Information on EC 2.1.1.107 - uroporphyrinogen-III C-methyltransferase:

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The expected taxonomic range for this enzyme is: Bacteria

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EC NUMBERCOMMENTARY
2.1.1.107-

RECOMMENDED NAMEGeneOntology No.
uroporphyrinogen-III C-methyltransferaseGO:0004851

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2
show the reaction diagram
----
S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1
show the reaction diagram
----

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
methyl group transfer----

PATHWAYKEGG LinkMetaCyc Link
Biosynthesis of secondary metabolites01110 -
Metabolic pathways01100 -
Porphyrin and chlorophyll metabolism00860 -

SYSTEMATIC NAMEIUBMB Comments
S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferaseThis enzyme catalyses two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. The second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase) and the third step involves the chelation of Fe2+ to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). 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 SirA being responsible for the above reaction. Also involved in the biosynthesis of cobalamin.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
adenosylmethionine-uroporphyrinogen III methyltransferase----
CobA/HemDLactobacillus reuteri--714579
HemD-CobADesulfovibrio vulgaris--696120
NirEPseudomonas aeruginosa--703663, 719948
S-adenosyl-L-methionine dependent uroporphyrinogen III methylase----
S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferasePseudomonas aeruginosaP95417-719948
S-adenosyl-L-methionine: uroporphyrinogen III methyltransferaseZea mays--676956
SAM-dependent uroporphyrinogen III methyltransferasePseudomonas aeruginosa--703663
sirohaem synthase----
SUMTPseudomonas denitrificans--662638
SUMTZea mays--676956
SUMTPseudomonas aeruginosa--703663
SUMTGeobacillus stearothermophilus, Geobacillus stearothermophilus VQ6TA16-706702
uroporphyrinogen III C-methyltransferase----
uroporphyrinogen III methylase----
uroporphyrinogen III methyltransferaseZea mays--676956
uroporphyrinogen III methyltransferasePseudomonas aeruginosa--703663
uroporphyrinogen III methyltransferase/synthaseDesulfovibrio vulgaris--696120
uroporphyrinogen III synthase/methyltransferaseLactobacillus reuteri--714579
uroporphyrinogen methyltransferase,----

CAS REGISTRY NUMBERCOMMENTARY
73665-99-3-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thalianagenomic DNA, cDNA has accession number L47479485090Q96532SwissProtManually annotated by BRENDA team
Desulfovibrio vulgarisgene cobA/hemD696120--Manually annotated by BRENDA team
Escherichia coli-485083, 485084, 485091, 485092--Manually annotated by BRENDA team
Geobacillus stearothermophilus-485088--Manually annotated by BRENDA team
Geobacillus stearothermophilusgene cobA706702Q6TA16UniProtManually annotated by BRENDA team
Geobacillus stearothermophilus Vgene cobA706702Q6TA16UniProtManually annotated by BRENDA team
Lactobacillus reuteri-714579--Manually annotated by BRENDA team
Lactobacillus reuteri CRL 1098-714579--Manually annotated by BRENDA team
Propionibacterium freudenreichii-485087Q51720SwissProtManually annotated by BRENDA team
Pseudomonas aeruginosa-719948P95417UniProtManually annotated by BRENDA team
Pseudomonas aeruginosastrain PAO1, gene nirE703663--Manually annotated by BRENDA team
Pseudomonas denitrificans-485085, 485092, 662638--Manually annotated by BRENDA team
Pseudomonas denitrificans-485086P21632GenBankManually annotated by BRENDA team
Saccharomyces cerevisiae-485092--Manually annotated by BRENDA team
Salmonella enterica subsp. enterica serovar Typhimurium-485092--Manually annotated by BRENDA team
Thermus thermophilus-660612--Manually annotated by BRENDA team
Zea mays-485089, 676956--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismDesulfovibrio vulgaris G200, Desulfovibrio vulgaris Groningen, Desulfovibrio vulgaris Hildenborough ATCC 29579, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris Marburg, Desulfovibrio vulgaris Miyazaki F., Desulfovibrio vulgaris Miyazaki F, Desulfovibrio vulgaris Miyazaki, Desulfovibrio vulgaris-the enzyme is involved in the tetrapyrrole biosynthesis. Uroporphyrinogen III represents the first branch point in the pathway, where the action of enzymes such as HemE, F (N) and G results in the formation of protoporphyrin IX, a precursor of modified tetrapyrroles such as haem and chlorophyll. Alternatively, uroporphyrinogen III can undergo a S-adenosylmethionine-dependent transmethylation positions 2 and 7, by CysG, Met1p or CobA depending on the organism, to generate precorrin-2, a highly unstable yellow dipyrrocorphin, overview696120
metabolismPseudomonas aeruginosa-the enzyme is important in the heme d1 biosynthesis, the essential prosthetic group of the dissimilatory nitrite reductase cytochrome cd1 requiring the methylation of the tetrapyrrole precursor uroporphyrinogen III at positions C-2 and C-7, pathway overview703663
metabolismLactobacillus reuteri 121, Lactobacillus reuteri 21, Lactobacillus reuteri ATCC 55739, Lactobacillus reuteri ATCC PTA 6475, Lactobacillus reuteri BR11, Lactobacillus reuteri CRL 1098, Lactobacillus reuteri CRL1098, Lactobacillus reuteri CRL 1100, Lactobacillus reuteri CRL 1101, Lactobacillus reuteri L103, Lactobacillus reuteri L461, Lactobacillus reuteri MEP181R88, Lactobacillus reuteri RT-5, Lactobacillus reuteri TMW1.106, Lactobacillus reuteri-uroporphyrinogen III synthase/methyltransferase is a key bifunctional enzyme in the biosynthesis of cobalamin and other tetrapyrrols714579
physiological functionGeobacillus stearothermophilus, Geobacillus stearothermophilus VQ6TA16the role of SUMT methyltransferase in tellurite(ate) detoxification is not related to tellurium volatilization706702

