ID   GUAC_POLSJ              Reviewed;         325 AA.
AC   Q12CT8;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Bpro_1718;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591;
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., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I., Richardson P.;
RT   "Complete sequence of chromosome of Polaromonas sp. JS666.";
RL   Submitted (APR-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; CP000316; ABE43654.1; -; Genomic_DNA.
DR   RefSeq; YP_548552.1; -.
DR   GeneID; 4015620; -.
DR   GenomeReviews; CP000316_GR; Bpro_1718.
DR   KEGG; pol:Bpro_1718; -.
DR   NMPDR; fig|296591.1.peg.4021; -.
DR   HOGENOM; Q12CT8; -.
DR   OMA; Q12CT8; NSRSECD.
DR   BioCyc; PSP296591:BPRO_1718-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_0000294282.
FT   NP_BIND     202    225       NADP (Potential).
FT   ACT_SITE    173    173       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   325 AA;  35566 MW;  030A46B033E60830 CRC64;
     MEIFDYENVL LLPRKCRVES RSECNAGVAL GGRTFRIPVV PANMKTVVDE NICAWMAKNG
     YFYVMHRFDL DNLQFVKNMK AKGVYASISL GVKKPDYDTV DQFVAEGLAP EYITIDIAHG
     HADTVQRMIA YLKQKLPASF VIAGNVATPE AVIDLENWGA DATKVGIGPG KVCITKMKTG
     FGTGGWQLSA LKWCARVATK PIIADGGIRE HGDIAKSIRF GATMVMIGSL LAGLEESPGK
     TVEVDGKLFK EYYGSASDFN KGEYKHVEGK RILEPIKGTL ADTLREMEED IQSSISYAGG
     KKLMDIRKAN YVILGGDNAG EHLLM
//