ID   GUAC_BACCR              Reviewed;         328 AA.
AC   Q814I1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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=BC_5452;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016877; AAP12313.1; -; Genomic_DNA.
DR   RefSeq; NP_835112.1; NC_004722.1.
DR   AlphaFoldDB; Q814I1; -.
DR   SMR; Q814I1; -.
DR   STRING; 226900.BC_5452; -.
DR   MetOSite; Q814I1; -.
DR   EnsemblBacteria; AAP12313; AAP12313; BC_5452.
DR   KEGG; bce:BC5452; -.
DR   PATRIC; fig|226900.8.peg.5633; -.
DR   HOGENOM; CLU_022552_5_0_9; -.
DR   OMA; AYKEYFG; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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; IPR001295; Dihydroorotate_DH_CS.
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..328
FT                   /note="GMP reductase"
FT                   /id="PRO_0000093748"
FT   ACT_SITE        176
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT   BINDING         205..228
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ   SEQUENCE   328 AA;  36306 MW;  10CD18A4A129E81D CRC64;
     MMENVFDYED IQLIPAKCIV NSRSECDTTV TLGKHKFKLP VVPANMQTII DERIATYLAE
     NNYFYIMHRF QPEKRISFIR DMQSRGLIAS ISVGVKEDEY EFVQQLAAEQ LTPEYITIDI
     AHGHSNAVIN MIQHIKKHLP ESFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKI
     KTGFGTGGWQ LAALRWCAKA ASKPIIADGG IRTHGDVAKS IRFGATMVMI GSLFAGHEES
     PGETIERDGK LYKEYFGSAS EFQKGEKKNV EGKKMFVEHK GSLEDTLIEM EQDLQSSISY
     AGGTKLDAIR TVDYVVVKNS IFNGDKVY