ID   GUAC_BACSU              Reviewed;         326 AA.
AC   O05269;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 125.
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 (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
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   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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   SEQUENCE REVISION TO 262.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   PROBABLE FUNCTION, AND REGULATION OF EXPRESSION.
RC   STRAIN=168;
RX   PubMed=11591660; 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 of GMP
CC       to IMP. It functions in the conversion of nucleobase, nucleoside and
CC       nucleotide derivatives of G to A nucleotides, and in maintaining the
CC       intracellular balance of A and G nucleotides (Probable). {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH;
CC         Xref=Rhea:RHEA:17185, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58053, ChEBI:CHEBI:58115,
CC         ChEBI:CHEBI:58349; EC=1.7.1.7;
CC   -!- INDUCTION: Expression is regulated by PurR.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z93939; CAB07955.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15203.2; -; Genomic_DNA.
DR   PIR; C70015; C70015.
DR   RefSeq; NP_391093.2; NC_000964.3.
DR   RefSeq; WP_003244278.1; NZ_JNCM01000033.1.
DR   AlphaFoldDB; O05269; -.
DR   SMR; O05269; -.
DR   STRING; 224308.BSU32130; -.
DR   jPOST; O05269; -.
DR   PaxDb; O05269; -.
DR   PRIDE; O05269; -.
DR   EnsemblBacteria; CAB15203; CAB15203; BSU_32130.
DR   GeneID; 937189; -.
DR   KEGG; bsu:BSU32130; -.
DR   PATRIC; fig|224308.179.peg.3479; -.
DR   eggNOG; COG0516; Bacteria.
DR   InParanoid; O05269; -.
DR   OMA; AYKEYFG; -.
DR   PhylomeDB; O05269; -.
DR   BioCyc; BSUB:BSU32130-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01511; GMP_reduct_type2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005994; GuaC_type_2.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
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   NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..326
FT                   /note="GMP reductase"
FT                   /id="PRO_0000093752"
FT   ACT_SITE        175
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..227
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        262
FT                   /note="Q -> P (in Ref. 1; CAB07955)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   326 AA;  35850 MW;  4CEF76F398E1D353 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 FQKGEKKNVE GKKMHVAHKG SIKDTLIEME QDLQSSISYA
     GGTKLNAIRN VDYVIVKNSI FNGDKY