Enzyme

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     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
Description:GMP synthase (glutamine-hydrolyzing).
Alternative Name: GMP synthetase (glutamine-hydrolyzing).
Prosite: PDOC00405;
PDB:
PDBScop
Cath: 3.30.300.10; 3.40.50.620; 3.40.50.880;

3D structure

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References

External Links

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
MSA:

6.3.5.2;

Phylogenetic Tree:

6.3.5.2;

Uniprot:
M-CSA:
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
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References

TitleAuthorsDatePubMed ID
Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.Zalkin H, Argos P, Narayana SV, Tiedeman AA, Smith JM1985 Mar 252982857
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 WA2006 Dec17103135
Biosynthesis of guanosine 5'-phosphate. II. Amination of xanthosine 5'-phosphate by purified enzyme from pigeon liver.LAGERKVIST U1958 Jul13563458