ID   GUAC_BACSU              Reviewed;         326 AA.
AC   O05269;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 57.
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; Synonyms=yumD; OrderedLocusNames=BSU32130;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Oudega B., Koningstein G., de Sales Ramon M., Rodrigues L.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PROBABLE FUNCTION, AND REGULATION OF EXPRESSION.
RC   STRAIN=168;
RX   MEDLINE=21475760; PubMed=11591660;
RX   DOI=10.1128/JB.183.21.6175-6183.2001;
RA   Saxild H.H., Brunstedt K., Nielsen K.I., Jarmer H., Nygaard P.;
RT   "Definition of the Bacillus subtilis PurR operator using genetic and
RT   bioinformatic tools and expansion of the PurR regulon with glyA, guaC,
RT   pbuG, xpt-pbuX, yqhZ-folD, and pbuO.";
RL   J. Bacteriol. 183:6175-6183(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       (Probable).
CC   -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NH(3) + NADP(+) =
CC       guanosine 5'-phosphate + NADPH.
CC   -!- INDUCTION: Expression is regulated by purR.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2
CC       subfamily.
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DR   EMBL; Z93939; CAB07955.1; -; Genomic_DNA.
DR   EMBL; Z99120; CAB15203.1; -; Genomic_DNA.
DR   PIR; C70015; C70015.
DR   RefSeq; NP_391093.1; -.
DR   HSSP; P12268; 1B3O.
DR   SMR; O05269; 1-321.
DR   GeneID; 937189; -.
DR   GenomeReviews; AL009126_GR; BSU32130.
DR   KEGG; bsu:BSU32130; -.
DR   NMPDR; fig|224308.1.peg.3219; -.
DR   SubtiList; BG12392; guaC.
DR   HOGENOM; O05269; -.
DR   OMA; O05269; NSRSECD.
DR   BioCyc; BSUB224308:BSU3210-MON; -.
DR   BRENDA; 1.7.1.7; 150.
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   2: Evidence at transcript level;
KW   Complete proteome; NADP; Oxidoreductase.
FT   CHAIN         1    326       GMP reductase.
FT                                /FTId=PRO_0000093752.
FT   NP_BIND     204    227       NADP (By similarity).
FT   ACT_SITE    175    175       Thioimidate intermediate (By similarity).
SQ   SEQUENCE   326 AA;  35819 MW;  4D5EC6F22951D353 CRC64;
     MENVFDYEDI QLIPAKCIVN SRSECDTSVR LGGHTFKLPV VPANMQTIID EKLAISLAEN
     GYFYVMHRFE PETRIDFIKD MNARGLFSSI SVGVKDEEYE FVRQLAEENL TPEYVTIDIA
     HGHSNAVIEM IQHLKKHLPD SFVIAGNVGT PEAVRELENA GADATKVGIG PGKVCITKIK
     TGFGTGGWQL AALRWCAKAA SKPIIADGGI RTHGDIAKSI RFGATMVMIG SLFAGHEESP
     GQTIEKDGKL YKEYFGSASE FPKGEKKNVE GKKMHVAHKG SIKDTLIEME QDLQSSISYA
     GGTKLNAIRN VDYVIVKNSI FNGDKY
//