ID A0A1S3AMD0_ERIEU Unreviewed; 348 AA.
AC A0A1S3AMD0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Name=GMPR2 {ECO:0000313|RefSeq:XP_007537619.1};
GN Synonyms=GMPR {ECO:0000256|HAMAP-Rule:MF_03195};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007537619.1};
RN [1] {ECO:0000313|RefSeq:XP_007537619.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|HAMAP-
CC Rule:MF_03195, 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 RefSeq; XP_007537619.1; XM_007537557.2.
DR AlphaFoldDB; A0A1S3AMD0; -.
DR STRING; 9365.ENSEEUP00000010640; -.
DR GeneID; 103126644; -.
DR CTD; 51292; -.
DR eggNOG; KOG2550; Eukaryota.
DR InParanoid; A0A1S3AMD0; -.
DR OrthoDB; 5472229at2759; -.
DR Proteomes; UP000079721; Unplaced.
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:SF4; GMP REDUCTASE 2; 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|HAMAP-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:UP000079721}.
FT DOMAIN 10..339
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 348 AA; 37858 MW; E744871C6E780661 CRC64;
MPHIDNDIKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQQYTGIPV IAANMDTVGT
FEMAKALCQF SLFTAVHKHY NLEQWQEFAS QNPDCLEHLA ASSGTGSSDF EQLECILEAV
PQVKYICLDV ANGYSEHFVE FVKGVRRRFP QHTIMAGNVV TGEMVEELIL SGADIIKVGI
GPGSVCTTRR KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM
LGGMLAGHKE SGGELIERDG KKYKLFYGMS SEMAMKKYAG GVADYRASEG KTVEVPFKGE
VAHTIKDILG GIRSTCTYVG AAKLKELSRR TTFIRVTQQV NPVFSDAS
//