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate
LITERATURE/
Substrate
COMMENTARY/
Product
LITERATURE/
Product
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + heptacarboxyporphyrinogen III?
show the reaction diagram
Pseudomonas denitrificans--485085--?
S-adenosyl-L-methionine + hexacarboxyporphyrinogen III?
show the reaction diagram
Pseudomonas denitrificans--485085--?
S-adenosyl-L-methionine + pentacarboxyporphyrinogen III?
show the reaction diagram
Pseudomonas denitrificans--485085--?
S-adenosyl-L-methionine + uroporphyrinogen I?
show the reaction diagram
Pseudomonas denitrificans--485085--?
S-adenosyl-L-methionine + uroporphyrinogen I?
show the reaction diagram
Escherichia coli-methylates positions 2 and 7485083--?
S-adenosyl-L-methionine + uroporphyrinogen I?
show the reaction diagram
Propionibacterium freudenreichiiQ51720methylates positions 2 and 7485087--?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans--485085produces equal amounts of precorrin-1 and precorrin-2485085?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Propionibacterium freudenreichiiQ51720-485087after prolonged incubation (15 h) also tri- and tetra-methylated compounds formed, third methyl group at position 12485087?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli, Saccharomyces cerevisiae--485092product is precorrin-2485092?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Geobacillus stearothermophilus--485088product is precorrin-2485088?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Zea mays--485089product is precorrin-2485089?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans--485085product is precorrin-2485085?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans--485092product is precorrin-2485092?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificansP21632-485086product is precorrin-2485086?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Propionibacterium freudenreichiiQ51720-485087product is precorrin-2485087?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Arabidopsis thalianaQ96532-485090product is precorrin-2485090?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-methylates positions 2 and 7485083product is precorrin-2485083?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-methylates positions 2 and 7485084product is precorrin-2485084?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-methylates positions 2 and 7485091product is precorrin-2485091?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-methylates positions 2 and 7485092product is precorrin-2485092?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-involved in biosynthesis of sirohydrochlorin485083product is precorrin-2485083?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-involved in biosynthesis of sirohydrochlorin485084product is precorrin-2485084?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Propionibacterium freudenreichiiQ51720involved in biosynthesis of sirohydrochlorin485087product is precorrin-2485087?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Saccharomyces cerevisiae-involved in biosynthesis of siroheme485092product is precorrin-2485092?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Zea mays-involved in biosynthesis of siroheme485089product is precorrin-2485089?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Arabidopsis thalianaQ96532involved in biosynthesis of siroheme485090product is precorrin-2485090?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-involved in biosynthesis of cobalamin485091product is precorrin-2485091?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans-involved in biosynthesis of cobalamin485085product is precorrin-2485085?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificansP21632involved in biosynthesis of cobalamin485086product is precorrin-2485086?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Propionibacterium freudenreichiiQ51720involved in biosynthesis of cobalamin485087product is precorrin-2485087?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Arabidopsis thalianaQ96532no synthesis of cobalamin485090product is precorrin-2485090?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans SC510-involved in biosynthesis of cobalamin485086product is precorrin-2485086?
S-adenosyl-L-methionine + uroporphyrinogen III?
show the reaction diagram
Lactobacillus reuteri--714579--?
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + precorrin-2
show the reaction diagram
Pseudomonas aeruginosaP95417-719948--ir
uroporphyrinogen III + S-adenosyl-L-methionineprecorrin-2 + S-adenosyl-L-homocysteine
