ID   GUAC_LACAC              Reviewed;         330 AA.
AC   Q5FHY3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=LBA1893;
OS   Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=272621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX   PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA   Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA   McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA   Hamrick A., Cano R., Klaenhammer T.R.;
RT   "Complete genome sequence of the probiotic lactic acid bacterium
RT   Lactobacillus acidophilus NCFM.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(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_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; CP000033; AAV43691.1; -; Genomic_DNA.
DR   RefSeq; WP_011254608.1; NC_006814.3.
DR   RefSeq; YP_194722.1; NC_006814.3.
DR   AlphaFoldDB; Q5FHY3; -.
DR   SMR; Q5FHY3; -.
DR   STRING; 272621.LBA1893; -.
DR   PRIDE; Q5FHY3; -.
DR   EnsemblBacteria; AAV43691; AAV43691; LBA1893.
DR   GeneID; 56943440; -.
DR   KEGG; lac:LBA1893; -.
DR   PATRIC; fig|272621.13.peg.1799; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_9; -.
DR   OMA; AYKEYFG; -.
DR   BioCyc; LACI272621:G1G49-1845-MON; -.
DR   Proteomes; UP000006381; 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..330
FT                   /note="GMP reductase"
FT                   /id="PRO_0000093758"
FT   ACT_SITE        180
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT   BINDING         209..232
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ   SEQUENCE   330 AA;  36657 MW;  3E8A176D3B43A018 CRC64;
     MSNYFSMEAF DYDDIQLIPN KGIIKSRRDA DTSVKFGNRT FKIPVVPANM ESVIDDKLAV
     WLAENDYYYV MHRFEPEKRI PFIKMMHEKG LFASISVGIK DSEYDFIDEL VKQNLKPEYI
     TIDVAHGHSV YVIKMIKYIK EKLPNSFLTA GNIATPEAVR ELENAGADAT KVGVGPGKAC
     ITKLKTGFGT GGWQLAALRM CSKVASKPLI ADGGIRHNGD IAKSVRFGAS MVMIGSMLAG
     HEESPGNVIK IDGKTFKQYW GSASEVQKGA YKNVEGKQML VPYRGSIKDT LREMQEDLQS
     AISYAGGREL NSIKLVDYVI VKDNIFDGDK