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Database: UniProt
Entry: M3W4C4_FELCA
LinkDB: M3W4C4_FELCA
Original site: M3W4C4_FELCA 
ID   M3W4C4_FELCA            Unreviewed;       315 AA.
AC   M3W4C4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   24-JAN-2024, entry version 65.
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|Ensembl:ENSFCAP00000005191.4,
GN   ECO:0000313|VGNC:VGNC:62613};
GN   Synonyms=GMPR {ECO:0000256|HAMAP-Rule:MF_03195};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000005191.4, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000005191.4, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005191.4,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000005191.4, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005191.4,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000005191.4}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000005191.4};
RG   Ensembl;
RL   Submitted (SEP-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}.
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};
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03195}.
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DR   EMBL; AANG04001761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3W4C4; -.
DR   Ensembl; ENSFCAT00000005594.6; ENSFCAP00000005191.4; ENSFCAG00000005592.6.
DR   VGNC; VGNC:62613; GMPR2.
DR   eggNOG; KOG2550; Eukaryota.
DR   GeneTree; ENSGT00940000159574; -.
DR   HOGENOM; CLU_022552_5_3_1; -.
DR   Proteomes; UP000011712; Chromosome B3.
DR   Bgee; ENSFCAG00000005592; Expressed in eyeball of camera-type eye and 10 other cell types or tissues.
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; 2.
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   PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR   PANTHER; PTHR43170:SF4; GMP REDUCTASE 2; 1.
DR   Pfam; PF00478; IMPDH; 2.
DR   PIRSF; PIRSF000235; GMP_reductase; 2.
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:UP000011712}.
FT   DOMAIN          10..84
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
FT   DOMAIN          115..306
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
FT   ACT_SITE        153
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03195,
FT                   ECO:0000256|PIRSR:PIRSR000235-1"
FT   ACT_SITE        155
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         147..148
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         148
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         150
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         153
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03195"
FT   BINDING         156
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03195"
FT   BINDING         186..188
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03195"
FT   BINDING         209..210
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03195"
FT   BINDING         235..237
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03195"
FT   BINDING         236
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         252..253
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         253..257
FT                   /ligand="GMP"
FT                   /ligand_id="ChEBI:CHEBI:58115"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03195"
FT   BINDING         281..284
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   315 AA;  34068 MW;  8ECC91772FEF2C3D CRC64;
     MPHIDNDVKL DFKDVLLRPK RSTLKSRSEV DLTRSFSFRN SKQMYTGIPI IAANMDTVGT
     FEMAKVLCKF SLFTAVHKHY SLEQWKDFAS QNPDCLQHLA ASSGMGSSDF EQLEQILEAV
     PQAGNVVTGE MVEELILSGA DIIKVGIGPG SVCTTRKKTG VGYPQLSAVM ECADAAHGLK
     GHIISDGGCS CPGDVAKAFG AGADFVMLGG MLAGHNESGG ELIERDGKKY KLFYGMSSEM
     AMKKYAGGVA EYRASEGKTV EVPFKGDVDH TIRDILGGIR STCTYVGAAK LKELSRRTTF
     IRVTQQVNPI FSDDS
//
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