ID A0A024U0Q9_9STRA Unreviewed; 358 AA.
AC A0A024U0Q9;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=H310_08143 {ECO:0000313|EMBL:ETV99461.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV99461.1};
RN [1] {ECO:0000313|EMBL:ETV99461.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV99461.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) 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}.
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; KI913967; ETV99461.1; -; Genomic_DNA.
DR RefSeq; XP_008872017.1; XM_008873795.1.
DR AlphaFoldDB; A0A024U0Q9; -.
DR EnsemblFungi; H310_08143-t26_2; H310_08143-t26_2-p1; H310_08143.
DR EnsemblProtists; ETV99461; ETV99461; H310_08143.
DR GeneID; 20085193; -.
DR VEuPathDB; FungiDB:H310_08143; -.
DR OrthoDB; 5472229at2759; -.
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}.
FT DOMAIN 10..331
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 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 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; 38604 MW; 403CCC21BD8C4B08 CRC64;
MPRIETEPKL DFKDVLIRPK RSTLKSRSQV DVSRTYTFRN SKRTWTGVPV IAANMDTVGT
FEMARVLAAN QCITCIHKHY TVDEWHAFAK TYPSVLPFVA VSAGTSAADL ERVSAVLHAH
DAIAFVCLDV ANGYSEHFVD AVRSVRANHP THTIIAGNVV TGEMVEELVL SGADIIKIGI
GPGSVCTTRK QTGVGYPQLS AVLECADAAH GLRGHVISDG GCTCPGDVAK AFGAGADFVM
LGGMLAGHDE SGGDVIETSD GRIFKRFYGM SSATAMKKHA GGVAEYRSSE GKSVTVPYRG
PVDNTIKDIL GGVRSTCTYV GASMLKELSK VRHWRLRPSQ RNSSLTALWR CSERLLFV
//
