AC   MF_03195;
DC   Protein; auto
c?   <OC:Eukaryota>
TR   HAMAP; MF_00596; -; 1; level=0
XX
Names: GMP_reduct_type1_euk
XX
ID   GMPR
DE   RecName: Full=GMP reductase;
DE            Short=GMPR;
DE            EC=1.7.1.7;
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase;
DE            Short=Guanosine monophosphate reductase;
case <OC:Vertebrata> or <OC:Kinetoplastea>
GN   Name=GMPR;
end case
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.
case <OC:Kinetoplastea> and <FTTag:Microbody>
CC   -!- SUBCELLULAR LOCATION: Glycosome.
end case
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
XX
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1; trigger=no
DR   PROSITE; PS51371; CBS; 0-2; trigger=yes
DR   Pfam; PF00478; IMPDH; 1; trigger=no
DR   Pfam; PF00571; CBS; 0-2; trigger=no
DR   NCBIfam; TIGR01305; GMP_reduct_1; 1; trigger=no
DR   PIRSF; PIRSF000235; GMP_reductase; 1; trigger=no
XX
KW   Metal-binding
KW   NADP
KW   Oxidoreductase
KW   Potassium
KW   Purine metabolism
case <OC:Kinetoplastea> and <FTTag:Microbody>
KW   Glycosome
KW   Peroxisome
end case
XX
GO   GO:0003920; F:GMP reductase activity
GO   GO:0006163; P:purine nucleotide metabolic process
XX
FT   From: GMPR2_HUMAN (Q9P2T1)
FT   BINDING         26..27
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT   Condition: S-R
FT   BINDING         129..131
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT   Condition: D-[IV]-A
FT   BINDING         180..181
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT   Condition: [IV]-G
FT   BINDING         285..286
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT   Condition: Y-R
FT   BINDING         314..317
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT   Condition: S-[ATG]-[CI]-[TS]
FT   BINDING         219..221
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: D-G-G
FT   BINDING         242..243
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: G-[GN]
FT   BINDING         268..270
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: G-M-[AS]
FT   BINDING         286..290
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT   Condition: [RL]-[AV]-[SAP]-E-G
FT   ACT_SITE        186
FT                   /note="Thioimidate intermediate"
FT   Condition: C
FT   ACT_SITE        188
FT                   /note="Proton donor/acceptor"
FT   Condition: T
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
FT   BINDING         186
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: C
FT   BINDING         189
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT   Condition: R
FT   BINDING         78
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT   Condition: [KR]
FT   BINDING         269
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /note="in other chain"
FT   Condition: M
FT   From: GMPR_LEIMA (Q4QEB3)
case <OC:Kinetoplastea>
FT   MOTIF           490..Cter
FT                   /note="Microbody targeting signal"
FT   Tag: Microbody; Condition: [AS]-K-[ML]
end case
XX
Size: 339-553;
Related: None;
Template: Q9P2T1; P36959; Q4QEB3;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.11 2023/06/01
//