ID   GUAC_LACS1              Reviewed;         325 AA.
AC   Q1WT04;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=LSL_1139;
OS   Lactobacillus salivarius subsp. salivarius (strain UCC118).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=362948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C.,
RA   Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F.,
RA   van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(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; CP000233; ABD99947.1; -; Genomic_DNA.
DR   RefSeq; YP_536030.1; -.
DR   GeneID; 3977879; -.
DR   GenomeReviews; CP000233_GR; LSL_1139.
DR   KEGG; lsl:LSL_1139; -.
DR   HOGENOM; Q1WT04; -.
DR   OMA; Q1WT04; NSRSECD.
DR   BioCyc; LSAL362948:LSL_1139-MON; -.
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_0000292053.
FT   NP_BIND     203    226       NADP (Potential).
FT   ACT_SITE    174    174       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   325 AA;  35714 MW;  253C67F02267DE36 CRC64;
     MPVFDYEDIQ LVPNKCIVKS RSEVNTKVKF GPMTFKIPVV PANMQTIIDE NLAVWLAKNG
     YFYIMHRFYE NERVDFVKNM HDKGLFASIS VGVKPAEYDL IDELSQKNLV PEYITIDIAH
     GHSDTVINMI KHIKHKLPGV FVIAGNVGTP EAVRELENAG ADATKVGIGP GKACITKLKT
     GFGTGGWQLA AIRACAKAAS KPIVADGGIR NNGDIAKSIR FGASMCMIGS LFAGHDETPG
     DIIEKDGKKF KTYFGSASQY QKGEYKNVEG KKLLLPYKGK IADTLREMQE DLQSAISYAG
     GKELLALRKV DYVIVKNSIY NGDML
//