GUAC_SALCH
ID GUAC_SALCH Reviewed; 347 AA.
AC Q57TB5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_00596};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_00596};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00596};
DE Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_00596};
GN Name=guaC {ECO:0000255|HAMAP-Rule:MF_00596}; OrderedLocusNames=SCH_0140;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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_00596}.
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_00596};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00596}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00596}.
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DR EMBL; AE017220; AAX64046.1; -; Genomic_DNA.
DR RefSeq; WP_001538997.1; NC_006905.1.
DR AlphaFoldDB; Q57TB5; -.
DR SMR; Q57TB5; -.
DR EnsemblBacteria; AAX64046; AAX64046; SCH_0140.
DR KEGG; sec:SCH_0140; -.
DR HOGENOM; CLU_022552_5_3_6; -.
DR OMA; AYKEYFG; -.
DR Proteomes; UP000000538; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_00596; GMP_reduct_type1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005993; GMPR.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 1.
DR TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW Metal-binding; NADP; Oxidoreductase; Potassium.
FT CHAIN 1..347
FT /note="GMP reductase"
FT /id="PRO_1000025616"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT BINDING 108..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT BINDING 216..239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
SQ SEQUENCE 347 AA; 37149 MW; C78C9136D3B88FA8 CRC64;
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKYS GQTWSGVPII AANMDTVGTF
EMAQALAGFD ILTAVHKHYT VEEWAAFINT ASADVLKHVM VSTGTSDADF EKTVQILALN
PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEEPIL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTMPGDVAK AFGGGADFVM
LGGMLAGHEE SGGSVVEENG EKFMLFYGMS SESAMNRHVG GVAKYRAAEG KTVKLPLRGP
VGNTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNSL