GMPR1_RAT
ID GMPR1_RAT Reviewed; 345 AA.
AC Q9Z244;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=GMP reductase 1 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=GMPR 1 {ECO:0000255|HAMAP-Rule:MF_03195};
DE EC=1.7.1.7 {ECO:0000255|HAMAP-Rule:MF_03195};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase 1 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=Guanosine monophosphate reductase 1 {ECO:0000255|HAMAP-Rule:MF_03195};
GN Name=Gmpr; Synonyms=Gmpr1 {ECO:0000255|HAMAP-Rule:MF_03195};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brown adipose tissue;
RX PubMed=9813009; DOI=10.1074/jbc.273.47.31092;
RA Salvatore D., Bartha T., Larsen P.R.;
RT "The guanosine monophosphate reductase gene is conserved in rats and its
RT expression increases rapidly in brown adipose tissue during cold
RT exposure.";
RL J. Biol. Chem. 273:31092-31096(1998).
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_03195}.
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_03195};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03195}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03195}.
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DR EMBL; AF090867; AAC78657.1; -; mRNA.
DR RefSeq; NP_476536.1; NM_057188.1.
DR AlphaFoldDB; Q9Z244; -.
DR SMR; Q9Z244; -.
DR STRING; 10116.ENSRNOP00000023613; -.
DR iPTMnet; Q9Z244; -.
DR PhosphoSitePlus; Q9Z244; -.
DR jPOST; Q9Z244; -.
DR PaxDb; Q9Z244; -.
DR PRIDE; Q9Z244; -.
DR GeneID; 117533; -.
DR KEGG; rno:117533; -.
DR CTD; 2766; -.
DR RGD; 70980; Gmpr.
DR eggNOG; KOG2550; Eukaryota.
DR InParanoid; Q9Z244; -.
DR OrthoDB; 618077at2759; -.
DR PhylomeDB; Q9Z244; -.
DR BRENDA; 1.7.1.7; 5301.
DR Reactome; R-RNO-74217; Purine salvage.
DR PRO; PR:Q9Z244; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009409; P:response to cold; IEP:RGD.
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 2: Evidence at transcript level;
KW Metal-binding; NADP; Oxidoreductase; Phosphoprotein; Potassium;
KW Purine metabolism; Reference proteome.
FT CHAIN 1..345
FT /note="GMP reductase 1"
FT /id="PRO_0000093725"
FT ACT_SITE 186
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT ACT_SITE 188
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 26..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 78
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 129..131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 180..181
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 181
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 183
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 189
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 242..243
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 268..270
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 269
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 285..286
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 286..290
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT BINDING 314..317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03195"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCZ1"
SQ SEQUENCE 345 AA; 37488 MW; 8B35AE591E32B3EE CRC64;
MPRIDADLKL DFKDVLLRPK RSSLKSRSEV DLERTFTFRN SKQTYSGIPV IVANMDTVGT
FEMAVVMSQH AMFTAIHKHY SLDDWKHFAE NHPECLQHVA VSSGSGQNDL EKMSLILEAV
PQVKFICLDV ANGYSEHFVE FVKLVRSKFP EHTIMAGNVV TGEMVEELIL SGADIIKVGV
GPGSVCTTRT KTGVGYPQLS AVIECADSAH GLKGHIISDG SCTCPGDVAK AFGAGADFVM
LGGMFSGHTE CAGEVIERNG QKLKLFYGMS SDTAMKKHAG GVAEYRASEG KTVEVPYKGD
VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFG
