ID   GMPR2_MOUSE             Reviewed;         348 AA.
AC   Q99L27; Q8R1T5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 63.
DE   RecName: Full=GMP reductase 2;
DE            EC=1.7.1.7;
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase 2;
DE            Short=Guanosine monophosphate reductase 2;
GN   Name=Gmpr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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.
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DR   EMBL; BC003886; AAH03886.1; -; mRNA.
DR   EMBL; BC024109; AAH24109.1; -; mRNA.
DR   IPI; IPI00116248; -.
DR   UniGene; Mm.390685; -.
DR   HSSP; P49058; 1EEP.
DR   SMR; Q99L27; 10-337.
DR   PRIDE; Q99L27; -.
DR   Ensembl; ENSMUSG00000002326; Mus musculus.
DR   MGI; MGI:1917903; Gmpr2.
DR   HOGENOM; Q99L27; -.
DR   HOVERGEN; Q99L27; -.
DR   BRENDA; 1.7.1.7; 244.
DR   Bgee; Q99L27; -.
DR   CleanEx; MM_GMPR2; -.
DR   GermOnline; ENSMUSG00000002326; Mus musculus.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:EC.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005993; GMP_reduct1.
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; PIRSF000235; GMP_reductase; 1.
DR   TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; NADP; Oxidoreductase; Potassium.
FT   CHAIN         1    348       GMP reductase 2.
FT                                /FTId=PRO_0000093727.
FT   NP_BIND     108    131       NADP (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).
FT   BINDING     219    219       NADP (By similarity).
FT   CONFLICT    105    105       T -> S (in Ref. 1; AAH24109).
SQ   SEQUENCE   348 AA;  38033 MW;  83E69980D6877A97 CRC64;
     MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV ELTRSFSFRN SKQMYSGIPV IAANMDTVGT
     FEMARVLCKF SLFTAIHKHY SIHQWQEFAS QNPDCLECLA ASSGTGSADF EQLEQILEAI
     PQVKYICLDV ANGYSEHFVE FVKDVRKRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI
     GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM
     LGGMLAGHSE SGGELIERDG KKYKLFYGMS SEMAMKKYSG GVAEYRASEG KIVEVPFKGD
     VEHTIRDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPIFSNSQ
//