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Information on EC 2.1.1.107 - uroporphyrinogen-III C-methyltransferase and Organism(s) Methanobacterium ivanovii and UniProt Accession P29564

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.107 uroporphyrinogen-III C-methyltransferase
IUBMB Comments
This 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.
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Methanobacterium ivanovii
UNIPROT: P29564
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Word Map
The taxonomic range for the selected organisms is: Methanobacterium ivanovii
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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Synonyms
uroporphyrinogen iii methyltransferase, s-adenosyl-l-methionine:uroporphyrinogen iii methyltransferase, uroporphyrinogen iii methylase, s-adenosyl-l-methionine uroporphyrinogen iii methyltransferase, sam-dependent uroporphyrinogen iii methyltransferase, uroporphyrinogen-iii c-methyltransferase, sirohaem synthase, uroporphyrinogen iii synthase/methyltransferase, s-adenosyl-l-methionine-dependent uroporphyrinogen iii methyltransferase, uroporphyrinogen iii c-methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase
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adenosylmethionine-uroporphyrinogen III methyltransferase
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S-adenosyl-L-methionine dependent uroporphyrinogen III methylase
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sirohaem synthase
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uroporphyrinogen III C-methyltransferase
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uroporphyrinogen III methylase
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uroporphyrinogen methyltransferase,
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:uroporphyrinogen-III C-methyltransferase
This 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.
CAS REGISTRY NUMBER
COMMENTARY hide
73665-99-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + uroporphyrinogen III
2 S-adenosyl-L-homocysteine + precorrin-2
show the reaction diagram
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.052
uroporphyrinogen III
pH 7.7, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUMT_METIV
231
0
24916
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
2 * 29000, SDS-PAGE
58200
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 29000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Pseudomonas denitrificans
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Blanche, F.; Robin, C.; Couder, M.; Faucher, D.; Cauchois, L.; Cameron, B.; Crouzet, J.
Purification, characterization, and molecular cloning of S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase from Methanobacterium ivanovii
J. Bacteriol.
173
4637-4645
1991
Methanobacterium ivanovii (P29564), Methanobacterium ivanovii
Manually annotated by BRENDA team