AC   MF_01931;
DC   Protein; auto
TR   HAMAP; MF_01931; -; 1; level=0
XX
Names: PurF
XX
ID   PUR1
DE   RecName: Full=Amidophosphoribosyltransferase;
DE            Short=ATase;
DE            EC=2.4.2.14;
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase;
DE            Short=GPATase;
GN   Name=purF;
XX
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC         Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58681; EC=2.4.2.14;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
end case
case <FTGroup:2>
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
end case
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 1/2.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family.
XX
DR   PROSITE; PS51278; GATASE_TYPE_2; 1; trigger=yes
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1; trigger=no
DR   Pfam; PF00310; GATase_2; 0-1; trigger=no
DR   Pfam; PF00156; Pribosyltran; 1; trigger=no
DR   Pfam; PF13537; GATase_7; 0-1; trigger=no
DR   NCBIfam; TIGR01134; purF; 1; trigger=no
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1; trigger=no
XX
KW   Glutamine amidotransferase
KW   Glycosyltransferase
KW   Purine biosynthesis
KW   Transferase
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
case <FTGroup:2>
KW   4Fe-4S
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
end case
XX
GO   GO:0004044; F:amidophosphoribosyltransferase activity
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
case <FTGroup:2>
GO   GO:0051536; F:iron-sulfur cluster binding
end case
GO   GO:0006189; P:'de novo' IMP biosynthetic process
XX
FT   From: PUR1_BACSU (P00497)
FT   ACT_SITE        12
FT                   /note="Nucleophile"
FT   Condition: C
FT   BINDING         247
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Optional; Group: 2; Condition: C
FT   BINDING         294
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: [ST]
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         393
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Optional; Group: 2; Condition: C
FT   BINDING         448
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Optional; Group: 2; Condition: C
FT   BINDING         451
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Optional; Group: 2; Condition: C
XX
Size: 430-600;
Related: None;
Template: P0AG16; P00497;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: The N-terminus is cleaved. The mature enzyme starts with cysteine (active site).
XX
# Revision 1.8 2023/06/01
//