ID   GUAC_ALIFM              Reviewed;         347 AA.
AC   B5EUG3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_00596};
DE            EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_00596};
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00596};
DE            Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_00596};
GN   Name=guaC {ECO:0000255|HAMAP-Rule:MF_00596};
GN   OrderedLocusNames=VFMJ11_A0782;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00596}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00596};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00596}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00596}.
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DR   EMBL; CP001133; ACH64018.1; -; Genomic_DNA.
DR   RefSeq; WP_012535163.1; NC_011186.1.
DR   AlphaFoldDB; B5EUG3; -.
DR   SMR; B5EUG3; -.
DR   EnsemblBacteria; ACH64018; ACH64018; VFMJ11_A0782.
DR   KEGG; vfm:VFMJ11_A0782; -.
DR   HOGENOM; CLU_022552_5_3_6; -.
DR   OMA; AYKEYFG; -.
DR   Proteomes; UP000001857; Chromosome II.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00596; GMP_reduct_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005993; GMPR.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000235; GMP_reductase; 1.
DR   TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   Metal-binding; NADP; Oxidoreductase; Potassium.
FT   CHAIN           1..347
FT                   /note="GMP reductase"
FT                   /id="PRO_1000129869"
FT   ACT_SITE        186
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   BINDING         108..131
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   BINDING         181
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   BINDING         183
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   BINDING         216..239
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
SQ   SEQUENCE   347 AA;  37250 MW;  1AEC6C322CAD9DC9 CRC64;
     MRIEQELKLG FKDVLFRPKR STLKSRSQVE LTRNFTFKHS GRQWSGTPVI AANMDSVGSF
     AMAKALSEHG VMTAVHKHYT VADWAEFIKE NDASVLKNAM VSTGTSEADF QKTKDIMALT
     DDLIFICIDI ANGYSEHLVQ YVEKVRAEFP DKVISAGNVV TGDMVEELIL AGADIVKVGI
     GPGSVCTTRV KTGVGYPQLS AIIECADAAH GLGGRIIGDG GCSCAGDVSK AFGGGADFVM
     LGGMLAGHEE SGGEVIEQDG KQFMKFYGMS SQSAMDKHSG GVAKYRAAEG KTVLLPFRGS
     VHNTISDILG GVRSTCTYVG AAQLKELTKR TTFIRVQEQE NNVFGKE