show the reaction diagram
Pseudomonas aeruginosa--703663--?
uroporphyrinogen III + S-adenosyl-L-methionineprecorrin-2 + S-adenosyl-L-homocysteine
show the reaction diagram
Desulfovibrio vulgaris-via precorrin-1696120--?
uroporphyrinogen III + S-adenosyl-L-methionineprecorrin-2 + S-adenosyl-L-homocysteine
show the reaction diagram
Pseudomonas aeruginosa-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 biosynthesis703663--?
uroporphyrinogen III + S-adenosyl-L-methionineprecorrin-2 + S-adenosyl-L-homocysteine
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus VQ6TA16the enzyme binds S-adenosyl-L-methionine and catalyzes the production of III methyl uroporphyrinogen in vitro706702--?
additional information?-Arabidopsis thalianaQ96532no formation of sirohydrochlorin in presence of NAD+ or NADP+485090---
additional information?-Pseudomonas denitrificans-uroporphyrin III is not a substrate of the enzyme485085---
additional information?-Desulfovibrio vulgaris-uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris696120---
additional information?-Pseudomonas aeruginosa-at high enzyme concentrations NirE catalyzes an overmethylation of uroporphyrinogen III, resulting in the formation of trimethylpyrrocorphin703663---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)
COMMENTARY PRODUCTLITERATURE
(Product)
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli--485092product is precorrin-2485092
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Geobacillus stearothermophilus--485088product is precorrin-2485088
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans--485092product is precorrin-2485092
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-involved in biosynthesis of sirohydrochlorin485083product is precorrin-2485083
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-involved in biosynthesis of sirohydrochlorin485084product is precorrin-2485084
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Propionibacterium freudenreichiiQ51720involved in biosynthesis of sirohydrochlorin485087product is precorrin-2485087
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Saccharomyces cerevisiae-involved in biosynthesis of siroheme485092product is precorrin-2485092
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Zea mays-involved in biosynthesis of siroheme485089product is precorrin-2485089
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Arabidopsis thalianaQ96532involved in biosynthesis of siroheme485090product is precorrin-2485090
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Escherichia coli-involved in biosynthesis of cobalamin485091product is precorrin-2485091
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans-involved in biosynthesis of cobalamin485085product is precorrin-2485085
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificansP21632involved in biosynthesis of cobalamin485086product is precorrin-2485086
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Propionibacterium freudenreichiiQ51720involved in biosynthesis of cobalamin485087product is precorrin-2485087
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Arabidopsis thalianaQ96532no synthesis of cobalamin485090product is precorrin-2485090
S-adenosyl-L-methionine + uroporphyrinogen IIIS-adenosyl-L-homocysteine + dihydrosirohydrochlorin
show the reaction diagram
Pseudomonas denitrificans SC510-involved in biosynthesis of cobalamin485086product is precorrin-2485086
uroporphyrinogen III + S-adenosyl-L-methionineprecorrin-2 + S-adenosyl-L-homocysteine
show the reaction diagram
Pseudomonas aeruginosa--703663--
uroporphyrinogen III + S-adenosyl-L-methionineprecorrin-2 + S-adenosyl-L-homocysteine
show the reaction diagram
Desulfovibrio vulgaris-via precorrin-1696120--
additional information?-Desulfovibrio vulgaris-uroporphyrinogen III synthase is fused to uroporphyrinogen III methyltransferase in Desulfovibrio vulgaris696120--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
S-adenosyl-L-methionineDesulfovibrio vulgaris--696120 2D-image
S-adenosyl-L-methioninePseudomonas aeruginosa-dependent on703663 2D-image
S-adenosyl-L-methionineGeobacillus stearothermophilus, Geobacillus stearothermophilus VQ6TA16-706702 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Pseudomonas denitrificans, Pseudomonas denitrificans CCUG 2519, Pseudomonas denitrificans G3575, Pseudomonas denitrificans SC510 Rif, Pseudomonas denitrificans SC510 Rifr(pXL1149), Pseudomonas denitrificans SC510 RifT, Pseudomonas denitrificans SC510 (RifT)-complete inhibition by 0.1 mM, mechanism unclear485085

