ID   GMPR_ASCSU              Reviewed;         356 AA.
AC   P27442;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-NOV-2008, entry version 49.
DE   RecName: Full=GMP reductase;
DE            EC=1.7.1.7;
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase;
DE            Short=Guanosine monophosphate reductase;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Ascaridida; Ascaridoidea;
OC   Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92319011; PubMed=1620164; DOI=10.1016/0166-6851(92)90059-S;
RA   Gruidl M.E., Bunch K., Gharib S., Bennett K.L.;
RT   "The GMP reductase gene of the nematode Ascaris lumbricoides var.
RT   suum.";
RL   Mol. Biochem. Parasitol. 52:271-274(1992).
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   -!- 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; M82838; AAA29373.1; -; mRNA.
DR   HSSP; P12268; 1B3O.
DR   SMR; P27442; 10-340.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:InterPro.
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_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   2: Evidence at transcript level;
KW   Metal-binding; NADP; Oxidoreductase; Potassium.
FT   CHAIN         1    356       GMP reductase.
FT                                /FTId=PRO_0000093728.
FT   NP_BIND     111    134       NADP (By similarity).
FT   ACT_SITE    189    189       Thioimidate intermediate (By similarity).
FT   METAL       184    184       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       186    186       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     222    222       NADP (By similarity).
SQ   SEQUENCE   356 AA;  39252 MW;  2D1B4F1B64EFB26A CRC64;
     MPRIEFEPKL DFKDVLLRPK RSTLRSRAEV DLMREYVFRN SKKTYVGVPV VASNMDTVGT
     FEMAEVLAKF SLFTTIHKHY QVDEWKAFVQ RVDSNPQIMS QIGISSGIST SDFDKLRTVC
     DMIPELEYIC LDVANGYSEV FVDFIRRVRE QFPTHTIFAG NVVTGEMVEE LILSGADVVK
     VGIGPGSVCT TRKKAGVGYP QLSAVLECAD ASHGLNGHVM SDGGCTNPGD VAKAFGGGAD
     FVMIGGLLAG HDQCGGEVVE KDGKKYKLFY GMSSDTAMKK YQGSVAEYRA SEGKTIYMPY
     RGDVSRTIHD LLGGLRSACT YIGATKLKEL SKRATFVRVT QQTNDQYSAY EVPRID
//