ID   GUAC_BACAH              Reviewed;         328 AA.
AC   A0RLN5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   16-JUN-2009, 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=BALH_4963;
OS   Bacillus thuringiensis (strain Al Hakam).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=412694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17337577; DOI=10.1128/JB.00241-07;
RA   Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Green L.D., Han C.S., Hill K.K., Hitchcock P.,
RA   Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S.,
RA   Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O.,
RA   Wills P.L., Gilna P., Brettin T.S.;
RT   "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL   J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK88128.1; -; Genomic_DNA.
DR   RefSeq; YP_897635.1; -.
DR   SMR; A0RLN5; 2-322.
DR   GeneID; 4543702; -.
DR   GenomeReviews; CP000485_GR; BALH_4963.
DR   KEGG; btl:BALH_4963; -.
DR   OMA; A0RLN5; 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_0000292049.
FT   NP_BIND     205    228       NADP (Potential).
FT   ACT_SITE    176    176       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   328 AA;  36303 MW;  7770C14C1FF1EE72 CRC64;
     MMENVFDYED IQLIPAKCIV NSRSECDTTV TLGKHKFKLP VVPANMQTII DERIATYLAE
     NNYFYIMHRF QPEKRISFIR DMQSRGLIAS ISVGVKEDEY EFVQQLAAEH LTPEYITIDI
     AHGHSNAVIN MIQHIKKHLP ESFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKI
     KTGFGTGGWQ LAALRWCAKA ASKPIIADGG IRTHGDVAKS IRFGATMVMI GSLFAGHEES
     PGETIEKDGK LYKEYFGSAS EFQKGEKKNV EGKKMFVEHK GSLEDTLIEM EQDLQSSISY
     AGGTKLDSIR TVDYVVVKNS IFNGDKVY
//