ID   GUAC_POLSJ              Reviewed;         325 AA.
AC   Q12CT8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=Bpro_1718;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(2008).
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; CP000316; ABE43654.1; -; Genomic_DNA.
DR   RefSeq; WP_011482653.1; NC_007948.1.
DR   AlphaFoldDB; Q12CT8; -.
DR   SMR; Q12CT8; -.
DR   STRING; 296591.Bpro_1718; -.
DR   EnsemblBacteria; ABE43654; ABE43654; Bpro_1718.
DR   KEGG; pol:Bpro_1718; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_4; -.
DR   OMA; AYKEYFG; -.
DR   OrthoDB; 532857at2; -.
DR   Proteomes; UP000001983; 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..325
FT                   /note="GMP reductase"
FT                   /id="PRO_0000294282"
FT   ACT_SITE        173
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT   BINDING         202..225
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ   SEQUENCE   325 AA;  35566 MW;  030A46B033E60830 CRC64;
     MEIFDYENVL LLPRKCRVES RSECNAGVAL GGRTFRIPVV PANMKTVVDE NICAWMAKNG
     YFYVMHRFDL DNLQFVKNMK AKGVYASISL GVKKPDYDTV DQFVAEGLAP EYITIDIAHG
     HADTVQRMIA YLKQKLPASF VIAGNVATPE AVIDLENWGA DATKVGIGPG KVCITKMKTG
     FGTGGWQLSA LKWCARVATK PIIADGGIRE HGDIAKSIRF GATMVMIGSL LAGLEESPGK
     TVEVDGKLFK EYYGSASDFN KGEYKHVEGK RILEPIKGTL ADTLREMEED IQSSISYAGG
     KKLMDIRKAN YVILGGDNAG EHLLM