ID A0A0G3CNC5_9GAMM Unreviewed; 347 AA.
AC A0A0G3CNC5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=QQ39_04555 {ECO:0000313|EMBL:AKJ41438.1};
OS Pragia fontium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Pragia.
OX NCBI_TaxID=82985 {ECO:0000313|EMBL:AKJ41438.1, ECO:0000313|Proteomes:UP000068021};
RN [1] {ECO:0000313|EMBL:AKJ41438.1, ECO:0000313|Proteomes:UP000068021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24613 {ECO:0000313|EMBL:AKJ41438.1,
RC ECO:0000313|Proteomes:UP000068021};
RX PubMed=26159528;
RA Snopkova K., Sedlar K., Bosak J., Chaloupkova E., Provaznik I., Smajs D.;
RT "Complete Genome Sequence of Pragia fontium 24613, an Environmental
RT Bacterium from the Family Enterobacteriaceae.";
RL Genome Announc. 3:e00740-15(2015).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010423; AKJ41438.1; -; Genomic_DNA.
DR RefSeq; WP_047780181.1; NZ_UGTK01000001.1.
DR STRING; 82985.QQ39_04555; -.
DR KEGG; pfq:QQ39_04555; -.
DR PATRIC; fig|82985.3.peg.961; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000068021; 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|RuleBase:RU003929};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000068021}.
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596"
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 BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596"
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; 37618 MW; AC07889E74EF6EAB CRC64;
MRIEEDLKLG FKDVLIRPKR STLKSRSEVE LERTYTFKHS GHQWSGIPII AANMDTVGTF
TMAEALASFG LLTAVHKHYT VEQWREFVAR VPESVLRHVM VSTGTSEADF TKLSQIMSFS
PALKFICIDV ANGYSEHFVG FLQKAREAHM DKVICAGNVV TGEMVEELVL SGADIVKVGI
GPGSVCTTRV KTGVGYPQLS AVIECADAAH GLGGQIVSDG GCTMPGDVAK AFGGGADFVM
LGGMLAAHEE CEGKVIEENG NQYMLFYGMS STSAMNRHVG GVAEYRAAEG KTVQLTYRGP
VENTVRDILG GLRSACTYVG AERLKELTKR TTFIRVAEQE NRVFGQS
//
