EC Tree |
6. Ligases |
6.3 Forming carbon-nitrogen bonds |
6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor |
ID: | 6.3.5.3 | ||
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Description: | Phosphoribosylformylglycinamidine synthase. | ||
Alternative Name: |
Phosphoribosylformylglycinamidine synthetase. Formylglycinamide ribotide amidotransferase. FGARAT. FGAR amidotransferase. FGAM synthetase. FGAM synthase. | ||
Prosite: | PDOC00405; | ||
PDB: |
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Cath: | 1.10.8.750; 3.30.1280.10; 3.30.1330.10; 3.30.70.1670; 3.40.50.880; 3.90.650.10; |
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 6.3.5.3 |
BRENDA Enzyme Link: | BRENDA 6.3.5.3 |
KEGG Enzyme Link: | KEGG6.3.5.3 |
BioCyc Enzyme Link: | BioCyc 6.3.5.3 |
ExPASy Enzyme Link: | ExPASy6.3.5.3 |
EC2PDB Enzyme Link: | EC2PDB 6.3.5.3 |
ExplorEnz Enzyme Link: | ExplorEnz 6.3.5.3 |
PRIAM enzyme-specific profiles Link: | PRIAM 6.3.5.3 |
IntEnz Enzyme Link: | IntEnz 6.3.5.3 |
MEDLINE Enzyme Link: | MEDLINE 6.3.5.3 |
RHEA:17129 | ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide = 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate |
RULE(radius=1) | [*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[C;H0;+0:6](=[*:7])-[NH2;+0:8].[*:9]=[P;H0;+0:10](-[*:11])(-[*:12])-[O;H0;+0:13]-[*:14].[OH2;+0:15]>>[*:1]-[C;H0;+0:2](-[*:3])=[NH;+0:8].[*:5]-[C;H0;+0:6](=[*:7])-[OH;+0:4].[*:14]-[OH;+0:13].[*:9]=[P;H0;+0:10](-[*:11])(-[*:12])-[OH;+0:15] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Purification of, generation of monoclonal antibodies to, and mapping of phosphoribosyl N-formylglycinamide amidotransferase. | Barnes TS, Bleskan JH, Hart IM, Walton KA, Barton JW, Patterson D | 1994 Feb 22 | 8110788 |
Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization. | Schendel FJ, Mueller E, Stubbe J, Shiau A, Smith JM | 1989 Mar 21 | 2659070 |
Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily. | Morar M, Anand R, Hoskins AA, Stubbe J, Ealick SE | 2006 Dec 19 | 17154526 |
The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation. | Hoskins AA, Anand R, Ealick SE, Stubbe J | 2004 Aug 17 | 15301530 |
Biosynthesis of the purines. XIV. Conversion of (alpha-N-formyl) glycinamide ribotide to (alpha-N-formyl) glycinamidine ribotide; purification and requirements of the enzyme system. | MELNICK I, BUCHANAN JM | 1957 Mar | 13416226 |