GUAC_STRPZ
ID GUAC_STRPZ Reviewed; 327 AA.
AC B5XLI1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=GMP reductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_01511};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000255|HAMAP-Rule:MF_01511};
DE Short=Guanosine monophosphate reductase {ECO:0000255|HAMAP-Rule:MF_01511};
GN Name=guaC {ECO:0000255|HAMAP-Rule:MF_01511}; OrderedLocusNames=Spy49_0885;
OS Streptococcus pyogenes serotype M49 (strain NZ131).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=471876;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZ131;
RX PubMed=18820018; DOI=10.1128/jb.00672-08;
RA McShan W.M., Ferretti J.J., Karasawa T., Suvorov A.N., Lin S., Qin B.,
RA Jia H., Kenton S., Najar F., Wu H., Scott J., Roe B.A., Savic D.J.;
RT "Genome sequence of a nephritogenic and highly transformable M49 strain of
RT Streptococcus pyogenes.";
RL J. Bacteriol. 190:7773-7785(2008).
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_01511}.
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_01511};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01511}.
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DR EMBL; CP000829; ACI61193.1; -; Genomic_DNA.
DR RefSeq; WP_012560703.1; NC_011375.1.
DR AlphaFoldDB; B5XLI1; -.
DR SMR; B5XLI1; -.
DR EnsemblBacteria; ACI61193; ACI61193; Spy49_0885.
DR KEGG; soz:Spy49_0885; -.
DR HOGENOM; CLU_022552_5_0_9; -.
DR OMA; AYKEYFG; -.
DR Proteomes; UP000001039; 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 3: Inferred from homology;
KW NADP; Oxidoreductase.
FT CHAIN 1..327
FT /note="GMP reductase"
FT /id="PRO_1000146144"
FT ACT_SITE 176
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
FT BINDING 205..228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01511"
SQ SEQUENCE 327 AA; 35915 MW; 1733CADB2F4A4A2D CRC64;
MFNDIPVFDY EDIQLIPNKC IITSRSQADT SVTLGKYQFK LPVIPANMQT IIDETIAEQL
AKEGYFYIMH RFDEDSRKPF IKRMHEQGLI ASISVGVKAC EYDFVTSLKE DAPEFITIDI
AHGHANSVID MIKHIKTELP ETFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKV
KTGFGTGGWQ LAALRWCAKA ARKPIIADGG IRTHGDIAKS IRFGASMVMI GSLFAGHIES
PGKTVEVDGE TFKEYYGSAS EYQKGEHKNV EGKKILLPTK GHLSDTLTEM QQDLQSSISY
AGGKDLDSLR HVDYVIVKNS IWNGDSI