ID C3TQF7_ECOLX Unreviewed; 347 AA.
AC C3TQF7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_00596};
DE EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_00596};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00596};
DE Short=Guanosine monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_00596};
GN Name=guaC {ECO:0000256|HAMAP-Rule:MF_00596,
GN ECO:0000313|EMBL:QCL50214.1};
GN ORFNames=C9E67_25565 {ECO:0000313|EMBL:QCL50214.1}, ECs0108
GN {ECO:0000313|EMBL:ACI71509.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI71509.1};
RN [1] {ECO:0000313|EMBL:ACI71509.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=493/89 {ECO:0000313|EMBL:ACI71509.1}, 86-24
RC {ECO:0000313|EMBL:ACI71510.1}, 87-14 {ECO:0000313|EMBL:ACI71511.1},
RC TB182A {ECO:0000313|EMBL:ACI71512.1}, and TW14359
RC {ECO:0000313|EMBL:ACI71513.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
RN [2] {ECO:0000313|EMBL:QCL50214.1, ECO:0000313|Proteomes:UP000298553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=143 {ECO:0000313|EMBL:QCL50214.1,
RC ECO:0000313|Proteomes:UP000298553};
RA Bono J.L., Arthur T.M.;
RT "WGA of Escherichia coli O157:H7: comparison of multiple isolates.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000256|ARBA:ARBA00037691, ECO:0000256|HAMAP-Rule:MF_00596,
CC ECO:0000256|RuleBase:RU003929}.
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 Evidence={ECO:0000256|ARBA:ARBA00000930, ECO:0000256|HAMAP-
CC Rule:MF_00596, ECO:0000256|RuleBase:RU003929};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00596}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00596}.
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DR EMBL; EU906395; ACI71509.1; -; Genomic_DNA.
DR EMBL; EU906396; ACI71510.1; -; Genomic_DNA.
DR EMBL; EU906397; ACI71511.1; -; Genomic_DNA.
DR EMBL; EU906398; ACI71512.1; -; Genomic_DNA.
DR EMBL; EU906399; ACI71513.1; -; Genomic_DNA.
DR EMBL; CP028607; QCL50214.1; -; Genomic_DNA.
DR RefSeq; WP_001217330.1; NZ_WJRH01000007.1.
DR PATRIC; fig|562.7073.peg.573; -.
DR OMA; AYKEYFG; -.
DR Proteomes; UP000298553; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR01305; GMP_reduct_1; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000235; GMP_reductase; 1.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00596,
KW ECO:0000256|PIRSR:PIRSR000235-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00596};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00596};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00596}.
FT DOMAIN 9..338
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-1"
FT BINDING 108..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 216..239
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596"
SQ SEQUENCE 347 AA; 37398 MW; 912C5AE96D400441 CRC64;
MRIEEDLKLG FKDVLIRPKR STLKSRSDVE LERQFTFKHS GQSWSGVPII AANMDTVGTF
SMASALASFD ILTAVHKHYS VEEWQAFINN SSADVLKHVM VSTGTSDADF EKTKQILDLN
PALNFVCIDV ANGYSEHFVQ FVAKAREAWP TKTICAGNVV TGEMCEELIL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGMIISDG GCTTPGDVAK AFGGGADFVM
LGGMLAGHEE SGGRIVEENG EKFMLFYGMS SESAMKRHVG GVAEYRAAEG KTVKLPLRGP
VENTARDILG GLRSACTYVG ASRLKELTKR TTFIRVQEQE NRIFNNL
//
