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2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
S-adenosyl-L-methionine + heptacarboxyporphyrinogen III
?
-
-
-
-
?
S-adenosyl-L-methionine + hexacarboxyporphyrinogen III
?
-
-
-
-
?
S-adenosyl-L-methionine + pentacarboxyporphyrinogen III
?
-
-
-
-
?
S-adenosyl-L-methionine + precorrin-1
S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
S-adenosyl-L-methionine + precorrin-2
S-adenosyl-L-homocysteine + trimethylpyrrocorphin
-
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen I
?
S-adenosyl-L-methionine + uroporphyrinogen III
?
S-adenosyl-L-methionine + uroporphyrinogen III
S-adenosyl-L-homocysteine + precorrin-1
-
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
additional information
?
-
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
no synthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
methylates positions 2 and 7
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
after prolonged incubation (15 h) also tri- and tetra-methylated compounds formed, third methyl group at position 12, product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
produces equal amounts of precorrin-1 and precorrin-2, product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
overall reaction
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
ir
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen I
?
-
methylates positions 2 and 7
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen I
?
methylates positions 2 and 7
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen I
?
-
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen III
?
-
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen III
?
-
-
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
via precorrin-1
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
the enzyme binds S-adenosyl-L-methionine and catalyzes the production of III methyl uroporphyrinogen in vitro
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
the enzyme binds S-adenosyl-L-methionine and catalyzes the production of III methyl uroporphyrinogen in vitro
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
-
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
NirE binds S-adenosyl-L-methionine, although not with the same avidity as reported for other SAM-dependent uroporphyrinogen III methyltransferases involved in siroheme and cobalamin biosynthesis
-
-
?
additional information
?
-
Q96532
no formation of sirohydrochlorin in presence of NAD+ or NADP+
-
-
?
additional information
?
-
-
no formation of sirohydrochlorin in presence of NAD+ or NADP+
-
-
?
additional information
?
-
-
uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris
-
-
?
additional information
?
-
-
at high enzyme concentrations NirE catalyzes an overmethylation of uroporphyrinogen III, resulting in the formation of trimethylpyrrocorphin
-
-
?
additional information
?
-
-
uroporphyrin III is not a substrate of the enzyme
-
-
?
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2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
S-adenosyl-L-methionine + precorrin-1
S-adenosyl-L-homocysteine + precorrin-2
-
-
-
?
S-adenosyl-L-methionine + precorrin-2
S-adenosyl-L-homocysteine + trimethylpyrrocorphin
-
-
-
-
?
S-adenosyl-L-methionine + uroporphyrinogen III
S-adenosyl-L-homocysteine + precorrin-1
-
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
additional information
?
-
-
uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
Q96532
no synthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of sirohydrochlorin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of cobalamin
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
-
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + dihydrosirohydrochlorin + 2 H+
-
involved in biosynthesis of siroheme
product is precorrin-2
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
-
-
-
-
?
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
overall reaction
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
via precorrin-1
-
-
?
uroporphyrinogen III + S-adenosyl-L-methionine
precorrin-2 + S-adenosyl-L-homocysteine
-
-
-
-
?
