ID A0A3E1RBW1_9BURK Unreviewed; 325 AA.
AC A0A3E1RBW1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=GMP reductase {ECO:0000256|HAMAP-Rule:MF_01511};
DE EC=1.7.1.7 {ECO:0000256|HAMAP-Rule:MF_01511};
DE AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01511};
DE Short=Guanosine monophosphate reductase {ECO:0000256|HAMAP-Rule:MF_01511};
GN Name=guaC {ECO:0000256|HAMAP-Rule:MF_01511};
GN ORFNames=DIC66_10080 {ECO:0000313|EMBL:RFO96848.1};
OS Rhodoferax lacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2184758 {ECO:0000313|EMBL:RFO96848.1, ECO:0000313|Proteomes:UP000260665};
RN [1] {ECO:0000313|EMBL:RFO96848.1, ECO:0000313|Proteomes:UP000260665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26218 {ECO:0000313|EMBL:RFO96848.1,
RC ECO:0000313|Proteomes:UP000260665};
RA Park M.;
RT "Rhodoferax soyangensis sp.nov., isolated from an oligotrophic freshwater
RT lake.";
RL Submitted (MAY-2018) 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_01511}.
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_01511};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. GuaC type 2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01511}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFO96848.1}.
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DR EMBL; QFZK01000005; RFO96848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1RBW1; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000260665; Unassembled WGS sequence.
DR GO; GO:1902560; C:GMP reductase complex; IEA:InterPro.
DR GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-UniRule.
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_01511; GMP_reduct_type2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005994; GuaC_type_2.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01306; GMP_reduct_2; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF036500; GMP_red_Firmic; 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 NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01511};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01511}; Reference proteome {ECO:0000313|Proteomes:UP000260665}.
FT DOMAIN 5..311
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 173
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
FT BINDING 202..225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
SQ SEQUENCE 325 AA; 35618 MW; 8D10344A1D5C6B99 CRC64;
MEIFDYDNIL LLPRKCRVES RSECDAGVEL GGRTFRLPVV PANMKTVVDE TICIWLAQNG
YFYVMHRFDL DNVQFTADMH AKGLYASISL GVKKPDYDTV DQLLAKGLIP EYITIDIAHG
HADSVKNMIE YLKAKMPASF IIAGNVGTPE AVIDLENWGA DATKVGIGPG KVCITKLKTG
FGTGGWQLSA LKWCARVATK PIIADGGIRD HGDIAKSVRF GASMVMIGSL FAGHEESPGQ
TVEVDGRLYK EYYGSASDFN KGEYKHVEGK RILEPIKGKL ADTLIEMEQD VQSSISYSGG
KKLMDIRKVN YVTLGGTNAA EHLLM
//