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
S-adenosyl-L-homocysteinePseudomonas denitrificans-competitive485085 2D-image
S-adenosyl-L-homocysteinePseudomonas aeruginosa-product inhibition at concentrations above 0.002 mM703663 2D-image
S-adenosyl-L-homocysteinePseudomonas aeruginosaP95417-719948 2D-image
uroporphyrinogen IIIPseudomonas denitrificans-substrate inhibition above 0.002 mM485085 2D-image
uroporphyrinogen IIIPseudomonas aeruginosa-substrate inhibition at concentrations above 0.017 mM703663 2D-image
additional informationPseudomonas denitrificans-no inhibition by cobalamine or intermediates of synthesis485085-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0042-heptacarboxyporphyrinogen IIIPseudomonas denitrificans--485085-
0.0047-hexacarboxyporphyrinogen IIIPseudomonas denitrificans--485085-
0.0034-pentacarboxyporphyrinogen IIIPseudomonas denitrificans--485085-
0.0063-S-adenosyl-L-methioninePseudomonas denitrificans--485085 2D-image
0.0004-uroporphyrinogen IIIDesulfovibrio vulgaris-pH 8.0, 22°C, CobA/HemD696120 2D-image
0.001-uroporphyrinogen IIIPseudomonas denitrificans--485085 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
38-uroporphyrinogen IIIPseudomonas denitrificans, Pseudomonas denitrificans CCUG 2519, Pseudomonas denitrificans G3575, Pseudomonas denitrificans SC510 Rif, Pseudomonas denitrificans SC510 Rifr(pXL1149), Pseudomonas denitrificans SC510 RifT, Pseudomonas denitrificans SC510 (RifT)--485085 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00032-S-adenosyl-L-homocysteinePseudomonas denitrificans, Pseudomonas denitrificans CCUG 2519, Pseudomonas denitrificans G3575, Pseudomonas denitrificans SC510 Rif, Pseudomonas denitrificans SC510 Rifr(pXL1149), Pseudomonas denitrificans SC510 RifT, Pseudomonas denitrificans SC510 (RifT)--485085 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.000044-Pseudomonas aeruginosa-recombinant enzyme703663
0.003-Desulfovibrio vulgaris-purified recombinant CobA/HemD696120
0.0062-Pseudomonas denitrificans-purified enzyme485085
0.0091-Arabidopsis thalianaQ96532purified enzyme485090

