ID   GUAC_OENOB              Reviewed;         323 AA.
AC   Q04GD9;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 18.
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=OEOE_0535;
OS   Oenococcus oeni (strain BAA-331 / PSU-1).
OC   Bacteria; Firmicutes; Lactobacillales; Oenococcus.
OX   NCBI_TaxID=203123;
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; CP000411; ABJ56483.1; -; Genomic_DNA.
DR   RefSeq; YP_810148.1; -.
DR   GeneID; 4416658; -.
DR   GenomeReviews; CP000411_GR; OEOE_0535.
DR   KEGG; ooe:OEOE_0535; -.
DR   NMPDR; fig|203123.1.peg.1452; -.
DR   OMA; Q04GD9; 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    323       GMP reductase.
FT                                /FTId=PRO_0000294279.
FT   NP_BIND     203    226       NADP (Potential).
FT   ACT_SITE    174    174       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   323 AA;  35343 MW;  D9ABC3A38DF9D89C CRC64;
     MEVFDYENVQ LIPNKCLISS RSEADTSVEF GGHRFKLPVV PANMASVIDD KLAIWLAENG
     YFYIMHRFEP GKRFNFVTDM KQRGLISSIS VGVKEEEYRL IDELVDAGLT PDYITIDIAH
     GYANTVIDMI HYIKKHLPKA FVVAGNIATP DAVRELEDAG ADATKVGIGP GRACITKLKT
     GFGTAGWQLA AVRLCAKAAR KPIIADGGIR HNGDIAKSVR FGASMVMIGS LFAGHKQSPG
     SDLVIDHRHY KQYYGSASAK QKGVYKNVEG KDLLVPYRGD IANTLNEMAQ DLQSSISYAG
     GNNLQALRTV NYVIVQNTIM NGD
//