ID C5K5U0_PERM5 Unreviewed; 300 AA.
AC C5K5U0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=GMP reductase {ECO:0000256|ARBA:ARBA00015800};
DE EC=1.7.1.7 {ECO:0000256|ARBA:ARBA00012678};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|ARBA:ARBA00030699};
GN ORFNames=Pmar_PMAR016329 {ECO:0000313|EMBL:EER20153.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER20153.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) 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}.
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};
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DR EMBL; GG670783; EER20153.1; -; Genomic_DNA.
DR RefSeq; XP_002788357.1; XM_002788311.1.
DR AlphaFoldDB; C5K5U0; -.
DR EnsemblProtists; EER20153; EER20153; Pmar_PMAR016329.
DR GeneID; 9053668; -.
DR InParanoid; C5K5U0; -.
DR OrthoDB; 5472229at2759; -.
DR Proteomes; UP000007800; Unassembled WGS sequence.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR GO; GO:0006144; P:purine nucleobase metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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: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 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000235-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000235-3};
KW Purine metabolism {ECO:0000256|ARBA:ARBA00022631};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT DOMAIN 13..234
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT REGION 240..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000235-1"
FT BINDING 75
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 77
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|PIRSR:PIRSR000235-3"
SQ SEQUENCE 300 AA; 31890 MW; E2FCF12B8D35C1A7 CRC64;
MKDDLIKLKS VMEISKANFI CLDVANGYAE AFVEAVRTLR KDYPDKVIMA GNVVTGEMCE
ELLLSGADIV KVGIGPGSVC TTRKMTGVGY PQLSAVIECA DAAHGIGGMI ISDGGCTCSG
DVCKAFGGGA DFVMLGGMLA GHDESGGQLV HDVRSEKWYK EFYGMSSDTA MNKYAGGVAN
YRASEGKSVK VPYRGPVSHT IQDVLGGLRS CCTYVGARAL KELSKRTTFV RVTQQLNPVF
DHAPAAPQPP KAPPQPTVAA AKEAHETESE GAPSPKRARS GSLGSPRHHR HESNSPRHRH
//
