ID   GUAC_LACBA              Reviewed;         328 AA.
AC   Q03TT0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=LVIS_0226;
OS   Lactobacillus brevis (strain ATCC 367 / JCM 1170).
OC   Bacteria; Firmicutes; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=387344;
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000416; ABJ63392.1; -; Genomic_DNA.
DR   RefSeq; YP_794423.1; -.
DR   GeneID; 4413048; -.
DR   GenomeReviews; CP000416_GR; LVIS_0226.
DR   KEGG; lbr:LVIS_0226; -.
DR   NMPDR; fig|387344.8.peg.218; -.
DR   HOGENOM; Q03TT0; -.
DR   OMA; Q03TT0; NSRSECD.
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    328       GMP reductase.
FT                                /FTId=PRO_0000292050.
FT   NP_BIND     206    229       NADP (Potential).
FT   ACT_SITE    177    177       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   328 AA;  36006 MW;  DD7A0C66BF41F14B CRC64;
     MHPAEVFDYE DIQLVPNKCI IDSRSEADTS IEFGPRRFKI PVVPANMETV INEPLAVWLA
     EHDYFYVMHR FQPEDRRGFI ERMQAKSLFA SISVGVKPEE VTFIDELATA GLTPEYITID
     IAHGHSDAVI RMIHHIKQQL PNSFVIAGNV GTPEAVRELE NAGADATKVG IGPGKACITK
     LKTGFGTGGW QLAAVRLCAK AARKPIVADG GIRYNGDIAK SIRFGASMVM IGSMLAGHEQ
     SPGSLLTIDG RTFKQYWGSA SEKQKGAYRN VEGKQMLVPY RGDIDQTLTA MEEDLQSAIS
     YAGGRNLLDI RTVDYVIVKS SILNGDNY
//