ID I7KGC3_9LACO Unreviewed; 330 AA.
AC I7KGC3;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=BN55_06195 {ECO:0000313|EMBL:CCI81145.1};
OS Lactobacillus hominis DSM 23910 = CRBIP 24.179.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1423758 {ECO:0000313|EMBL:CCI81145.1, ECO:0000313|Proteomes:UP000009320};
RN [1] {ECO:0000313|EMBL:CCI81145.1, ECO:0000313|Proteomes:UP000009320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRBIP 24.179T {ECO:0000313|Proteomes:UP000009320};
RA Cousin S., Ma L., Bizet C., Loux V., Bouchier C., Clermont D., Creno S.;
RT "Draft Genome Sequence of Lactobacillus hominis Strain CRBIP 24.179T,
RT isolated from human intestine.";
RL Submitted (JUN-2012) 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:CCI81145.1}.
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DR EMBL; CAKE01000002; CCI81145.1; -; Genomic_DNA.
DR RefSeq; WP_008469787.1; NZ_CAKE01000002.1.
DR AlphaFoldDB; I7KGC3; -.
DR STRING; 1423758.FC41_GL001420; -.
DR GeneID; 82846422; -.
DR eggNOG; COG0516; Bacteria.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000009320; 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}.
FT DOMAIN 10..314
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 180
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
FT BINDING 209..232
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
SQ SEQUENCE 330 AA; 36588 MW; AC0B1E287C0BB420 CRC64;
MSNYFSMEAF DYDDIQLVPN KCIIKSRKEA DTSVKFGNRT FKIPVVPANM ESVIDEKLAI
WLAENDYYYV MHRFYPEKRA NFIKMMHDKG LFASISVGIK DSEYDFIDQL AKENLVPEYI
TIDVAHGHSN FVIKMIKYIK DKLPDSFLTA GNIATPEAVR ELENAGADAT KVGVGPGRAC
ITKLKTGFGT GGWQLAALRM CSKAASKPLI ADGGIRHNGD IAKSVRFGAS MVMIGSLFAG
HEESPGNIIK IDGKTYKQYW GSASEVQKGA YRNVEGKQML VPYRGSIKDT LQEMQEDLQS
SISYAGGKDL NAIRLVDYVI VKSSIMDGDK
//
