ID   GUAC_ALBFT              Reviewed;         325 AA.
AC   Q21U05;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=Rfer_3037;
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD70748.1; -; Genomic_DNA.
DR   RefSeq; WP_011465314.1; NC_007908.1.
DR   AlphaFoldDB; Q21U05; -.
DR   SMR; Q21U05; -.
DR   STRING; 338969.Rfer_3037; -.
DR   EnsemblBacteria; ABD70748; ABD70748; Rfer_3037.
DR   KEGG; rfr:Rfer_3037; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_4; -.
DR   OMA; AYKEYFG; -.
DR   OrthoDB; 532857at2; -.
DR   Proteomes; UP000008332; 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_0000294283"
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;  35813 MW;  0DBB4DB4564FB50D CRC64;
     MEIFDYDNIL LLPRKCRVES RSECDASVEL GRQRFRIPVV PANMKTVVDE SICVWLAQNS
     YFYVMHRFDL DNVQFVKNMK ARGLYASISL GVKKPDYDTV DQLLALGLVP DYITIDIAHG
     HADSVKNMIG YLKEKMPTVF IIAGNVATPE AVIDLENWGA DATKVGIGPG KVCITKLKTG
     FGTGGWQLSA VKWCARVATK PIIADGGIHE HGDIAKSIRF GATMVMIGSM LAGHEESPGK
     SVEVDGKLYK EYYGSASDFN KGEYKHVEGK RILEPVKGKL ADTLIEMEQD VQSSISYSGG
     KRLMDIRKVN YVTLGGDNAG EHLLM