DB code: T00082

CATH domain 3.40.50.20 : Rossmann fold
3.30.470.20 : D-amino Acid Aminotransferase; Chain A, domain 1 Catalytic domain
3.30.1490.20 : Dna Ligase; domain 1
E.C. 4.1.1.21
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.30.1490.20 : Dna Ligase; domain 1 M00035 M00037 T00107 T00108
3.30.470.20 : D-amino Acid Aminotransferase; Chain A, domain 1 D00298 M00035 M00037 M00051 T00107 T00108
3.40.50.20 : Rossmann fold M00037 T00107 T00108

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P09029 N5-carboxyaminoimidazole ribonucleotide synthase
N5-CAIR synthase
EC 6.3.4.18
5-(carboxyamino)imidazole ribonucleotide synthetase
NP_415055.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488811.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF02222 (ATP-grasp)
[Graphical View]

KEGG enzyme name
phosphoribosylaminoimidazole carboxylase
5-phosphoribosyl-5-aminoimidazole carboxylase
5-amino-1-ribosylimidazole 5-phosphate carboxylase
AIR carboxylase
1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase
ADE2
class II PurE
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate carboxy-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P09029 PURK_ECOLI 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO(2). Homodimer.

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

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C03373 C00011 C00002 C00001 L00008 C00008 C00009
E.C.
Compound Magnesium 1-(5-Phospho-D-ribosyl)-5-aminoimidazole CO2 ATP H2O 1-(5-Phospho-D-ribosyl)-5-carboxyamino-imidazole ADP Orthophosphate
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide others amine group,nucleotide H2O amide group,carboxyl group,nucleotide amine group,nucleotide phosphate group/phosphate ion
ChEBI 18420
 18420
 		16526
 16526
 		15422
 15422
 		15377
 15377
 		48000
 48000
 		16761
 16761
 		26078
 26078
PubChem 888
 888
 		161500
 161500
 		280
 280
 		5957
 5957
 		22247451
 962
 22247451
 962
 		23657851
 23657851
 		6022
 6022
 		1004
 22486802
 1004
 22486802
1b6rA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6rA02 Unbound Unbound Unbound Unbound Unbound Unbound Analogue:SO4
1b6sA02 Bound:_MG Unbound Unbound Unbound Unbound Bound:ADP Unbound
1b6sB02 Bound:_MG Unbound Unbound Unbound Unbound Bound:ADP Unbound
1b6sC02 Bound:_MG Unbound Unbound Unbound Unbound Bound:ADP Unbound
1b6sD02 Bound:_MG Unbound Unbound Unbound Unbound Bound:ADP Unbound
1b6rA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sB03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sC03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b6sD03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1b6s

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b6rA01
1b6sA01
1b6sB01
1b6sC01
1b6sD01
1b6rA02 GLU 226;GLU 238(magnesium binding)
1b6sA02 GLU 226;GLU 238(magnesium binding)
1b6sB02 GLU 226;GLU 238(magnesium binding)
1b6sC02 GLU 226;GLU 238(magnesium binding)
1b6sD02 GLU 226;GLU 238(magnesium binding)
1b6rA03
1b6sA03
1b6sB03
1b6sC03
1b6sD03

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.15489, p.15491

References
[1]
Resource
Comments CHARACTERIZATION, AND SEQUENCE OF 1-20.
Medline ID 92287929
PubMed ID 1534690
Journal Biochemistry
Year 1992
Volume 31
Pages 5022-32
Authors Meyer E, Leonard NJ, Bhat B, Stubbe J, Smith JM
Title Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway.
Related PDB
Related UniProtKB P09029
[2]
Resource
Comments
Medline ID
PubMed ID 7918411
Journal Biochemistry
Year 1994
Volume 33
Pages 11927-34
Authors Firestine SM, Poon SW, Mueller EJ, Stubbe J, Davisson VJ
Title Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10074353
Journal Biochemistry
Year 1999
Volume 38
Pages 3012-8
Authors Meyer E, Kappock TJ, Osuji C, Stubbe J
Title 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.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
Medline ID 20039871
PubMed ID 10569930
Journal Biochemistry
Year 1999
Volume 38
Pages 15480-92
Authors Thoden JB, Kappock TJ, Stubbe J, Holden HM
Title Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily.
Related PDB 1b6r 1b6s
Related UniProtKB P09029

Comments

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