ID GUAC_YERPA Reviewed; 347 AA.
AC Q1C3T0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=YPA_2930;
OS Yersinia pestis bv. Antiqua (strain Antiqua).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=360102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Antiqua;
RX PubMed=16740952; DOI=10.1128/jb.00124-06;
RA Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA Worsham P., Chu M.C., Andersen G.L.;
RT "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT evidence of gene reduction in an emerging pathogen.";
RL J. Bacteriol. 188:4453-4463(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; CP000308; ABG14892.1; -; Genomic_DNA.
DR RefSeq; WP_002209320.1; NZ_CP009906.1.
DR AlphaFoldDB; Q1C3T0; -.
DR SMR; Q1C3T0; -.
DR GeneID; 66842876; -.
DR KEGG; ypa:YPA_2930; -.
DR Proteomes; UP000001971; 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; Aldolase class I; 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 NCBIfam; TIGR01305; GMP_reduct_1; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 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 Metal-binding; NADP; Oxidoreductase; Potassium.
FT CHAIN 1..347
FT /note="GMP reductase"
FT /id="PRO_1000025625"
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; 37492 MW; 4BF8680985AB19DF CRC64;
MRIEEGLKLG FKDVLIRPKR STLKSRSEVA LERQFTFKHS GWNWSGVPII AANMDTVGTF
RMAEVLASFD ILTAVHKHYT LEQWAEFVKR SPESVLRHVM VSTGTSSADF DKMKQILALS
PSLKFICIDV ANGYSEHFVS FLQRAREACP DKVICAGNVV TGEMVEELIL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGQIVSDG GCSVPGDVAK AFGGGADFVM
LGGMLAGHDE CEGRVVEENG EKFMLFYGMS SESAMKRHVG GVAQYRAAEG KTVKLPLRGS
VDNTVRDIMG GLRSACTYVG ASHLKELTKR TTFIRVAEQE NRVFGTD
//