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.77.8Pseudomonas denitrificans--485085
8-Desulfovibrio vulgaris-assay at696120
8-Pseudomonas aeruginosa-assay at703663

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
22-Desulfovibrio vulgaris, Desulfovibrio vulgaris G200, Desulfovibrio vulgaris Groningen, Desulfovibrio vulgaris Hildenborough, Desulfovibrio vulgaris Hildenborough ATCC 29579, Desulfovibrio vulgaris Marburg, Desulfovibrio vulgaris Miyazaki, Desulfovibrio vulgaris Miyazaki F., Desulfovibrio vulgaris Miyazaki F-assay at room temperature696120
37-Pseudomonas aeruginosa-assay at703663

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
No entries in this field

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastArabidopsis thalianaQ96532-9507485090Manually annotated by BRENDA team
solublePropionibacterium freudenreichiiQ51720--485087Manually annotated by BRENDA team
solubleThermus thermophilus---660612Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
2ybo, downloadSCOP (2ybo)CATH (2ybo)Pseudomonas aeruginosa
2ybq, downloadSCOP (2ybq)CATH (2ybq)Pseudomonas aeruginosa
1s4d, downloadSCOP (1s4d)CATH (1s4d)Pseudomonas denitrificans
1pjq, downloadSCOP (1pjq)CATH (1pjq)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
1pjs, downloadSCOP (1pjs)CATH (1pjs)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
1pjt, downloadSCOP (1pjt)CATH (1pjt)Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
1v9a, downloadSCOP (1v9a)CATH (1v9a)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
1ve2, downloadSCOP (1ve2)CATH (1ve2)Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
27000-Propionibacterium freudenreichiiQ51720SDS-PAGE485087
27610-Geobacillus stearothermophilus-calculated from DNA sequence485088
28000-Geobacillus stearothermophilus-SDS-PAGE485088
29200-Pseudomonas denitrificansP21632calculated from DNA sequence485086
29200-Pseudomonas denitrificans SC510-calculated from DNA sequence485086
30000-Pseudomonas denitrificans-SDS-PAGE485085
39900-Arabidopsis thalianaQ96532calculated from DNA sequence485090
41000-Arabidopsis thalianaQ96532SDS-PAGE485090
49930-Escherichia coli-calculated from DNA-sequence485084
50000-Geobacillus stearothermophilus-gel filtration485088
52000-Escherichia coli-SDS-PAGE485084
52000-Zea mays-gel filtration676956
56000-Pseudomonas denitrificans-gel filtration485085
60000-Pseudomonas aeruginosa-gel filtration703663
60000-Geobacillus stearothermophilus, Geobacillus stearothermophilus VQ6TA16recombinant enzyme, native PAGE and gel filtration706702
66000-Escherichia coli-gel filtration485084
67000-Arabidopsis thalianaQ96532SDS-PAGE, uncleaved fusion protein485090
79000-Zea mays-dynamic light scattering assay676956

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Desulfovibrio vulgaris-x * 55000, about, recombinant CobA/HemD, SDS-PAGE696120
?Lactobacillus reuteri-x * 51000, SDS-PAGE714579
dimerPseudomonas denitrificans-homodimer, 2 * 30000, SDS-PAGE, gel filtration485085
dimerGeobacillus stearothermophilus-homodimer, 2 * 27000, SDS-PAGE, gel filtration485088
dimerThermus thermophilus-crystallization data, 2 * 26233, calculated660612
dimerPseudomonas denitrificans-crystallization data662638
homodimerZea mays-2 * 34000, SDS-PAGE676956
homodimerPseudomonas aeruginosa-2 * 30000, SDS-PAGE703663
homodimerGeobacillus stearothermophilus, Geobacillus stearothermophilus VQ6TA162 * 30000, recombinant enzyme, SDS-PAGE706702
homodimerPseudomonas aeruginosaP95417-719948
monomerEscherichia coli-SDS-PAGE, gel filtration485084

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
sitting drop vapor diffusion method, using Tris, pH 8.0, 24% (w/v) PEG 6000 for enzyme without substrate, and 0.2 M lithium sulfate, 0.1 M Tris, pH 8.5, 1.26 M ammonium sulfate for enzyme in complex with uroporphyrinogen IIIPseudomonas aeruginosaP95417719948
enzyme topology diagrammPseudomonas denitrificans, Pseudomonas denitrificans CCUG 2519, Pseudomonas denitrificans G3575, Pseudomonas denitrificans SC510 (RifT), Pseudomonas denitrificans SC510 Rif, Pseudomonas denitrificans SC510 Rifr(pXL1149), Pseudomonas denitrificans SC510 RifT-662638
both apoform and with S-adenosyl-L-methionineThermus thermophilus-660612

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
65-Geobacillus stearothermophilus-thermostable, 17% of activity remaining after 10 min incubation485088

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
complete loss of activity when treated with Triton X-100Arabidopsis thalianaQ96532485090

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, 10 mM Tris, pH 7.7, stable for several weeksPseudomonas denitrificans, Pseudomonas denitrificans CCUG 2519, Pseudomonas denitrificans G3575, Pseudomonas denitrificans SC510 (RifT), Pseudomonas denitrificans SC510 Rif, Pseudomonas denitrificans SC510 Rifr(pXL1149), Pseudomonas denitrificans SC510 RifT-485085

