ID   GUAC_BUCAP              Reviewed;         349 AA.
AC   Q8K9U0;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   04-NOV-2008, entry version 47.
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=BUsg_198;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67762.1; -; Genomic_DNA.
DR   RefSeq; NP_660551.1; -.
DR   HSSP; P12268; 1B3O.
DR   GeneID; 1005395; -.
DR   GenomeReviews; AE013218_GR; BUsg_198.
DR   KEGG; bas:BUsg198; -.
DR   HOGENOM; Q8K9U0; -.
DR   BioCyc; BAPH198804:BUSG198-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    349       GMP reductase.
FT                                /FTId=PRO_0000093733.
FT   NP_BIND     108    131       NADP (By similarity).
FT   NP_BIND     216    239       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).
SQ   SEQUENCE   349 AA;  38618 MW;  D5CCF618376665CF CRC64;
     MRIEEDIKLG FKDVLIRPKR STLKSRSEVN LIRCFSFKYS TMKWFGIPLI AANMDTIGTF
     RMAEALSKFN ILTAVHKYYS FDEWKNFISV SSKEILEHVI VSIGTSNLDF FKIKKIFSLS
     SELKYICIDV ANGYSEHFVS FLKKIRSFFP DKIICAGNVV TGEMVEELIL SGADIVKVGI
     GPGSVCTTRL KTGIGYPQLS AIIECADAAH GLNGQIISDG GCTVSGDIAK AFGGGADFVM
     LGGMFAGHTE CLGEIIQEKS KKFMLFYGMS STSAMKRYTG KIPGYRASEG KIVKIPFRGN
     VDVTVRDILG GLRSSCTYVG AQKLKELTKR TTFIRVSEQE NCIFNNFKN
//