ID A8WIY8_CAEBR Unreviewed; 358 AA. AC A8WIY8; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 02-SEP-2026, entry version 102. 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=CBG23625 {ECO:0000313|EMBL:CAP20432.1, GN ECO:0000313|WormBase:CBG23625}, CBG_23625 GN {ECO:0000313|EMBL:CAP20432.1}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP20432.1, ECO:0000313|Proteomes:UP000008549}; RN [1] {ECO:0000313|EMBL:CAP20432.1, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP20432.1, RC ECO:0000313|Proteomes:UP000008549}; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). RN [2] {ECO:0000313|EMBL:CAP20432.1, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP20432.1, RC ECO:0000313|Proteomes:UP000008549}; RA Ross J.A., Koboldt D.C., Staisch J.E., Chamberlin H.M., Gupta B.P., RA Miller R.D., Baird S.E., Haag E.S.; RT "Caenorhabditis briggsae recombinant inbred line genotypes reveal inter- RT strain incompatibility and the evolution of recombination."; RL PLoS Genet. 7:E1002174-E1002174(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; HE601352; CAP20432.1; -; Genomic_DNA. DR RefSeq; XP_002647836.1; XM_002647790.1. DR AlphaFoldDB; A8WIY8; -. DR FunCoup; A8WIY8; 1982. DR STRING; 6238.A8WIY8; -. DR GeneID; 8589835; -. DR KEGG; cbr:CBG_23625; -. DR CTD; 8589835; -. DR WormBase; CBG23625; CBP12522; WBGene00041935; -. DR eggNOG; KOG2550; Eukaryota. DR HOGENOM; CLU_022552_5_3_1; -. DR InParanoid; A8WIY8; -. DR OMA; IVWRQNS; -. DR OrthoDB; 418595at2759; -. DR Proteomes; UP000008549; 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:UP000008549}. FT DOMAIN 10..340 FT /note="IMP dehydrogenase/GMP reductase" FT /evidence="ECO:0000259|Pfam:PF00478" FT ACT_SITE 187 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195, FT ECO:0000256|PIRSR:PIRSR000235-1" FT ACT_SITE 189 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 130..132 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..182 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 182 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 184 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 187 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 190 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 220..222 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 243..244 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 269..271 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 270 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..287 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 287..291 FT /ligand="GMP" FT /ligand_id="ChEBI:CHEBI:58115" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03195" FT BINDING 315..318 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 358 AA; 38817 MW; 231AD34ADF11005E CRC64; MPRIEFEPKL DFKDVLLRPK RSTLKSRADV DLDREYIFRN SKATYTGVPV VASNMDTVGT FEMASALNNH KMFTTIHKHY SVDEWKAFAA SAAPGTFDNL AISSGISEND WNKLSEVIKA LPQLKYICLD VANGYSESFV DFIRRVREAY PKHTIMAGNV VTGEMVEELI LSGADIVKVG IGPGSVCTTR KKAGVGYPQL SAVLECADAA HGLNGHVMSD GGCSNPGDVA KAFGAGADFV MIGGLFAGHD QSGGDLIESN GKKYKLFYGM SSDTAMKKHH GSVAEYRASE GKTVTIPYRG DVNGTVQDIL GGIRSACTYT GSKQLKELAK RATFIRVTQQ TNDMYVPFEV PTIPSQSK //