| ID: | 2.1.1.271 |
|---|---|
| Description: | Cobalt-precorrin-4 methyltransferase. |
| Cath: | 3.30.950.10; 3.40.1010.10; |
Click one PDB to see exact 3D structure provided by NGL.
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 2.1.1.271 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.271 |
| KEGG Enzyme Link: | KEGG2.1.1.271 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.271 |
| ExPASy Enzyme Link: | ExPASy2.1.1.271 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.271 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.271 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.271 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.271 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.271 |
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:26277 | Co-precorrin-4 + S-adenosyl-L-methionine = Co-precorrin-5A + H(+) + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[CH2;+0:2]-[c;H0;+0:3]1:[c;H0;+0:4](-[*:5]):[c;H0;+0:6](-[*:7]):[c;H0;+0:8]2:[n;H0;+0:9]:1-[*:10]-[*:11]-[C;H0;+0:12](-[CH;+0:13](-[*:14])-[*:15])=[CH;+0:16]-2.[*:17]-[S+;H0:18](-[*:19])-[CH3;+0:20]>>[*:1]-[CH;+0:2]=[C;H0;+0:3]1-[C;H0;+0:4](-[*:5])=[C;H0;+0:6](-[*:7])-[C;H0;+0:8]2(-[CH3;+0:20])-[CH2;+0:16]-[C;H0;+0:12](=[C;H0;+0:13](-[*:14])-[*:15])-[*:11]-[*:10]-[N;H0;+0:9]-1-2.[*:17]-[S;H0;+0:18]-[*:19] |
| Reaction | ![]() |
| Core-to-Core |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The X-ray structure of a cobalamin biosynthetic enzyme, cobalt-precorrin-4 methyltransferase. | Schubert HL, Wilson KS, Raux E, Woodcock SC, Warren MJ | 1998 Jul | 9665173 |
| Genetically engineered synthesis and structural characterization of cobalt-precorrin 5A and -5B, two new intermediates on the anaerobic pathway to vitamin B12: definition of the roles of the CbiF and CbiG enzymes. | Kajiwara Y, Santander PJ, Roessner CA, Pérez LM, Scott AI | 2006 Aug 2 | 16866557 |