ID   GUAC_SALPB              Reviewed;         347 AA.
AC   A9MZN3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   04-NOV-2008, entry version 9.
DE   RecName: Full=GMP reductase;
DE            EC=1.7.1.7;
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase;
DE            Short=Guanosine monophosphate reductase;
GN   Name=guaC; OrderedLocusNames=SPAB_00176;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Salmonella;
OC   Salmonella enterica subsp. enterica serovar Paratyphi B.
OX   NCBI_TaxID=272994;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V.,
RA   Nash W., Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the irreversible NADPH-dependent deamination
CC       of GMP to IMP. It functions in the conversion of nucleobase,
CC       nucleoside and nucleotide derivatives of G to A nucleotides, and
CC       in maintaining the intracellular balance of A and G nucleotides
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) =
CC       guanosine 5'-phosphate + NADPH.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1
CC       subfamily.
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DR   EMBL; CP000886; ABX65618.1; -; Genomic_DNA.
DR   RefSeq; YP_001586451.1; -.
DR   GeneID; 5781231; -.
DR   GenomeReviews; CP000886_GR; SPAB_00176.
DR   KEGG; spq:SPAB_00176; -.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:HAMAP.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP.
DR   HAMAP; MF_00596; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005993; GMP_reduct1.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 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   Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium.
FT   CHAIN         1    347       GMP reductase.
FT                                /FTId=PRO_1000082440.
FT   NP_BIND     108    131       NADP (By similarity).
FT   NP_BIND     216    239       NADP; ribose moiety (By similarity).
FT   ACT_SITE    186    186       Thioimidate intermediate (By similarity).
FT   METAL       181    181       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       183    183       Potassium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   347 AA;  37140 MW;  FE1ECEF8A5C8B7C9 CRC64;
     MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQTWSGVPII AANMDTVGTF
     EMAQALAGFD ILTAVHKHYT VEEWAAFINT ASADVLKHVM VSTGTSDADF EKTVQILALD
     PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI
     GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTMPGDVAK AFGGGADFVM
     LGGMLAGHEE SGGSVVEENG EKFMLFYGMS SESAMNRHVG GVAKYRAAEG KTVKLPLRGP
     VGNTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNSL
//