ID   GUAC_PHOPR              Reviewed;         347 AA.
AC   Q6LGK4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   04-NOV-2008, entry version 42.
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=PBPRB1716;
OS   Photobacterium profundum (Photobacterium sp. (strain SS9)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=74109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N.,
RA   Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N.,
RA   Romualdi C., Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and
RT   expression analysis.";
RL   Science 307:1459-1461(2005).
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   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1
CC       subfamily.
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DR   EMBL; CR378680; CAG23576.1; -; Genomic_DNA.
DR   RefSeq; YP_133376.1; -.
DR   HSSP; P12268; 1B3O.
DR   GeneID; 3121815; -.
DR   GenomeReviews; CR354532_GR; PBPRB1716.
DR   KEGG; ppr:PBPRB1716; -.
DR   NMPDR; fig|298386.1.peg.1838; -.
DR   HOGENOM; Q6LGK4; -.
DR   BioCyc; PPRO298386:PBPRB1716-MON; -.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:HAMAP.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP.
DR   HAMAP; MF_00596; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005993; GMP_reduct1.
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; PIRSF000235; GMP_reductase; 1.
DR   TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium.
FT   CHAIN         1    347       GMP reductase.
FT                                /FTId=PRO_1000025615.
FT   NP_BIND     108    131       NADP (By similarity).
FT   NP_BIND     216    239       NADP; ribose moiety (By similarity).
FT   ACT_SITE    186    186       Thioimidate intermediate (By similarity).
FT   METAL       181    181       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       183    183       Potassium; via carbonyl oxygen (By
FT                                similarity).
SQ   SEQUENCE   347 AA;  37374 MW;  0638BB1EE360BF83 CRC64;
     MRIEQDLKLG FKDVLFRPKR STLKSRSQVE LTRDFTFKHS GRQWSGVPII AANMDSVGSF
     EMAASLSKHN VMTAIHKHYT VDDWAGFVKN NDAAVLNNAM VSTGTSEADF QKTKDIMALT
     EDLIFICIDI ANGYSEHLVE YVQKVRAEFP TKVISAGNVV TGDMVEELIL AGADIVKVGI
     GPGSVCTTRV KTGVGYPQLS AIIECSDAAH GLGGRIIGDG GCSCAGDVSK AFGGGADFVM
     LGGMLAGHEE SNGEVIEKDG EMFMKFYGMS SQSAMDKHSG GVANYRAAEG KTVLLPFRGP
     VENTIQDIMG GIRSTCTYVG AAQLKELTKR ATFIRVQEQE NNVYGKE
//