EC Tree |
6. Ligases |
6.3 Forming carbon-nitrogen bonds |
6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor |
ID: | 6.3.5.2 | ||
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Description: | GMP synthase (glutamine-hydrolyzing). | ||
Alternative Name: |
GMP synthetase (glutamine-hydrolyzing). | ||
Prosite: | PDOC00405; | ||
PDB: |
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Cath: | 3.30.300.10; 3.40.50.620; 3.40.50.880; |
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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 6.3.5.2 |
BRENDA Enzyme Link: | BRENDA 6.3.5.2 |
KEGG Enzyme Link: | KEGG6.3.5.2 |
BioCyc Enzyme Link: | BioCyc 6.3.5.2 |
ExPASy Enzyme Link: | ExPASy6.3.5.2 |
EC2PDB Enzyme Link: | EC2PDB 6.3.5.2 |
ExplorEnz Enzyme Link: | ExplorEnz 6.3.5.2 |
PRIAM enzyme-specific profiles Link: | PRIAM 6.3.5.2 |
IntEnz Enzyme Link: | IntEnz 6.3.5.2 |
MEDLINE Enzyme Link: | MEDLINE 6.3.5.2 |
RHEA:11680 | ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate |
RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[*:5]-[O;H0;+0:6]-[P;H0;+0:7](-[*:8])(=[*:9])-[*:10].[*:11]:[c;H0;+0:12](=[O;H0;+0:13]):[nH;+0:14]:[*:15].[OH2;+0:16]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:13].[*:5]-[OH;+0:6].[*:8]-[P;H0;+0:7](=[*:9])(-[*:10])-[OH;+0:16].[*:11]:[c;H0;+0:12](-[NH2;+0:4]):[n;H0;+0:14]:[*:15] |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
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Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase. | Zalkin H, Argos P, Narayana SV, Tiedeman AA, Smith JM | 1985 Mar 25 | 2982857 |
The effects of removing the GAT domain from E. coli GMP synthetase. | Abbott JL, Newell JM, Lightcap CM, Olanich ME, Loughlin DT, Weller MA, Lam G, Pollack S, Patton WA | 2006 Dec | 17103135 |
Biosynthesis of guanosine 5'-phosphate. II. Amination of xanthosine 5'-phosphate by purified enzyme from pigeon liver. | LAGERKVIST U | 1958 Jul | 13563458 |