ID   GUAC_RHOFD              Reviewed;         325 AA.
AC   Q21U05;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Rfer_3037;
OS   Rhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM
RT   15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000267; ABD70748.1; -; Genomic_DNA.
DR   RefSeq; YP_524279.1; -.
DR   GeneID; 3961012; -.
DR   GenomeReviews; CP000267_GR; Rfer_3037.
DR   KEGG; rfr:Rfer_3037; -.
DR   NMPDR; fig|338969.3.peg.3457; -.
DR   HOGENOM; Q21U05; -.
DR   OMA; Q21U05; NSRSECD.
DR   BioCyc; RFER338969:RFER_3037-MON; -.
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    325       GMP reductase.
FT                                /FTId=PRO_0000294283.
FT   NP_BIND     202    225       NADP (Potential).
FT   ACT_SITE    173    173       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   325 AA;  35813 MW;  0DBB4DB4564FB50D CRC64;
     MEIFDYDNIL LLPRKCRVES RSECDASVEL GRQRFRIPVV PANMKTVVDE SICVWLAQNS
     YFYVMHRFDL DNVQFVKNMK ARGLYASISL GVKKPDYDTV DQLLALGLVP DYITIDIAHG
     HADSVKNMIG YLKEKMPTVF IIAGNVATPE AVIDLENWGA DATKVGIGPG KVCITKLKTG
     FGTGGWQLSA VKWCARVATK PIIADGGIHE HGDIAKSIRF GATMVMIGSM LAGHEESPGK
     SVEVDGKLYK EYYGSASDFN KGEYKHVEGK RILEPVKGKL ADTLIEMEQD VQSSISYSGG
     KRLMDIRKVN YVTLGGDNAG EHLLM
//