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
from recombinant E. coliArabidopsis thalianaQ96532485090
recombinant CobA/HemD , HemD, and CobA from Escherichia coli strain BL21(DE3) by nickel affinity chromatographyDesulfovibrio vulgaris-696120
-Escherichia coli-485084, 485091
from recombinant E. coliGeobacillus stearothermophilus-485088
Ni2+-Sepharose column chromatographyPseudomonas aeruginosaP95417719948
recombinant His-tagged NirE from Escherichia coli by metal chelate chromatography and gel filtration to homogeneityPseudomonas aeruginosa-703663
from recombinant E. coli using His-tagSaccharomyces cerevisiae-485092
recombinant proteinThermus thermophilus-660612
by Ni–NTA columnZea mays-676956

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
in Escherichia coli CBK103, amino acids 202-457 responsible for EC 2.1.1.107 activityArabidopsis thalianaQ96532485090
DNA and amino acid sequence determination and analysis, the uroporphyrinogen III synthase is naturally fused with the methyltransferase, bypassing the need for uroporphyrinogen III decarboxylase activity, overview. Expression of cobA/hemD and isolate hemD or cobA in Escherichia coli strain BL21(DE3)Desulfovibrio vulgaris-696120
complementation experiments with cysteine autotroph strainEscherichia coli-485091
cysG containing plasmid transformed into Escherichia coli CBK103; overexpression of cysG geneEscherichia coli-485084
overexpression of cysG geneEscherichia coli-485083
gene cobA, expression in Escherichia coli strain JM109(DE3), the recombinant enzyme renders the bacteria morre resistant to potassium tellurite and potassium tellurateGeobacillus stearothermophilusQ6TA16706702
in Escherichia coli JM83 and MV1184Geobacillus stearothermophilus-485088
gene cobA, expression in Escherichia coli strain JM109(DE3), the recombinant enzyme renders the bacteria morre resistant to potassium tellurite and potassium tellurateGeobacillus stearothermophilus VQ6TA16706702
expressed in Escherichia coli BL21(DE3) cellsLactobacillus reuteri, Lactobacillus reuteri 121, Lactobacillus reuteri 21, Lactobacillus reuteri ATCC 55739, Lactobacillus reuteri ATCC PTA 6475, Lactobacillus reuteri BR11, Lactobacillus reuteri CRL 1098, Lactobacillus reuteri CRL 1100, Lactobacillus reuteri CRL 1101, Lactobacillus reuteri CRL1098, Lactobacillus reuteri L103, Lactobacillus reuteri L461, Lactobacillus reuteri MEP181R88, Lactobacillus reuteri RT-5, Lactobacillus reuteri TMW1.106-714579
overexpression of cobA gene in Escherichia coli TB1Propionibacterium freudenreichiiQ51720485087
recombinant expression of C-terminally His-tagged NirE in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH10BPseudomonas aeruginosa-703663
50 fold increase of enzyme activity when overexpressedPseudomonas denitrificans-485085
expression of 5 open reading frames, codon 1120-1959 (cobA) encodes EC 2.1.1.107 activityPseudomonas denitrificansP21632485086
expression of 5 open reading frames, codon 1120-1959 (cobA) encodes EC 2.1.1.107 activityPseudomonas denitrificans SC510-485086
EC 2.1.1.107 deficient mutants complemented with cysG from Salmonella typhimurium and Escherichia coli and cobA from Pseudomonas denitrificans, overexpression of yeast gene product in Escherichia coliSaccharomyces cerevisiae-485092
expression in Escherichia coliThermus thermophilus-660612
Escherichia coli JM109 used for cloning all recombinant plasmids and expressing the pUC18-derived plasmid, Escherichia coli strain S13009 and BL21(DE3) used for expressing the pQE-derived plasmids and the pET-derived plasmidZea mays-676956
in Escherichia coli CBK103Zea mays-485089