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D248A
-
no transmethylase activity
G224A
-
unable to bind S-adenosyl-L-methionine
R298L
-
unable to bind S-adenosyl-L-methionine
R309L
-
no transmethylase activity
H161F
the mutant shows reduced activity compared to the wild type enzyme
K102A
the mutant shows no activity and strongly reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
R149K
the mutant shows no activity compared to the wild type enzyme
R51D
residue R51 is mainly involved in stabilization of the propionate side chain of ring A by hydrophobic interactions with an average distance of 4.1 A. In the mutant R51K, the side chain of K51 makes stable electrostatic interactions with the acetate side chain of ring A, however there are no hydrophobic interactions
R51K
the mutant shows reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
D47N
-
binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1
F106A
-
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity
L49A
-
binds about half the quantity of S-adenosyl-L-methionine compared with wild-type, reaction products are oxidised forms of both precorrin-1 and precorrin-2
M184A
-
slight enzymic activity
T130A
-
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine
Y183A
-
considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity
G12A
site-directed mutagenesis of cobA abolishes the tellurite resistance of the mesophilic, heterologous host Escherichia coli and the SUMT activity in vitro. Cells overexpressing SUMT G12A show 7fold less tolerance to K2TeO3 as compared to that exhibit by cells expressing the wild-type methyltransferase
G12A
-
site-directed mutagenesis of cobA abolishes the tellurite resistance of the mesophilic, heterologous host Escherichia coli and the SUMT activity in vitro. Cells overexpressing SUMT G12A show 7fold less tolerance to K2TeO3 as compared to that exhibit by cells expressing the wild-type methyltransferase
-
E114Q
the mutant shows strongly reduced activity compared to the wild type enzyme
E114Q
increase in the root mean square deviations of the uroporphyrinogen III substrate in respect to the wild-type
G189K
the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
G189K
increase in activity compared to wild-type. The side chain of K189 makes electrostatic interactions with the propionate side chain of ring B with an average distance of 4.0 A. The backbone of K189 makes hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III
G189N
the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
G189N
increase in activity compared to wild-type. Both side chain and the backbone of N189 residue participates in hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III
M186L
the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
M186L
loss of hydrophobic interactions between the side chain of L186 and methyl group of SAM
R111K
the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme
R111K
the side chain of residue R111 stabilizes the uroporphyrinogen III ring A acetate side chain by electrostatic interactions. Mutant R111K makes very unstable interactions with an average distance of 5 A between the acetate of ring A of uroporphyrinogen III
additional information
-
separation of the individual enzyme activities, uroporphyrinogen III synthase and uroporphyrinogen III methyltransferase, by dissecting the relevant gene to allow the production of two distinct proteins
additional information
-
construction of a nirE transposon mutant, which is not complemented by native cobA encoding the SAM-dependent uroporphyrinogen III methyltransferase involved in cobalamin formation, overview
additional information
-
deletion mutants, truncated one deleting the C-terminal extra 52 amino acids actively expressed in Escherichia coli, the mature SUMT fusion mutant or the mature SUMT deleting the N-terminal 36 amino acids including glycine-rich region involved directly in SAM binding expressed as an inclusion body in Escherichia coli
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Warren, M.J.; Gonzalez, M.D.; Williams, H.J.; Stolowich, N.J.; Scott, A.I.
Uroporpyrinogen III methylase catalyzes the enzymatic synthesis of sirohydrochlorines II and IV by a clockwise mechanism
J. Am. Chem. Soc.
112
5343-5345
1990
Escherichia coli
-
brenda
Warren, M.J.; Roessner, C.A.; Santander, P.J.; Scott, A.I.
The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase
Biochem. J.
265
725-729
1990
Escherichia coli
brenda
Blanche, F.; Debussche, L.; Thibaut, D.; Crouzet, J.; Cameron, B.
Purification and characterization of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Pseudomonas denitrificans
J. Bacteriol.
171
4222-4231
1989
Pseudomonas denitrificans (nom. rej.)
brenda
Crouzet, J.; Cauchois, L.; Blanche, F.; Debussche, L.; Thibaut, D.; Rouyez, M.C.; Rigault, S.; Mayaux, J.F.; Cameron, B.
Nucleotide sequence of a Pseudomonas denitrificans 5.4-kilobase DNA fragment containing five cob genes and identification of structural genes encoding S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase and cobyrinic acid a,c-diamide synthase
J. Bacteriol.
172
5968-5979
1990
Pseudomonas denitrificans (nom. rej.) (P21632), Pseudomonas denitrificans (nom. rej.)
brenda
Sattler, I.; Roessner, C.A.; Stolowich, N.J.; Hardin, S.H.; Harris-Haller, L.W.; Yokubaitis, N.T.; Murooka, Y.; Hashimoto, Y.; Scott, A.I.
Cloning, sequencing, and expression of the uroporphyrinogen III methyltransferease cobA gene of Propionibacterium freudenreichii (shermanii)
J. Bacteriol.
177
1564-1569
1995
Propionibacterium freudenreichii (Q51720), Propionibacterium freudenreichii
brenda
Chou, P.L.; Ohtsuka, M.; Minowa, T.; Yamasato, K.; Sakano, Y.; Matsuzawa, H.; Ohta, T.; Sakai, H.
