ID   GUAC_CHRVO              Reviewed;         316 AA.
AC   Q7NTY1;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JUN-2009, entry version 37.
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=CV_2922;
OS   Chromobacterium violaceum.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Chromobacterium.
OX   NCBI_TaxID=536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / IFO 12614 / JCM 1249 / NCIB 9131;
RX   MEDLINE=22882880; PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA   Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA   Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA   Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S.,
RA   Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A.,
RA   Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M.,
RA   Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O.,
RA   Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L.,
RA   Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A.,
RA   Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA   Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA   Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P.,
RA   Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S.,
RA   di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M.,
RA   Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C.,
RA   Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O.,
RA   Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P.,
RA   Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E.,
RA   Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N.,
RA   Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C.,
RA   Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L.,
RA   Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T.,
RA   Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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; AE016825; AAQ60590.1; -; Genomic_DNA.
DR   RefSeq; NP_902592.1; -.
DR   HSSP; P12268; 1B3O.
DR   GeneID; 2547468; -.
DR   GenomeReviews; AE016825_GR; CV_2922.
DR   KEGG; cvi:CV_2922; -.
DR   NMPDR; fig|243365.1.peg.2922; -.
DR   HOGENOM; Q7NTY1; -.
DR   OMA; Q7NTY1; NSRSECD.
DR   BioCyc; CVIO243365:CV_2922-MON; -.
DR   BRENDA; 1.7.1.7; 415.
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   ProDom; PD149806; TMP_synthase; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; NADP; Oxidoreductase.
FT   CHAIN         1    316       GMP reductase.
FT                                /FTId=PRO_0000294271.
FT   NP_BIND     202    225       NADP (Potential).
FT   ACT_SITE    175    175       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   316 AA;  34582 MW;  B010B6BA09FC9A8A CRC64;
     MIKTELNYGD VYLVPKKTVV DSRKECDTSV QFGPRRFAMP VYPSNMKSVV SAETCELFAR
     EGWFYTLHRF NVDAVAFTRY MQEQGLFASI SVGVNDDTYE QLDALKAAGL SPEYMTLDIA
     NAWCVKAERM IKHIKQHFPN TFLIGGNVAT AEAARDLEAW GCDAIKAGIA GGRVCITKNK
     TGFHRPMVST VRDCVAAVTI PVIADGGIVE HGDIAKALVC GATMVMAGSL FAGYDESAGD
     IVEIAGKHYK EYFGSASQFN KGAYVNVEGK KILVEYKGSM GKLLRELQED LQSSVSYAGG
     TTLAALREVE MIQVYR
//