EC Tree |
5. Isomerases |
5.4 Intramolecular transferases |
5.4.99 Transferring other groups |
ID: | 5.4.99.61 |
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Description: | Precorrin-8X methylmutase. |
Alternative Name: |
Precorrin isomerase. Hydrogenobyrinic acid-binding protein. HBA synthase. |
Cath: | 3.40.50.10230; |
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 5.4.99.61 |
BRENDA Enzyme Link: | BRENDA 5.4.99.61 |
KEGG Enzyme Link: | KEGG5.4.99.61 |
BioCyc Enzyme Link: | BioCyc 5.4.99.61 |
ExPASy Enzyme Link: | ExPASy5.4.99.61 |
EC2PDB Enzyme Link: | EC2PDB 5.4.99.61 |
ExplorEnz Enzyme Link: | ExplorEnz 5.4.99.61 |
PRIAM enzyme-specific profiles Link: | PRIAM 5.4.99.61 |
IntEnz Enzyme Link: | IntEnz 5.4.99.61 |
MEDLINE Enzyme Link: | MEDLINE 5.4.99.61 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:22512 | 3 H(+) + precorrin-8X = hydrogenobyrinate |
RULE(radius=1) | [*:1]-[C;H0;+0:2]1=[C;H0;+0:3](-[*:4])-[C;H0;+0:5]2=[N;H0;+0:6]-[C;H0;+0:7]-1(-[CH3;+0:8])-[CH2;+0:9]-[C;H0;+0:10]1=[N;H0;+0:11]-[C;H0;+0:12](=[C;H0;+0:13](-[CH3;+0:14])-[C;H0;+0:15]3=[N;H0;+0:16]-[C;H0;+0:17](-[*:18])(-[CH;+0:19]4-[*:20]=[*:21](-[*:22](-[CH2;+0:23]-[CH2;+0:24]-[*:25])-[*:26]-4-[*:27]-[C;H0;+0:28](=[O;H0;+0:29])-[OH;+0:30])-[CH;+0:31]-2-[CH3;+0:32])-[C;H0;+0:33](-[CH3;+0:34])(-[CH2;+0:35]-[*:36])-[CH;+0:37]-3-[*:38])-[*:39]-[*:40]-1.[H+;H0:41].[H+;H0:42].[H+;H0:43]>>[*:1]-[C;H0;+0:2]1(-[CH2;+0:35]-[*:36])-[C;H0;+0:7]2=[N;H0;+0:6]-[C;H0;+0:5](=[CH;+0:31]-[*:21]3=[*:20]-[C;H0;+0:19](=[C;H0;+0:17](-[*:18])-[C;H0;+0:33]4=[N;H0;+0:16]-[CH;+0:13](-[CH;+0:15](-[CH2;+0:24]-[*:25])-[C;H0;+0:37]-4(-[*:38])-[CH3;+0:34])-[C;H0;+0:12]4(-[CH3;+0:8])-[*:39]-[*:40]-[C;H0;+0:10](=[C;H0;+0:9]-2-[CH3;+0:14])-[NH;+0:11]-4)-[*:26](-[*:27]-[CH2;+0:28]-[C;H0;+0:32](=[O;H0;+0:29])-[OH;+0:30])-[*:22]-3-[CH3;+0:23])-[CH;+0:3]-1-[*:4] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans fragment carrying eight genes involved in transformation of precorrin-2 to cobyrinic acid. | Crouzet J, Cameron B, Cauchois L, Rigault S, Rouyez MC, Blanche F, Thibaut D, Debussche L | 1990 Oct | 2211521 |
The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8x as the substrate. | Thibaut D, Couder M, Famechon A, Debussche L, Cameron B, Crouzet J, Blanche F | 1992 Feb | 1732194 |
Crystal structure of precorrin-8x methyl mutase. | Shipman LW, Li D, Roessner CA, Scott AI, Sacchettini JC | 2001 Jul 3 | 11470433 |