ID   GUAC_ALIF1              Reviewed;         347 AA.
AC   Q5DZN1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
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}; OrderedLocusNames=VF_A0695;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000021; AAW87765.1; -; Genomic_DNA.
DR   RefSeq; WP_011263528.1; NC_006841.2.
DR   RefSeq; YP_206653.1; NC_006841.2.
DR   AlphaFoldDB; Q5DZN1; -.
DR   SMR; Q5DZN1; -.
DR   STRING; 312309.VF_A0695; -.
DR   EnsemblBacteria; AAW87765; AAW87765; VF_A0695.
DR   KEGG; vfi:VF_A0695; -.
DR   PATRIC; fig|312309.11.peg.3297; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_3_6; -.
DR   OMA; AYKEYFG; -.
DR   OrthoDB; 532857at2; -.
DR   Proteomes; UP000000537; 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; Reference proteome.
FT   CHAIN           1..347
FT                   /note="GMP reductase"
FT                   /id="PRO_1000025622"
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;  37224 MW;  F75E31C52E0F6B2F CRC64;
     MRIEQELKLG FKDVLFRPKR STLKSRSQVE LTRDFTFKHS GRQWSGTPVI AANMDSVGSF
     AMAKALSEHG VMTAVHKHYT VADWAEFIKE NDASVLKNAM VSTGTSEADF QKTKDIMALT
     DDLIFICIDI ANGYSEHLVQ YVEKVRAEFP DKVISAGNVV TGDMVEELIL AGADIVKVGI
     GPGSVCTTRV KTGVGYPQLS AIIECADAAH GLGGRIIGDG GCSCAGDVSK AFGGGADFVM
     LGGMLAGHEE SGGEVIEQDG KTFMKFYGMS SQSAMDKHSG GVAKYRAAEG KTVLLPFRGS
     VHNTISDILG GVRSTCTYVG AAKLKELTKR TTFIRVQEQE NNVFGKE