ID   GUAC_PEDPA              Reviewed;         325 AA.
AC   Q03GJ0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=PEPE_0595;
OS   Pediococcus pentosaceus (strain ATCC 25745 / 183-1w).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae; Pediococcus.
OX   NCBI_TaxID=278197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B.,
RA   Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N.,
RA   Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K.,
RA   Goodstein D.M., Hawkins T., Plengvidhya V., Welker D., Hughes J.,
RA   Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B.,
RA   Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E.,
RA   Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C.,
RA   Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J.,
RA   Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S.,
RA   Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2
CC       subfamily.
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DR   EMBL; CP000422; ABJ67682.1; -; Genomic_DNA.
DR   RefSeq; YP_804124.1; -.
DR   SMR; Q03GJ0; 3-319.
DR   GeneID; 4418216; -.
DR   GenomeReviews; CP000422_GR; PEPE_0595.
DR   KEGG; ppe:PEPE_0595; -.
DR   NMPDR; fig|278197.10.peg.547; -.
DR   OMA; Q03GJ0; ESPGNVI.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP.
DR   HAMAP; MF_01511; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005994; GMP_reduct2.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF036500; GMP_red_Firmic; 1.
DR   TIGRFAMs; TIGR01306; GMP_reduct_2; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase.
FT   CHAIN         1    325       GMP reductase.
FT                                /FTId=PRO_0000294280.
FT   NP_BIND     203    226       NADP (Potential).
FT   ACT_SITE    174    174       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   325 AA;  36061 MW;  2C83AA2A6F2CBBAA CRC64;
     MKVFDYEDIQ LIPAKCIVRS RTECDPTVVL GEHRFKLPVV PANMQTIINE EIAEKLAEDG
     YFYIMHRFEP ERRMDFVKKM KDKGLISSIS VGVKDDEYAL IDQLAEENLT PDYITIDVAH
     GHAQSVIDMI HYIKEKLPAA FVIAGNVGTQ EGVRELENAG ADATKVGIGP GKVCITKIKT
     GFGTGGWQLS ALRWCAKVAR KPLIADGGIR THGDIAKSIR FGATMVMIGS LFAGHIESPG
     ETKVEDGVKY KEYFGSASQY QKGEAKNVEG KKIWIHQRGH LRDTLQAMRE DLQSSISYAG
     GRDLEAIRKV DYVIVKNSIF NGDVL
//