ID   GUAC_HELPY              Reviewed;         327 AA.
AC   O25525;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-NOV-2008, entry version 51.
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=HP_0854;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   MEDLINE=97394467; PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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; AE000511; AAD07901.1; -; Genomic_DNA.
DR   PIR; F64626; F64626.
DR   RefSeq; NP_207648.1; -.
DR   HSSP; P12268; 1B3O.
DR   SMR; O25525; 5-321.
DR   DIP; DIP:3407N; -.
DR   GeneID; 899383; -.
DR   GenomeReviews; AE000511_GR; HP_0854.
DR   KEGG; hpy:HP0854; -.
DR   NMPDR; fig|85962.1.peg.845; -.
DR   TIGR; HP_0854; -.
DR   HOGENOM; O25525; -.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:InterPro.
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_DHase_GMPRtase.
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_0000093756.
FT   NP_BIND     205    228       NADP (By similarity).
FT   ACT_SITE    176    176       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   327 AA;  36039 MW;  E9ED3053C3E103C8 CRC64;
     MSLKVFDYED VQLIPNKCIV NSRSECDTTV ILGKHAFKMP IVPANMQTII NESIAEFLAE
     NGYFYIMHRF DGAARIPFVK KMKKRQWISS ISVGVKKEEC LFVEELAKQG LAPDYITIDI
     AHGHSNSVIE MIQRIKTHLP ETFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKI
     KTGFGTGGWQ LAALRWCAKA ARKPIIADGG IRTHGDIVKS IRFGATMVMI GSLFAGHEES
     SGETKIENGI AYKEYFGSAS EFQKGEKKNI EGKKIWIQHK GSLKDTLVEM HQDLQSSISY
     AGGRDLEAIR KVDYVIVKNS IFNGDAI
//