabidopsis thaliana
Physiol. Mol. Biol. Plants
22
351-359
2016
Arabidopsis thaliana (Q84JH7)
brenda
Videira, M.A.M.; Lobo, S.A.L.; Sousa, F.L.; Saraiva, L.M.
Identification of the sirohaem biosynthesis pathway in Staphylococcus aureus
FEBS J.
287
1537-1553
2020
Staphylococcus aureus (A0A0H3KA92)
brenda
Fujishiro, T.; Ogawa, S.
The nickel-sirohydrochlorin formation mechanism of the ancestral class II chelatase CfbA in coenzyme F430 biosynthesis
Chem. Sci.
12
2172-2180
2021
Methanocaldococcus jannaschii (A0A832WLA4)
brenda
Fujishiro, T.; Shimada, Y.; Nakamura, R.; Ooi, M.
Structure of sirohydrochlorin ferrochelatase SirB the last of the structures of the class II chelatase family
Dalton Trans.
48
6083-6090
2019
Bacillus subtilis (O34632), Bacillus subtilis 168 (O34632)
brenda
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