Reddish Escherichia coli cells caused by overproduction of Bacillus stearothermophilus uroporphyrinogen III methylase: cloning, sequencing, and expression of the gene
Biosci. Biotechnol. Biochem.
59
1817-1824
1995
Geobacillus stearothermophilus
brenda
Sakakibara, H.; Takei, K.; Sugiyama, T.
Isolation and characterization of a cDNA that encodes maize uroporphyrinogen III methyltransferase, an enzyme involved in the synthesis of siroheme, which is a prosthetic group of nitrite reductase
Plant J.
10
883-892
1996
Zea mays
brenda
Leustek, T.; Smith, M.; Murillo, M.; Singh, D.P.; Smith, A.G.; Woodcock, S.C.; Awan, S.J.; Warren, M.J.
Siroheme biosynthesis in higher plants. Analysis of an S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase from Arabidopsis thaliana
J. Biol. Chem.
272
2744-2752
1997
Arabidopsis thaliana (Q96532), Arabidopsis thaliana
brenda
Woodcock, S.C.; Raux, E.; Levillayer, F.; Thermes, C.; Rambach, A.; Warren, M.J.
Effect of mutations in the transmethylase and dehydrogenase/chelatase domains of siroheme synthase (CysG) on siroheme and cobalamin biosynthesis
Biochem. J.
330
121-129
1998
Escherichia coli
-
brenda
Raux, E.; McVeigh, T.; Peters, S.E.; Leustek, T.; Warren, M.J.
The role of Saccharomyces cerevisiae MET1p and MET8p in sirohaem and cobalamin biosynthesis
Biochem. J.
338
701-708
1999
Escherichia coli, Pseudomonas denitrificans (nom. rej.), Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium
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Zea mays
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Lobo, S.A.; Brindley, A.; Warren, M.J.; Saraiva, L.M.
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The Pseudomonas aeruginosa nirE gene encodes the S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase required for heme d1 biosynthesis
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Pseudomonas aeruginosa
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Geobacillus stearothermophilus (Q6TA16), Geobacillus stearothermophilus, Geobacillus stearothermophilus V (Q6TA16), Geobacillus stearothermophilus V
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Limosilactobacillus reuteri, Limosilactobacillus reuteri CRL 1098
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Crystal structure of the heme d1 biosynthesis enzyme NirE in complex with its substrate reveals new insights into the catalytic mechanism of S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferases
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Pseudomonas aeruginosa (P95417), Pseudomonas aeruginosa
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Blanche, F.; Robin, C.; Couder, M.; Faucher, D.; Cauchois, L.; Cameron, B.; Crouzet, J.
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Hordeum vulgare (D2KI47), Hordeum vulgare
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Wang, Z.; Yan, H.; Li, S.; Zhang, K.; Cheng, B.; Fan, J.
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Escherichia coli
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Wang, Z.; Li, S.; Li, J.; Li, J.; Rong, L.; Cheng, B.; Fan, J.
Engineering uroporphyrinogen III methyltransferase as a red fluorescent reporter in E. coli
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Hordeum vulgare (F2CPW6), Hordeum vulgare
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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
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Arabidopsis thaliana
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Videira, M.A.M.; Lobo, S.A.L.; Sousa, F.L.; Saraiva, L.M.
Identification of the sirohaem biosynthesis pathway in Staphylococcus aureus
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Staphylococcus aureus (A0A0H3KAA0), Staphylococcus aureus Newman (A0A0H3KAA0)
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Alleviation of nitrogen and sulfur deficiency and enhancement of photosynthesis in arabidopsis thaliana by overexpression of uroporphyrinogen III methyltransferase (UPM1)
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Arabidopsis thaliana
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Singh, W.; Karabencheva-Christova, T.G.; Black, G.W.; Ainsley, J.; Dover, L.; Christov, C.Z.
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Pseudomonas aeruginosa (P95417)
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