ID   GUAC_LACGA              Reviewed;         330 AA.
AC   Q045S8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-NOV-2008, 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=LGAS_0389;
OS   Lactobacillus gasseri (strain ATCC 33323 / DSM 20243).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=324831;
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; CP000413; ABJ59794.1; -; Genomic_DNA.
DR   RefSeq; YP_814232.1; -.
DR   GeneID; 4440320; -.
DR   GenomeReviews; CP000413_GR; LGAS_0389.
DR   KEGG; lga:LGAS_0389; -.
DR   NMPDR; fig|1596.1.peg.1138; -.
DR   HOGENOM; Q045S8; -.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
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_DHase_GMPRtase.
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    330       GMP reductase.
FT                                /FTId=PRO_0000294275.
FT   NP_BIND     209    232       NADP (Potential).
FT   ACT_SITE    180    180       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   330 AA;  36644 MW;  C20266C30D19BDDE CRC64;
     MSNYFSMEAF DYDDIQLVPN KCIIKSRKEA DTSVKFGSRT FKIPVVPANM ESVIDDDLAI
     WLAENGYYYV MHRFHPEKRA NFIKMMHDKG LFASISVGIK DSEYDFIDYL AKEKIIPEYI
     TIDVAHGHSD YVIKMIKYIK DKLPDTFLTA GNIATPEAVR ELENAGADAT KVGVGPGRAC
     ITKLKTGFGT GGWQLAALRM CSKAARKPLI ADGGIRHNGD IAKSVRFGAS MVMIGSLFAG
     HEESPGNLIT IDGKRYKQYW GSASEVQKGA YRNVEGKQML VPYRGSIKDT LREMQEDLQS
     SISYAGGKDL SAIRVVDYVI VKSSIFDGDK
//