GUAC_SHIF8
ID GUAC_SHIF8 Reviewed; 347 AA.
AC Q0T894;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=SFV_0096;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF02382.1; -; Genomic_DNA.
DR RefSeq; WP_001217322.1; NC_008258.1.
DR AlphaFoldDB; Q0T894; -.
DR SMR; Q0T894; -.
DR EnsemblBacteria; ABF02382; ABF02382; SFV_0096.
DR GeneID; 58392241; -.
DR KEGG; sfv:SFV_0096; -.
DR HOGENOM; CLU_022552_5_3_6; -.
DR OMA; AYKEYFG; -.
DR BioCyc; SFLE373384:SFV_RS00535-MON; -.
DR Proteomes; UP000000659; 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_1000025620"
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; 37353 MW; 811275F37982EB41 CRC64;
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF
SMASALASFD ILTAVHKHFS VEEWQAFINN SSADVLKHVM VSTGTSDADF EKTKQILDLN
PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM
LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVLEQE NRIFNNL