GUAC_ECOLI
ID GUAC_ECOLI Reviewed; 347 AA.
AC P60560; P15344; P78048;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
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=b0104, JW0101;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2904262; DOI=10.1042/bj2550035;
RA Andrews S.C., Guest J.R.;
RT "Nucleotide sequence of the gene encoding the GMP reductase of Escherichia
RT coli K12.";
RL Biochem. J. 255:35-43(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA Fujita N., Mori H., Yura T., Ishihama A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT 4.1 min (110,917-193,643 bp) region.";
RL Nucleic Acids Res. 22:1637-1639(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 233-235.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 244-347.
RC STRAIN=K12;
RX PubMed=7959070; DOI=10.1016/0378-1119(94)90851-6;
RA Whitchurch C.B., Mattick J.S.;
RT "Escherichia coli contains a set of genes homologous to those involved in
RT protein secretion, DNA uptake and the assembly of type-4 fimbriae in other
RT bacteria.";
RL Gene 150:9-15(1994).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
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.
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 -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P60560; P76015: dhaK; NbExp=2; IntAct=EBI-544491, EBI-544485;
CC P60560; P15288: pepD; NbExp=3; IntAct=EBI-544491, EBI-542419;
CC P60560; P15034: pepP; NbExp=3; IntAct=EBI-544491, EBI-554801;
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; X07917; CAA30751.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73215.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96673.2; -; Genomic_DNA.
DR EMBL; L28105; AAC36926.1; -; Genomic_DNA.
DR PIR; H64732; H64732.
DR RefSeq; NP_414646.1; NC_000913.3.
DR RefSeq; WP_001217338.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P60560; -.
DR SMR; P60560; -.
DR BioGRID; 4261108; 14.
DR BioGRID; 853234; 1.
DR DIP; DIP-47861N; -.
DR IntAct; P60560; 6.
DR STRING; 511145.b0104; -.
DR jPOST; P60560; -.
DR PaxDb; P60560; -.
DR PRIDE; P60560; -.
DR EnsemblBacteria; AAC73215; AAC73215; b0104.
DR EnsemblBacteria; BAB96673; BAB96673; BAB96673.
DR GeneID; 66671607; -.
DR GeneID; 948986; -.
DR KEGG; ecj:JW0101; -.
DR KEGG; eco:b0104; -.
DR PATRIC; fig|1411691.4.peg.2177; -.
DR EchoBASE; EB0417; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_3_6; -.
DR InParanoid; P60560; -.
DR OMA; AYKEYFG; -.
DR PhylomeDB; P60560; -.
DR BioCyc; EcoCyc:GMP-REDUCT-MON; -.
DR BioCyc; MetaCyc:GMP-REDUCT-MON; -.
DR PRO; PR:P60560; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032264; P:IMP salvage; IDA:MGI.
DR GO; GO:0015951; P:purine ribonucleotide interconversion; IDA:EcoCyc.
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 1: Evidence at protein level;
KW Direct protein sequencing; Metal-binding; NADP; Oxidoreductase; Potassium;
KW Reference proteome.
FT CHAIN 1..347
FT /note="GMP reductase"
FT /id="PRO_0000093735"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 108..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 216..239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 233..235
FT /note="GGG -> AR (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 37384 MW; 898F50DA7FD00441 CRC64;
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF
SMASALASFD ILTAVHKHYS VEEWQAFINN SSADVLKHVM VSTGTSDADF EKTKQILDLN
PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIVSDG GCTTPGDVAK AFGGGADFVM
LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL
