ID   GUAC_LACDB              Reviewed;         330 AA.
AC   Q04CB0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-NOV-2008, entry version 15.
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=LBUL_0246;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC BAA-365).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=321956;
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; CP000412; ABJ57912.1; -; Genomic_DNA.
DR   RefSeq; YP_812350.1; -.
DR   GeneID; 4435616; -.
DR   GenomeReviews; CP000412_GR; LBUL_0246.
DR   KEGG; lbu:LBUL_0246; -.
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_0000294274.
FT   NP_BIND     209    232       NADP (Potential).
FT   ACT_SITE    180    180       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   330 AA;  36689 MW;  C2D44E78A551BA0A CRC64;
     MNNYFSMEAF DYDDIQLVPN KAIVNSRKEC VTSVKFGNRT FKIPVVPANM ESVIDEKLAV
     WLAQNGYYYV MHRFQPEKRA DFIKMMHEKG LFASISVGIK DDEYDFIDEL VEKDLIPEYT
     TIDVAHGHSV YVIDMIKYIK EKMPDTFLTA GNVATPEAVR ELENAGADAT KVGVGPGKAC
     ITKLKTGFGT GGWQLAALRM CSKVARKPLI ADGGIRHNGD IAKSVRFGAS MVMIGSMLAG
     HEESPGNVIK IDGKTYKQYW GSASEVQKGA YRNVEGKQML VPYRGSIANT LEEMKEDLQS
     SISYAGGRDL ESIKRVDYVI VKNTIMNGDY
//