GUAC_STRR6
ID GUAC_STRR6 Reviewed; 328 AA.
AC Q8DPJ7;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=spr1128;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(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_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; AE007317; AAK99931.1; -; Genomic_DNA.
DR PIR; G98012; G98012.
DR RefSeq; NP_358721.1; NC_003098.1.
DR RefSeq; WP_000931162.1; NC_003098.1.
DR AlphaFoldDB; Q8DPJ7; -.
DR SMR; Q8DPJ7; -.
DR STRING; 171101.spr1128; -.
DR EnsemblBacteria; AAK99931; AAK99931; spr1128.
DR GeneID; 60234223; -.
DR KEGG; spr:spr1128; -.
DR PATRIC; fig|171101.6.peg.1224; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_0_9; -.
DR OMA; AYKEYFG; -.
DR Proteomes; UP000000586; 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; Reference proteome.
FT CHAIN 1..328
FT /note="GMP reductase"
FT /id="PRO_0000093776"
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 328 AA; 35883 MW; 1DD3F30FF8A091C5 CRC64;
MLNEFPIFDY EDIQLIPNKC VIKSRAEADT SVTLGNHTFK LPVVPANMQT ILDENVAEQL
AKGGYFYIMH RFDEAGRIPF IKRMHDQGLI ASISVGVKDY EYDFVSQLKA DAPEYITIDI
AHGHADSVIS MIQHIKKELP DTFVIAGNVG TPEAVRELEN AGADATKVGI GPGKVCITKV
KTGFGTGGWQ LAALRWCAKA ARKPIIADGG IRTHGDIAKS IRFGASMIMI GSLFAGHIES
PGKTIEVDGE QFKEYYGSAS QYQKGAYKNV EGKRILLPAK GHLQDTLTEM EQDLQSAISY
AGGRQVADLK HVDYVIVKNS IWNGDASH