ID A0A1I3BNU1_9LACT Unreviewed; 324 AA.
AC A0A1I3BNU1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN04489868_10821 {ECO:0000313|EMBL:SFH63913.1};
OS Pisciglobus halotolerans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae.
OX NCBI_TaxID=745365 {ECO:0000313|EMBL:SFH63913.1, ECO:0000313|Proteomes:UP000198668};
RN [1] {ECO:0000313|EMBL:SFH63913.1, ECO:0000313|Proteomes:UP000198668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27630 {ECO:0000313|EMBL:SFH63913.1,
RC ECO:0000313|Proteomes:UP000198668};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOQE01000008; SFH63913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3BNU1; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000198668; 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:UP000198668}.
FT DOMAIN 5..309
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 174
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
FT BINDING 203..226
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
SQ SEQUENCE 324 AA; 36043 MW; 981AD5C79E8FD400 CRC64;
MRIFDYEDVQ LIPNKSIVRS RSECDTHMAF GDRTFKMPVV PANMQTVIDE ELAEKLAADG
YFYIMHRFDE ESRLPFVQKM HEKGLFASIS VGVKEKEYDF VNTLAEKNLL PEYITIDIAH
GHSQSVIDMI QHIKKQLPEA FVIAGNVATP EAVRELENAG ADATKVGVGP GKVCITKLKT
GFGTGGWQLS ALRWCSKAAR KPLIADGGVR DHGDIAKSIR FGASMVMIGS LFAGHEESPG
KTIEKDGKKY KEYFGSASEY QKGERKNVEG KKILLEHKGS IEDTLTEMQQ DLQSSISYAG
GRDVESIRKV DYVIVKNSIF NGDR
//
