GUAC_BUCBP
ID GUAC_BUCBP Reviewed; 351 AA.
AC P59443;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=bbp_188;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 (By similarity).
CC {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016826; AAO26920.1; -; Genomic_DNA.
DR RefSeq; WP_011091321.1; NC_004545.1.
DR AlphaFoldDB; P59443; -.
DR SMR; P59443; -.
DR STRING; 224915.bbp_188; -.
DR EnsemblBacteria; AAO26920; AAO26920; bbp_188.
DR GeneID; 56470730; -.
DR KEGG; bab:bbp_188; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_3_6; -.
DR OMA; AYKEYFG; -.
DR OrthoDB; 532857at2; -.
DR Proteomes; UP000000601; 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; -; 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;
KW Metal-binding; NADP; Oxidoreductase; Potassium; Reference proteome.
FT CHAIN 1..351
FT /note="GMP reductase"
FT /id="PRO_0000093734"
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"
SQ SEQUENCE 351 AA; 38564 MW; 67FEEFB53391DD81 CRC64;
MRIEEDIKLG FKDVLIRPKR SILKSRSQVD LTRLFIFKHA QNKWSGIPLI AANMDTVGTF
KMAIALSSFG ILTAIHKYYS YLDWKKFIHT IPGTVVKHIM VSTGMLDEDF VKLKQILSLS
SKLKYICIDV ANGYSEKFVT FLKKVRECYC DKIICAGNVV TGEMVEELIL SGADIVKVGI
GPGSVCTTRA KTAIGYPQLS AVIECSDAAH GLGGQIISDG GCVVSGDIAK AFGGGADFVM
LGGMLAGHKE CEGLIFKENK KRYMIFYGMS SKFAMDRHIG GVARYKTPEG KTVKVLFRGA
VSETINNILG GLRSTCTYVG AFTLKELTKR TTFIKVSEQE NIIFNNQEVS N