GUAC_KLEP3
ID GUAC_KLEP3 Reviewed; 347 AA.
AC B5Y1T3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=KPK_4633;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(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_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; CP000964; ACI06948.1; -; Genomic_DNA.
DR AlphaFoldDB; B5Y1T3; -.
DR SMR; B5Y1T3; -.
DR EnsemblBacteria; ACI06948; ACI06948; KPK_4633.
DR KEGG; kpe:KPK_4633; -.
DR HOGENOM; CLU_022552_5_3_6; -.
DR OMA; AYKEYFG; -.
DR OrthoDB; 532857at2; -.
DR Proteomes; UP000001734; 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_1000129859"
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; 37349 MW; BBE0EB056680C4D1 CRC64;
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LEREFTFKHS GQTWSGVPII AANMDTVGTF
SMAKALATFG ILTAVHKHYT VEEWQAFVQG ASADVLKHVM VSTGTSDADF EKTQQILSQN
PQLKFVCIDV ANGYSEHFVQ FVAKAREAWP QKTIIAGNVV TGEMCEELIL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGQIISDG GCTMPGDVAK AFGGGADFVM
LGGMLAGHEE SGGTIVEENG EKFMLFYGMS SESAMTRHVG GVAKYRAAEG KTVKLPLRGP
VDNTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNSL