ID   GUAC_VEREI              Reviewed;         322 AA.
AC   A1WIJ3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=Veis_1695;
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-2.";
RL   Submitted (DEC-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; CP000542; ABM57450.1; -; Genomic_DNA.
DR   RefSeq; WP_011809457.1; NC_008786.1.
DR   AlphaFoldDB; A1WIJ3; -.
DR   SMR; A1WIJ3; -.
DR   STRING; 391735.Veis_1695; -.
DR   GeneID; 76460303; -.
DR   KEGG; vei:Veis_1695; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_5_0_4; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000000374; 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; Aldolase class I; 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   NCBIfam; TIGR01306; GMP_reduct_2; 1.
DR   PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR   PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF036500; GMP_red_Firmic; 1.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..322
FT                   /note="GMP reductase"
FT                   /id="PRO_0000294290"
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   322 AA;  35629 MW;  C41A91E7CDEC6D03 CRC64;
     MEIFDYDNVL LLPRKCRVRS RSECDTSVRL GERSFRIPVV PANMKTVVDE KICAWMAQNG
     YFYVMHRFDL DNVRFVRDMQ ARGCYASISL GVQPPDHDTV EQLAAQRITP EYITIDIAHG
     HADSVQEMIN RIKTRLPRAF VIAGNVATPE AVIDLENWGA DATKVGVGPG KVCITRLKTG
     FGTGGWQLSA LKWCARVATR PIIADGGIRS HGDIAKSIRF GASMVMVGAL LAGHEESPGQ
     TVEEGSERFK EYYGSASPFN KGEYKHVEGR RILEPIKGPL AHTLVEMEQD LQSSISYAGG
     KKLMDIRKVN YVILGGDNAV LM
//