ID E9GCV2_DAPPU Unreviewed; 351 AA. AC E9GCV2; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 04-NOV-2026, entry version 69. DE RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_03195}; DE Short=GMPR {ECO:0000256|HAMAP-Rule:MF_03195}; DE EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_03195}; DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03195}; DE Short=Guanosine monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_03195}; GN ORFNames=DAPPUDRAFT_210496 {ECO:0000313|EMBL:EFX82619.1}; OS Daphnia pulex (Water flea). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida; OC Branchiopoda; Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia. OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX82619.1, ECO:0000313|Proteomes:UP000000305}; RN [1] {ECO:0000313|EMBL:EFX82619.1, ECO:0000313|Proteomes:UP000000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21292972; DOI=10.1126/science.1197761; RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A., RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J., RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q., RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D., RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D., RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J., RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M., RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y., RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H., RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R., RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P., RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.; RT "The ecoresponsive genome of Daphnia pulex."; RL Science 331:555-561(2011). 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_03195, CC ECO:0000256|RuleBase:RU003929}. CC -!- CATALYTIC ACTIVITY: CC Reaction=IMP + NH4(+) + NADP(+) = GMP + NADPH + 2 H(+); 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:ARBA00048616, ECO:0000256|HAMAP- CC Rule:MF_03195, ECO:0000256|RuleBase:RU003929}; CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03195}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily. CC {ECO:0000256|HAMAP-Rule:MF_03195}. 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; GL732539; EFX82619.1; -; Genomic_DNA. DR AlphaFoldDB; E9GCV2; -. DR STRING; 6669.E9GCV2; -. DR KEGG; dpx:DAPPUDRAFT_210496; -. DR eggNOG; KOG2550; Eukaryota. DR HOGENOM; CLU_022552_5_3_1; -. DR InParanoid; E9GCV2; -. DR OMA; AFAKHQM; -. DR OrthoDB; 418595at2759; -. DR PhylomeDB; E9GCV2; -. DR Proteomes; UP000000305; Unassembled WGS sequence. 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 FunFam; 3.20.20.70:FF:000012; GMP reductase; 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; IPR050139; GMP_reductase. 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 NCBIfam; NF003470; PRK05096.1; 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|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03195}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_03195}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_03195}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03195}; KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631, ECO:0000256|HAMAP- KW Rule:MF_03195}; Reference proteome {ECO:0000313|Proteomes:UP000000305}. FT DOMAIN 10..340 FT /note="IMP dehydrogenase/GMP reductase" FT /evidence="ECO:0000259|Pfam:PF00478" FT ACT_SITE 186 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195, FT ECO:0000256|PIRSR:PIRSR000235-1" FT ACT_SITE 188 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03195" FT BINDING 181 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195, FT ECO:0000256|PIRSR:PIRSR000235-3" FT BINDING 183 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195, FT ECO:0000256|PIRSR:PIRSR000235-3" FT BINDING 186 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 189 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 219..221 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 242..243 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 268..270 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03195" FT BINDING 286..290 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_03195" SQ SEQUENCE 351 AA; 37796 MW; 1C4314E35F73D865 CRC64; MPRIDNDVKL DFKDVLLRPK RSTLKSRADV DLFREIKFRN SKQTIRGIPI IASNMDTVGT FEMASALAKH GLLTTIHKHY QVEEWVNFMQ KNKDVAGFVA ASSGSGKGDF EKLSKILNAV PEVRFVCLDV ANGYSEHFVE FVRSVREAFP QHVIMAGNVV TGEMVEELIL SGADIIKVGI GPGSVCTTRK KTGVGYPQIS AVIECADAAH GLGGHIISDG GCTCPGDVAK AFGAGADFVM LGGMLSGHDQ SGGDVIERDG KKYKLFYGMS SATAMNKHVG GVSEYRASEG KTVEVPYRGN VDATISDILG GLRSACTYTG AARLKELPKR TTFIRVTQQT NEIFSAFSSG D //