GMPR2_BOVIN
ID GMPR2_BOVIN Reviewed; 348 AA.
AC Q32L93;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=GMP reductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=GMPR 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_03195};
DE Short=Guanosine monophosphate reductase 2 {ECO:0000255|HAMAP-Rule:MF_03195};
GN Name=GMPR2 {ECO:0000255|HAMAP-Rule:MF_03195};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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 (Probable). Plays a role
CC in modulating cellular differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q9P2T1, ECO:0000255|HAMAP-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; BC109695; AAI09696.1; -; mRNA.
DR RefSeq; NP_001033208.1; NM_001038119.1.
DR AlphaFoldDB; Q32L93; -.
DR SMR; Q32L93; -.
DR STRING; 9913.ENSBTAP00000003519; -.
DR PaxDb; Q32L93; -.
DR PRIDE; Q32L93; -.
DR GeneID; 515837; -.
DR KEGG; bta:515837; -.
DR CTD; 51292; -.
DR eggNOG; KOG2550; Eukaryota.
DR InParanoid; Q32L93; -.
DR OrthoDB; 618077at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046037; P:GMP metabolic process; ISS:UniProtKB.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
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 Acetylation; Metal-binding; NADP; Oxidoreductase; Potassium;
KW Purine metabolism; Reference proteome.
FT CHAIN 1..348
FT /note="GMP reductase 2"
FT /id="PRO_0000253472"
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 219..221
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
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 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2T1"
SQ SEQUENCE 348 AA; 38033 MW; B4DA9AF8BC5474D2 CRC64;
MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFAFRN SKQMYTGIPI IAANMDTVGT
FEMAKVLCKF SLFTAVHKHY SLEQWKEFAS QNPDCLEHLA ASSGTGSSDF EQLEQILNAI
PQVKYVCLDV ANGYSEHFVE FVKDVRKRFP EHTIMAGNVV TGEMVEELIL SGADIIKVGI
GPGSVCTTRK KTGVGYPQLS AVMECADAAH GLKGHIISDG GCSCPGDVAK AFGAGADFVM
LGGMLAGHSE SGGELIERNG RKYKLFYGMS SEMAMKKYAG GVAEYRASEG KTVEVPFKGD
VEHTIRDIIG GIRSTCTYVG AAKQKELSRR TTFIRVTQQV KPIFSDES
