(data stored in ACNUC7421 zone)

SWISSPROT: GUAC_SALTY

ID   GUAC_SALTY              Reviewed;         347 AA.
AC   Q8ZRT5;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-DEC-2019, entry version 107.
DE   RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_00596};
DE            EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_00596};
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00596};
DE            Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_00596};
GN   Name=guaC {ECO:0000255|HAMAP-Rule:MF_00596}; OrderedLocusNames=STM0141;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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. {ECO:0000255|HAMAP-
CC       Rule:MF_00596}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00596};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00596}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00596}.
DR   EMBL; AE006468; AAL19105.1; -; Genomic_DNA.
DR   RefSeq; NP_459146.1; NC_003197.2.
DR   RefSeq; WP_001217365.1; NC_003197.2.
DR   SMR; Q8ZRT5; -.
DR   PaxDb; Q8ZRT5; -.
DR   PRIDE; Q8ZRT5; -.
DR   EnsemblBacteria; AAL19105; AAL19105; STM0141.
DR   GeneID; 1251659; -.
DR   KEGG; stm:STM0141; -.
DR   PATRIC; fig|99287.12.peg.150; -.
DR   eggNOG; ENOG4105CP4; Bacteria.
DR   eggNOG; COG0516; LUCA.
DR   HOGENOM; HOG000165756; -.
DR   KO; K00364; -.
DR   OMA; AYKEYFG; -.
DR   PhylomeDB; Q8ZRT5; -.
DR   BioCyc; SENT99287:STM0141-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR   GO; GO:0003920; F:GMP reductase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015951; P:purine ribonucleotide interconversion; IBA:GO_Central.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00596; GMP_reduct_type1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005993; GMPR.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000235; GMP_reductase; 1.
DR   TIGRFAMs; TIGR01305; GMP_reduct_1; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q8ZRT5.
DR   SWISS-2DPAGE; Q8ZRT5.
KW   Metal-binding; NADP; Oxidoreductase; Potassium; Reference proteome.
FT   CHAIN           1..347
FT                   /note="GMP reductase"
FT                   /id="PRO_0000093739"
FT   NP_BIND         108..131
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   NP_BIND         216..239
FT                   /note="NADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   ACT_SITE        186
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   METAL           181
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
FT   METAL           183
FT                   /note="Potassium; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00596"
SQ   SEQUENCE   347 AA;  37139 MW;  71223D342F001B45 CRC64;
     MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQTWSGVPII AANMDTVGTF
     EMAQALAGFD ILTAVHKHYT VEEWAAFINT ASADVLKHVM VSTGTSDADF EKTVQILALN
     PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI
     GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTMPGDVAK AFGGGADFVM
     LGGMLAGHEE SGGSVVEENG EKFMLFYGMS SESAMNRHVG GVAKYRAAEG KTVKLPLRGP
     VGNTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNSL
//

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