EC number:2.1.1.80
| ID: | 2.1.1.80 |
|---|---|
| Description: | Protein-glutamate O-methyltransferase. |
| Alternative Name: |
Methyl-accepting chemotaxis protein O-methyltransferase. |
| Cath: | 1.10.10.10; 1.10.155.10; 3.30.1330.20; 3.30.1330.200; 3.40.50.150; 3.40.50.180; 3.40.50.2300; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.80 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.80 |
| KEGG Enzyme Link: | KEGG2.1.1.80 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.80 |
| ExPASy Enzyme Link: | ExPASy2.1.1.80 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.80 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.80 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.80 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.80 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.80 |
| RHEA:24452 | L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-glutamate O(5)-methyl ester + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[OH;+0:2].[*:3]-[S+;H0:4](-[*:5])-[CH3;+0:6]>>[*:1]-[O;H0;+0:2]-[CH3;+0:6].[*:3]-[S;H0;+0:4]-[*:5] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. | Djordjevic S, Stock AM | 1997 Apr 15 | 9115443 |
| Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria. | Simms SA, Stock AM, Stock JB | 1987 Jun 25 | 3298235 |
| Physiological sites of deamidation and methyl esterification in sensory transducers of Halobacterium salinarum. | Koch MK, Staudinger WF, Siedler F, Oesterhelt D | 2008 Jul 4 | 18514223 |