Enzyme

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     5. Isomerases
        5.4 Intramolecular transferases
            5.4.99 Transferring other groups
ID:5.4.99.18
Description:5-(carboxyamino)imidazole ribonucleotide mutase.
Alternative Name: N(5)-carboxyaminoimidazole ribonucleotide mutase.
N(5)-CAIR mutase.
Cath: 3.30.1490.20; 3.30.470.20; 3.40.50.7700; 3.40.50.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 5.4.99.18
BRENDA Enzyme Link: BRENDA 5.4.99.18
KEGG Enzyme Link: KEGG5.4.99.18
BioCyc Enzyme Link: BioCyc 5.4.99.18
ExPASy Enzyme Link: ExPASy5.4.99.18
EC2PDB Enzyme Link: EC2PDB 5.4.99.18
ExplorEnz Enzyme Link: ExplorEnz 5.4.99.18
PRIAM enzyme-specific profiles Link: PRIAM 5.4.99.18
IntEnz Enzyme Link: IntEnz 5.4.99.18
MEDLINE Enzyme Link: MEDLINE 5.4.99.18
MSA:

5.4.99.18;

Phylogenetic Tree:

5.4.99.18;

Uniprot:
M-CSA:
RHEA:13193 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[NH;+0:4]-[*:5]:[cH;+0:6]:[*:7].[H+;H0:8]>>[*:1]=[C;H0;+0:2](-[*:3])-[c;H0;+0:6](:[*:7]):[*:5]-[NH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway.Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM1992 Jun 21534690
Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway.Mathews II, Kappock TJ, Stubbe J, Ealick SE1999 Nov 1510574791
Evidence for the direct transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase.Meyer E, Kappock TJ, Osuji C, Stubbe J1999 Mar 910074353