Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.1 Methyltransferases
ID:2.1.1.179
Description:16S rRNA (guanine(1405)-N(7))-methyltransferase.
Alternative Name: Sisomicin-gentamicin methyltransferase.
Cath: 1.10.8.10; 3.40.50.150;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.1.179
BRENDA Enzyme Link: BRENDA 2.1.1.179
KEGG Enzyme Link: KEGG2.1.1.179
BioCyc Enzyme Link: BioCyc 2.1.1.179
ExPASy Enzyme Link: ExPASy2.1.1.179
EC2PDB Enzyme Link: EC2PDB 2.1.1.179
ExplorEnz Enzyme Link: ExplorEnz 2.1.1.179
PRIAM enzyme-specific profiles Link: PRIAM 2.1.1.179
IntEnz Enzyme Link: IntEnz 2.1.1.179
MEDLINE Enzyme Link: MEDLINE 2.1.1.179
MSA:

2.1.1.179;

Phylogenetic Tree:

2.1.1.179;

Uniprot:
M-CSA:
RHEA:42772 guanosine(1405) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(1405) in 16S rRNA + S-adenosyl-L-homocysteine
RULE(radius=1) [*:1]-[S+;H0:2](-[*:3])-[CH3;+0:4].[*:5]:[n;H0;+0:6]:[*:7]>>[*:1]-[S;H0;+0:2]-[*:3].[*:5]:[n+;H0:6](:[*:7])-[CH3;+0:4]
Reaction
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References

TitleAuthorsDatePubMed ID
Structural basis for the methylation of G1405 in 16S rRNA by aminoglycoside resistance methyltransferase Sgm from an antibiotic producer: a diversity of active sites in m7G methyltransferases.Husain N, Tkaczuk KL, Tulsidas SR, Kaminska KH, Cubrilo S, Maravić-Vlahovicek G, Bujnicki JM, Sivaraman J2010 Jul20194115
Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm.Savic M, Ilic-Tomic T, Macmaster R, Vasiljevic B, Conn GL2008 Sep18586937