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D227AEscherichia coli-full activity485091
D248AEscherichia coli-no transmethylase activity485091
D303AEscherichia coli-full activity485091
G224AEscherichia coli-unable to bind S-adenosyl-L-methionine485091
K270IEscherichia coli-full activity485091
R298LEscherichia coli-unable to bind S-adenosyl-L-methionine485091
R309LEscherichia coli-no transmethylase activity485091
G12AGeobacillus stearothermophilus, Geobacillus stearothermophilus VQ6TA16site-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 methyltransferase706702
E114QPseudomonas aeruginosaP95417the mutant shows strongly reduced activity compared to the wild type enzyme719948
G189KPseudomonas aeruginosaP95417the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme719948
G189NPseudomonas aeruginosaP95417the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme719948
H161FPseudomonas aeruginosaP95417the mutant shows reduced activity compared to the wild type enzyme719948
K102APseudomonas aeruginosaP95417the mutant shows no activity and strongly reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme719948
R111KPseudomonas aeruginosaP95417the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme719948
R149KPseudomonas aeruginosaP95417the mutant shows no activity compared to the wild type enzyme719948
R51KPseudomonas aeruginosaP95417the mutant shows reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme719948
D47NPseudomonas denitrificans-binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1662638
F106APseudomonas denitrificans-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity662638
L49APseudomonas denitrificans-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-2662638
M184APseudomonas denitrificans-slight enzymic activity662638
T130APseudomonas denitrificans-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine662638
Y183APseudomonas denitrificans-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity662638
D47NPseudomonas denitrificans CCUG 2519-binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1662638
F106APseudomonas denitrificans CCUG 2519-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity662638
L49APseudomonas denitrificans CCUG 2519-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-2662638
T130APseudomonas denitrificans CCUG 2519-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine662638
Y183APseudomonas denitrificans CCUG 2519-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity662638
D47NPseudomonas denitrificans G3575-binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1662638
F106APseudomonas denitrificans G3575-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity662638
L49APseudomonas denitrificans G3575-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-2662638
T130APseudomonas denitrificans G3575-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine662638
Y183APseudomonas denitrificans G3575-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity662638
D47NPseudomonas denitrificans SC510 (RifT)-binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1662638
F106APseudomonas denitrificans SC510 (RifT)-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity662638
L49APseudomonas denitrificans SC510 (RifT)-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-2662638
T130APseudomonas denitrificans SC510 (RifT)-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine662638
Y183APseudomonas denitrificans SC510 (RifT)-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity662638
D47NPseudomonas denitrificans SC510 Rif-binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1662638
F106APseudomonas denitrificans SC510 Rif-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity662638
L49APseudomonas denitrificans SC510 Rif-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-2662638
T130APseudomonas denitrificans SC510 Rif-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine662638
Y183APseudomonas denitrificans SC510 Rif-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity662638
D47NPseudomonas denitrificans SC510 Rifr(pXL1149)-binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1662638
F106APseudomonas denitrificans SC510 Rifr(pXL1149)-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity662638
L49APseudomonas denitrificans SC510 Rifr(pXL1149)-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-2662638
T130APseudomonas denitrificans SC510 Rifr(pXL1149)-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine662638
Y183APseudomonas denitrificans SC510 Rifr(pXL1149)-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity662638
D47NPseudomonas denitrificans SC510 RifT-binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1662638
F106APseudomonas denitrificans SC510 RifT-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity662638
L49APseudomonas denitrificans SC510 RifT-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-2662638
T130APseudomonas denitrificans SC510 RifT-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine662638
additional informationDesulfovibrio vulgaris-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 proteins696120
M186LPseudomonas aeruginosaP95417the mutant shows strongly reduced activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme719948
additional informationPseudomonas aeruginosa-construction of a nirE transposon mutant, which is not complemented by native cobA encoding the SAM-dependent uroporphyrinogen III methyltransferase involved in cobalamin formation, overview703663
Y183APseudomonas denitrificans SC510 RifT-considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzyminc activity662638
additional informationZea mays-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 coli676956

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
analysisZea mays-red fluorescent compounds are associated with the recombinant mature SUMT which are identified as sirohydrochlorin and trimethylpyrrocorphin by spectroscopic analysis, slightly alter the protein secondary structure676956

