DB code: M00037

CATH domain 3.40.50.20 : Rossmann fold
3.30.1490.20 : Dna Ligase; domain 1
3.30.470.20 : D-amino Acid Aminotransferase; Chain A, domain 1
3.90.600.10 : Glycinamide Ribonucleotide Synthetase; Chain A, domain 4
E.C. 6.3.4.13
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.30.1490.20 : Dna Ligase; domain 1 T00082 M00035 T00107 T00108
3.30.470.20 : D-amino Acid Aminotransferase; Chain A, domain 1 T00082 D00298 M00035 M00051 T00107 T00108
3.40.50.20 : Rossmann fold T00082 T00107 T00108

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P15640 Phosphoribosylamine--glycine ligase
EC 6.3.4.13
GARS
Glycinamide ribonucleotide synthetase
Phosphoribosylglycinamide synthetase
NP_418433.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_491455.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01071 (GARS_A)
PF02843 (GARS_C)
PF02844 (GARS_N)
[Graphical View]

KEGG enzyme name
phosphoribosylamine---glycine ligase
phosphoribosylglycinamide synthetase
glycinamide ribonucleotide synthetase
phosphoribosylglycineamide synthetase
glycineamide ribonucleotide synthetase
2-amino-N-ribosylacetamide 5'-phosphate kinosynthase
5'-phosphoribosylglycinamide synthetase
GAR

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P15640 PUR2_ECOLI ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. Monomer. Binds 1 magnesium or manganese ion per subunit (By similarity).

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C03090 C00037 C00008 C00009 C03838
E.C.
Compound Magnesium ATP 5-Phospho-D-ribosylamine Glycine ADP Orthophosphate N1-(5-Phospho-D-ribosyl)glycinamide
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amine group,carbohydrate,phosphate group/phosphate ion amino acids amine group,nucleotide phosphate group/phosphate ion amide group,amine group,carbohydrate,phosphate group/phosphate ion
ChEBI 18420
 18420
 		15422
 15422
 		37737
 37737
 		15428
 57305
 15428
 57305
 		16761
 16761
 		26078
 26078
PubChem 888
 888
 		5957
 5957
 		439905
 439905
 		5257127
 750
 5257127
 750
 		6022
 6022
 		1004
 22486802
 1004
 22486802
 		160913
 160913
1gsoA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gsoA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gsoA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gsoA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1gsoA01
1gsoA02
1gsoA03
1gsoA04

References for Catalytic Mechanism
References Sections No. of steps in catalysis

References
[1]
Resource
Comments
Medline ID
PubMed ID 3756144
Journal Biochemistry
Year 1986
Volume 25
Pages 4356-65
Authors Schrimsher JL, Schendel FJ, Stubbe J
Title Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8299947
Journal Gene
Year 1993
Volume 137
Pages 195-202
Authors Kan JL, Jannatipour M, Taylor SM, Moran RG
Title Mouse cDNAs encoding a trifunctional protein of de novo purine synthesis and a related single-domain glycinamide ribonucleotide synthetase.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)
Medline ID 99060041
PubMed ID 9843369
Journal Biochemistry
Year 1998
Volume 37
Pages 15647-62
Authors Wang W, Kappock TJ, Stubbe J, Ealick SE
Title X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli.
Related PDB 1gso
Related UniProtKB P15640
[4]
Resource
Comments
Medline ID
PubMed ID 10089364
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 518-21
Authors Weaver TM, Wang W, Ealick SE
Title Purification, crystallization and preliminary X-ray diffraction data from selenomethionine glycinamide ribonucleotide synthetase.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-03-25 2009-02-26