GMPR_ASCSU
ID GMPR_ASCSU Reviewed; 356 AA.
AC P27442;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=GMP reductase;
DE EC=1.7.1.7;
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase;
DE Short=Guanosine monophosphate reductase;
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1620164; DOI=10.1016/0166-6851(92)90059-s;
RA Gruidl M.E., Bunch K., Gharib S., Bennett K.L.;
RT "The GMP reductase gene of the nematode Ascaris lumbricoides var. suum.";
RL Mol. Biochem. Parasitol. 52:271-274(1992).
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 -!- 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 -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000305}.
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DR EMBL; M82838; AAA29373.1; -; mRNA.
DR AlphaFoldDB; P27442; -.
DR SMR; P27442; -.
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; -; 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 Metal-binding; NADP; Oxidoreductase; Potassium; Purine metabolism.
FT CHAIN 1..356
FT /note="GMP reductase"
FT /id="PRO_0000093728"
FT ACT_SITE 189
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 191
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
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:0000250"
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:0000250"
FT BINDING 132..134
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:0000250"
FT BINDING 183..184
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:0000250"
FT BINDING 184
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 222..224
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 245..246
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 271..273
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 272
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:0000250"
FT BINDING 288..289
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:0000250"
FT BINDING 289..293
FT /ligand="GMP"
FT /ligand_id="ChEBI:CHEBI:58115"
FT /evidence="ECO:0000250"
FT BINDING 317..320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 39252 MW; 2D1B4F1B64EFB26A CRC64;
MPRIEFEPKL DFKDVLLRPK RSTLRSRAEV DLMREYVFRN SKKTYVGVPV VASNMDTVGT
FEMAEVLAKF SLFTTIHKHY QVDEWKAFVQ RVDSNPQIMS QIGISSGIST SDFDKLRTVC
DMIPELEYIC LDVANGYSEV FVDFIRRVRE QFPTHTIFAG NVVTGEMVEE LILSGADVVK
VGIGPGSVCT TRKKAGVGYP QLSAVLECAD ASHGLNGHVM SDGGCTNPGD VAKAFGGGAD
FVMIGGLLAG HDQCGGEVVE KDGKKYKLFY GMSSDTAMKK YQGSVAEYRA SEGKTIYMPY
RGDVSRTIHD LLGGLRSACT YIGATKLKEL SKRATFVRVT QQTNDQYSAY EVPRID