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
485083Warren, 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 mechanismJ. Am. Chem. Soc.1125343-53451990Escherichia coli-
485084Warren, M.J.; Roessner, C.A.; Santander, P.J.; Scott, A.I.The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylaseBiochem. J.265725-7291990Escherichia coli PubMed
485085Blanche, F.; Debussche, L.; Thibaut, D.; Crouzet, J.; Cameron, B.Purification and characterization of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Pseudomonas denitrificansJ. Bacteriol.1714222-42311989Pseudomonas denitrificans PubMed
485086Crouzet, 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 synthaseJ. Bacteriol.1725968-59791990Pseudomonas denitrificans (P21632), Pseudomonas denitrificans PubMed
485087Sattler, 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.1771564-15691995Propionibacterium freudenreichii, Propionibacterium freudenreichii (Q51720) PubMed
485088Chou, 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 geneBiosci. Biotechnol. Biochem.591817-18241995Geobacillus stearothermophilus PubMed
485089Sakakibara, 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 reductasePlant J.10883-8921996Zea mays PubMed
485090Leustek, 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 thalianaJ. Biol. Chem.2722744-27521997Arabidopsis thaliana, Arabidopsis thaliana (Q96532) PubMed
485091Woodcock, 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 biosynthesisBiochem. J.330121-1291998Escherichia coli-
485092Raux, E.; McVeigh, T.; Peters, S.E.; Leustek, T.; Warren, M.J.The role of Saccharomyces cerevisiae MET1p and MET8p in sirohaem and cobalamin biosynthesisBiochem. J.338701-7081999Escherichia coli, Pseudomonas denitrificans, Saccharomyces cerevisiae, Salmonella enterica subsp. enterica serovar Typhimurium-
660612Rehse, P.H.; Kitao, T.; Tahirov, T.H.Structure of a closed-form uroporphyrinogen-III C-methyltransferase from Thermus thermophilusActa Crystallogr. Sect. D61913-9192005Thermus thermophilus PubMed
662638Vevodova, J.; Graham, R.M.; Raux, E.; Schubert, H.L.; Roper, D.I.; Brindley, A.A.; Ian Scott, A.; Roessner, C.A.; Stamford, N.P.; Elizabeth Stroupe, M.; Getzoff, E.D.; Warren, M.J.; Wilson, K.S.Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesisJ. Mol. Biol.344419-4332004Pseudomonas denitrificans PubMed
676956Fan, J.; Wang, D.; Liang, Z.; Guo, M.; Teng, M.; Niu, L.Maize uroporphyrinogen III methyltransferase: overexpression of the functional gene fragments in Escherichia coli and one-step purificationProtein Expr. Purif.4640-462006Zea mays PubMed
696120Lobo, S.A.; Brindley, A.; Warren, M.J.; Saraiva, L.M.Functional characterization of the early steps of tetrapyrrole biosynthesis and modification in Desulfovibrio vulgaris HildenboroughBiochem. J.420317-3252009Desulfovibrio vulgaris, Desulfovibrio vulgaris (Q72DS3) PubMed
703663Storbeck, S.; Walther, J.; Mueller, J.; Parmar, V.; Schiebel, H.M.; Kemken, D.; Duelcks, T.; Warren, M.J.; Layer, G.The Pseudomonas aeruginosa nirE gene encodes the S-adenosyl-L-methionine-dependent uroporphyrinogen III methyltransferase required for heme d1 biosynthesisFEBS J.2765973-59822009Pseudomonas aeruginosa PubMed
706702Araya, M.A.; Tantalean, J.C.; Perez, J.M.; Fuentes, D.E.; Calderon, I.L.; Saavedra, C.P.; Burra, R.; Chasteen, T.G.; Vasquez, C.C.Cloning, purification and characterization of Geobacillus stearothermophilus V uroporphyrinogen-III C-methyltransferase: evaluation of its role in resistance to potassium tellurite in Escherichia coliRes. Microbiol.160125-1332009Geobacillus stearothermophilus, Geobacillus stearothermophilus (Q6TA16), Geobacillus stearothermophilus V (Q6TA16) PubMed
714579Vannini, V.; Rodriguez, A.; Vera, J.L.; de Valdez, G.F.; Taranto, M.P.; Sesma, F.Cloning and heterologous expression of Lactobacillus reuteri uroporphyrinogen III synthase/methyltransferase gene (cobA/hemD): preliminary characterizationBiotechnol. Lett.331625-16322011Lactobacillus reuteri, Lactobacillus reuteri (Q50EH6), Lactobacillus reuteri CRL 1098, Lactobacillus reuteri CRL 1098 (Q50EH6) PubMed
719948Storbeck, S.; Saha, S.; Krausze, J.; Klink, B.U.; Heinz, D.W.; Layer, G.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 methyltransferasesJ. Biol. Chem.28626754-267672011Pseudomonas aeruginosa, Pseudomonas aeruginosa (P95417) PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.107)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)