ID   GUAC_STAA3              Reviewed;         325 AA.
AC   Q2FH96;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=SAUSA300_1235;
OS   Staphylococcus aureus (strain USA300).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=367830;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16517273; DOI=10.1016/S0140-6736(06)68231-7;
RA   Diep B.A., Gill S.R., Chang R.F., Phan T.H., Chen J.H., Davidson M.G.,
RA   Lin F., Lin J., Carleton H.A., Mongodin E.F., Sensabaugh G.F.,
RA   Perdreau-Remington F.;
RT   "Complete genome sequence of USA300, an epidemic clone of community-
RT   acquired meticillin-resistant Staphylococcus aureus.";
RL   Lancet 367:731-739(2006).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000255; ABD21078.1; -; Genomic_DNA.
DR   RefSeq; YP_493932.1; -.
DR   SMR; Q2FH96; 3-319.
DR   GeneID; 3915209; -.
DR   GenomeReviews; CP000255_GR; SAUSA300_1235.
DR   KEGG; saa:SAUSA300_1235; -.
DR   HOGENOM; Q2FH96; -.
DR   OMA; Q2FH96; NSRSECD.
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    325       GMP reductase.
FT                                /FTId=PRO_0000294286.
FT   NP_BIND     203    226       NADP (Potential).
FT   ACT_SITE    174    174       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   325 AA;  36116 MW;  F1F1819AB540C446 CRC64;
     MKIFDYEDIQ LIPNKCIVES RSECDTTIQF GPKKFKLPVV PANMQTVMNE KLAKWFAEND
     YFYIMHRFDE EARIPFIKHM QNSGLFASIS VGVKKAEFDF IEKLAQEKLI PEYITIDIAH
     GHSDSVINMI KHIKTHIPDS FVIAGNVGTP EGVRELENAG ADATKVGIGP GRVCITKIKT
     GFGTGGWQLA ALNICSKAAR KPLIADGGIR THGDIAKSIR FGASMVMIGS LFAAHEESPG
     ETVELDGKQY KEYFGSASEF QKGEHKNVEG KKMFVEHKGS LMDTLKEMQQ DLQSSISYAG
     GKDLKSLRTV DYVIVRNSIF NGDRD
//