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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 2.1.1.107 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.107 |
| KEGG Enzyme Link: | KEGG2.1.1.107 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.107 |
| ExPASy Enzyme Link: | ExPASy2.1.1.107 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.107 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.107 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.107 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.107 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.107 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:32459 | 2 S-adenosyl-L-methionine + uroporphyrinogen III = H(+) + precorrin-2 + 2 S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]-[S+;H0:6](-[*:7])-[CH3;+0:8].[*:9]-[c;H0;+0:10]1:[c;H0;+0:11](-[*:12]):[c;H0;+0:13](-[CH2;+0:14]-[*:15]):[nH;+0:16]:[c;H0;+0:17]:1-[CH2;+0:18]-[c;H0;+0:19]1:[nH;+0:20]:[c;H0;+0:21](-[CH2;+0:22]-[*:23]):[c;H0;+0:24](-[*:25]):[c;H0;+0:26]:1-[*:27]>>[*:9]-[CH;+0:10]1-[C;H0;+0:17](-[CH;+0:18]=[C;H0;+0:19]2-[NH;+0:20]-[C;H0;+0:21](=[CH;+0:22]-[*:23])-[CH;+0:24](-[*:25])-[C;H0;+0:26]-2(-[*:27])-[CH3;+0:4])=[N;H0;+0:16]-[C;H0;+0:13](=[CH;+0:14]-[*:15])-[C;H0;+0:11]-1(-[*:12])-[CH3;+0:8].[*:1]-[S;H0;+0:2]-[*:3].[*:5]-[S;H0;+0:6]-[*:7] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The Escherichia coli cysG gene encodes S-adenosylmethionine-dependent uroporphyrinogen III methylase. | Warren MJ, Roessner CA, Santander PJ, Scott AI | 1990 Feb 1 | 2407234 |
| The structure of Saccharomyces cerevisiae Met8p, a bifunctional dehydrogenase and ferrochelatase. | Schubert HL, Raux E, Brindley AA, Leech HK, Wilson KS, Hill CP, Warren MJ | 2002 May 1 | 11980703 |