ID   GUAC_LACLA              Reviewed;         329 AA.
AC   Q9CGF1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE            EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_01511};
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE            Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_01511};
GN   Name=guaC {ECO:0000255|HAMAP-Rule:MF_01511}; OrderedLocusNames=LL1145;
GN   ORFNames=L158186;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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_01511}.
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_01511};
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01511}.
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DR   EMBL; AE005176; AAK05243.1; -; Genomic_DNA.
DR   PIR; A86768; A86768.
DR   RefSeq; NP_267301.1; NC_002662.1.
DR   RefSeq; WP_010905784.1; NC_002662.1.
DR   AlphaFoldDB; Q9CGF1; -.
DR   SMR; Q9CGF1; -.
DR   STRING; 272623.L158186; -.
DR   PaxDb; Q9CGF1; -.
DR   EnsemblBacteria; AAK05243; AAK05243; L158186.
DR   KEGG; lla:L158186; -.
DR   PATRIC; fig|272623.7.peg.1224; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_9; -.
DR   OMA; AYKEYFG; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
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_01511; GMP_reduct_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005994; GuaC_type_2.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF036500; GMP_red_Firmic; 1.
DR   TIGRFAMs; TIGR01306; GMP_reduct_2; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..329
FT                   /note="GMP reductase"
FT                   /id="PRO_0000093761"
FT   ACT_SITE        178
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT   BINDING         207..230
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ   SEQUENCE   329 AA;  35837 MW;  187BDCC3564FDA17 CRC64;
     MNNLNSVFDY EDIQLIPNKC VINSRLEADT SVKLGNFTFK LPVVPANMQT IIDDKIAEML
     AKEGYFYIMH RFEAENRAAF IKKMHQQGLI ASISVGVKAD EHAFIREISA DALIPEFITI
     DIAHGHADSV IKTIQLIKRL MPQTFVIAGN VGTPEAVREL ENAGADATKV GIGPGKVCIT
     KVKTGFGTGG WQLAAVKWCA KAASKPVIAD GGIRTHGDIA KSIRMGATMV MVGSLFAAHE
     ESPGQTVERD GQLFKEYFGS ASEYQKGEHK NVEGKKILLP HKGSLKDTLK EMEEDLQSSI
     SYAGGRDLSA LTKVDYVVVK NSIWNGDAI