ID B3QA52_RHOPT Unreviewed; 347 AA.
AC B3QA52;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_00596};
DE EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_00596};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00596};
DE Short=Guanosine monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_00596};
GN Name=guaC {ECO:0000256|HAMAP-Rule:MF_00596};
GN OrderedLocusNames=Rpal_5041 {ECO:0000313|EMBL:ACF03530.1};
OS Rhodopseudomonas palustris (strain TIE-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=395960 {ECO:0000313|EMBL:ACF03530.1, ECO:0000313|Proteomes:UP000001725};
RN [1] {ECO:0000313|EMBL:ACF03530.1, ECO:0000313|Proteomes:UP000001725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TIE-1 {ECO:0000313|EMBL:ACF03530.1,
RC ECO:0000313|Proteomes:UP000001725};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA Newman D.K., Roden E., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL Submitted (MAY-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, ECO:0000256|HAMAP-Rule:MF_00596}.
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_00596};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00596}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00596}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00596}.
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DR EMBL; CP001096; ACF03530.1; -; Genomic_DNA.
DR RefSeq; WP_012497723.1; NC_011004.1.
DR AlphaFoldDB; B3QA52; -.
DR KEGG; rpt:Rpal_5041; -.
DR HOGENOM; CLU_022552_5_3_5; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000001725; Chromosome.
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: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 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_00596,
KW ECO:0000256|PIRSR:PIRSR000235-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00596};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00596};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00596}.
FT DOMAIN 9..338
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 182
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-1"
FT BINDING 177
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 179
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596,
FT ECO:0000256|PIRSR:PIRSR000235-3"
FT BINDING 212..235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00596"
SQ SEQUENCE 347 AA; 37311 MW; 5281A85BBEF1B971 CRC64;
MHIDLNPKLD FRDVLIRPKR SVLSSRFEAN IKRSLRFRHS SRAWTGFPLI ASNMDTIGTL
EMAKAFKPFG ALVALHKFHH PDRLAEYLAG DEDANVFVTV GTGSADWERL AAVKAKVKVP
MLNIDVANGY TEAFVRAVAR LRDENPDAII MAGTVVTAEM TEALVLAGAD IVRVGIGSGS
VCTTRDLTGV GYPQLSAVIE CADAAHGLKG HVCSDGGCVV PGDLAKAYGG GADFVMLGGM
LAGHDECGGE LRYAEQNGQK TPTSMVFYGM SSETAMNKYH GGVADYRAAE GKTVEVPYRG
EVHATVEKIA GGLRSAMTYI GAENLKEIPK RTTFILVNAQ RNTVFDR
//
