ID   GMPR_CAEEL              Reviewed;         358 AA.
AC   O16294;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Probable GMP reductase;
DE            EC=1.7.1.7;
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase;
DE            Short=Guanosine monophosphate reductase;
GN   ORFNames=F32D1.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
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; AF016427; AAB65350.1; -; Genomic_DNA.
DR   PIR; T03917; T03917.
DR   RefSeq; NP_504202.1; -.
DR   UniGene; Cel.6523; -.
DR   HSSP; P49058; 1EEP.
DR   SMR; O16294; 2-339.
DR   Ensembl; F32D1.5; Caenorhabditis elegans.
DR   GeneID; 178834; -.
DR   KEGG; cel:F32D1.5; -.
DR   WormBase; WBGene00017984; F32D1.5.
DR   WormPep; F32D1.5; CE09869.
DR   OMA; O16294; NSRSECD.
DR   BRENDA; 1.7.1.7; 672.
DR   NextBio; 902748; -.
DR   ArrayExpress; O16294; -.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:EC.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0040007; P:growth; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
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   Complete proteome; Metal-binding; NADP; Oxidoreductase; Potassium.
FT   CHAIN         1    358       Probable GMP reductase.
FT                                /FTId=PRO_0000093729.
FT   NP_BIND     109    132       NADP (By similarity).
FT   ACT_SITE    187    187       Thioimidate intermediate (By similarity).
FT   METAL       182    182       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       184    184       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     220    220       NADP (By similarity).
SQ   SEQUENCE   358 AA;  38806 MW;  A4AEE84F2CB72360 CRC64;
     MPRIENEPKL DFKDVLLRPK RSTLKSRADV ELDREYVFRN SKATYTGVPV VASNMDTVGT
     FEMAAALNNH KIFTTIHKHY SVDEWKAFAA SASPDTFNNL AISSGISDND WTKLNTVITE
     LPQLKYICLD VANGYSESFV EFIRRVREAY PKHTIMAGNV VTGEMVEELI LSGADIVKVG
     IGPGSVCTTR KKAGVGYPQL SAVLECADAA HGLNGHVMSD GGCSNPGDVA KAFGAGADFV
     MIGGLFAGHD QSGGDLIEHN GKKFKLFYGM SSDTAMKKHH GSVAEYRASE GKTVTIPYRG
     DVNGTVQDIL GGIRSACTYT GAKHLKELAK RATFIRVTQQ TNDMYVPFEV PTVPAPSK
//