ID E3LKS3_CAERE Unreviewed; 358 AA.
AC E3LKS3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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=CRE_18973 {ECO:0000313|EMBL:EFP00306.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 + 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_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}.
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DR EMBL; DS268410; EFP00306.1; -; Genomic_DNA.
DR RefSeq; XP_003115818.1; XM_003115770.1.
DR AlphaFoldDB; E3LKS3; -.
DR STRING; 31234.E3LKS3; -.
DR EnsemblMetazoa; CRE18973.1; CRE18973.1; WBGene00057886.
DR GeneID; 9839483; -.
DR KEGG; crq:GCK72_019443; -.
DR CTD; 9839483; -.
DR eggNOG; KOG2550; Eukaryota.
DR HOGENOM; CLU_022552_5_3_1; -.
DR InParanoid; E3LKS3; -.
DR OMA; TMPRIEN; -.
DR OrthoDB; 5472229at2759; -.
DR Proteomes; UP000008281; 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: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 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_03195,
KW ECO:0000256|PIRSR:PIRSR000235-3};
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:UP000008281}.
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; 39038 MW; 82995B476F07B82B CRC64;
MPRIEFEPKL DFKDVLLRPK RSTLKSRADV DLDREYIFRN SKATYTGVPV VASNMDTVGT
FEMASALNNH KMFTTIHKHY SVEEWKAFAA SVPVETFNNL AISSGISEND WNKLNEVIKA
LPQLKYICLD VANGYSESFV DFIRRVREAY PTHTIMAGNV VTGEMVEELI LSGADIVKVG
IGPGSVCTTR KKAGVGYPQL SAVLECADAA HGLNGHVMSD GGCSNPGDVA KAFGAGADFV
MIGGLFAGHD QSGGDLIEHN GKKFKLFYGM SSDTAMKKHH GSVAEYRASE GKTVTIPYRG
DVNCTVQDIL GGIRSACTYT GSKQLKELAK RATFIRVTQQ TNDMYVPFEV PTLPSQSK
//
