AC   MF_00596;
DC   Protein; auto
c?   <OC:Bacteria>
TR   HAMAP; MF_00596; -; 1; level=0
XX
Names: GMP_reduct_type1
XX
ID   GUAC
DE   RecName: Full=GMP reductase;
DE            EC=1.7.1.7;
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase;
DE            Short=Guanosine monophosphate reductase;
GN   Name=guaC;
XX
CC   -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP
CC       to IMP. It functions in the conversion of nucleobase, nucleoside and
CC       nucleotide derivatives of G to A nucleotides, and in maintaining the
CC       intracellular balance of A and G nucleotides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC         Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58349; EC=1.7.1.7;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
XX
DR   Pfam; PF00478; IMPDH; 1; trigger=no
DR   PIRSF; PIRSF000235; GMP_reductase; 1; trigger=no
DR   NCBIfam; TIGR01305; GMP_reduct_1; 1; trigger=no
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1; trigger=no
XX
KW   Oxidoreductase
KW   NADP
KW   Metal-binding
KW   Potassium
XX
GO   GO:0003920; F:GMP reductase activity
GO   GO:0006163; P:purine nucleotide metabolic process
XX
FT   From: GUAC_ECOLI (P60560)
FT   BINDING         108..131
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         216..239
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   ACT_SITE        186
FT                   /note="Thioimidate intermediate"
FT   Condition: C
FT   BINDING         181
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: G
FT   BINDING         183
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: G
XX
Size: 347-351;
Related: None;
Template: P60560;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.28 2023/06/01
//