ID   GUAC_MYCMS              Reviewed;         320 AA.
AC   Q6MUI1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=MSC_0050;
OS   Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1;
RX   PubMed=14762060; DOI=10.1101/gr.1673304;
RA   Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA   Johansson K.-E., Pettersson B., Uhlen M.;
RT   "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT   PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL   Genome Res. 14:221-227(2004).
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; BX293980; CAE76703.1; -; Genomic_DNA.
DR   RefSeq; NP_975061.1; NC_005364.2.
DR   AlphaFoldDB; Q6MUI1; -.
DR   SMR; Q6MUI1; -.
DR   STRING; 272632.MSC_0050; -.
DR   EnsemblBacteria; CAE76703; CAE76703; MSC_0050.
DR   KEGG; mmy:MSC_0050; -.
DR   PATRIC; fig|272632.4.peg.50; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_14; -.
DR   OMA; AYKEYFG; -.
DR   Proteomes; UP000001016; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:InterPro.
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; IPR001093; IMP_DH_GMPRt.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF036500; GMP_red_Firmic; 1.
DR   TIGRFAMs; TIGR01306; GMP_reduct_2; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..320
FT                   /note="GMP reductase"
FT                   /id="PRO_0000294278"
FT   ACT_SITE        174
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT   BINDING         203..226
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ   SEQUENCE   320 AA;  35962 MW;  3C96F2F3EDA24979 CRC64;
     MKIFDYDDVQ LIPEMCIVNS RKECETTATL GKHTFKLPVV PANMATIINE ELAEKLARND
     YFYIMHRFNV DQLKFIKNMK DKNLITSISL GVKPDEYKLV DQMVQQNLIP DYITIDIAHG
     HALSVKNMIS YIREKMKDQV FIIAGNVTTP KAVRDLELWG ADATKIEIGP GKVCITKLKT
     GFGTGGWQLS ALKYCAKTAS KPIIADGGLR VHGDIAKSIR MGASFCMIVS LFAAHLESPG
     KEVEINNCIY KEYYGSASEY NKSEKRYVEG KKELIKIRGS IFDTLKEMTE DLQSSISYAG
     GKDLQAIKRV DYVLLGDYKD