ID   GUAC_CLOAB              Reviewed;         327 AA.
AC   Q97DK4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JUN-2009, 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=CA_C3471;
OS   Clostridium acetobutylicum.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   MEDLINE=21359325; PubMed=11466286;
RX   DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
RA   Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
RA   Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
RA   Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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. GuaC type 2
CC       subfamily.
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DR   EMBL; AE001437; AAK81399.1; -; Genomic_DNA.
DR   PIR; D97326; D97326.
DR   RefSeq; NP_350059.1; -.
DR   HSSP; P12268; 1B3O.
DR   SMR; Q97DK4; 1-321.
DR   GeneID; 1119653; -.
DR   GenomeReviews; AE001437_GR; CA_C3471.
DR   KEGG; cac:CAC3471; -.
DR   NMPDR; fig|272562.1.peg.3588; -.
DR   HOGENOM; Q97DK4; -.
DR   OMA; Q97DK4; NSRSECD.
DR   BioCyc; CACE272562:CAC3471-MON; -.
DR   BRENDA; 1.7.1.7; 2866.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:HAMAP.
DR   HAMAP; MF_01511; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005994; GMP_reduct2.
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; PIRSF036500; GMP_red_Firmic; 1.
DR   TIGRFAMs; TIGR01306; GMP_reduct_2; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase.
FT   CHAIN         1    327       GMP reductase.
FT                                /FTId=PRO_0000093754.
FT   NP_BIND     204    227       NADP (By similarity).
FT   ACT_SITE    175    175       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   327 AA;  36280 MW;  FA6105BC53D2D466 CRC64;
     MESVFDYEDI QLIPAKCIVR SRSECDTSVI LGEHSFRLPV VPANMQTIID ENIALFLAQN
     GYFYIMHRFE PEKRLSFIKN MKSKGLFASI SVGVKREEYD FIKQLAQENL SPEYITIDIA
     HGHSNTVIEM IQHIKKYLPK SFVIAGNVGT PEAVRELEHA GADATKVGIG PGKVCITKIK
     TGFGTGGWQL AALRWCSKAA SKPIIADGGI RTPGDIAKSI RFGATMVMIG SLFAGHEESP
     GETIEKDGKL YKEYFGSASE FQKGEKRNVE GKKMFVEYKG PLKDTLIEME QDLQSSISYA
     GGKSLDAIRT VDYVIVKNSI FNGDRIY
//