ID A0A0M4CNH9_LACPN Unreviewed; 325 AA.
AC A0A0M4CNH9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:ODO62933.1};
GN ORFNames=C7M40_02411 {ECO:0000313|EMBL:QHM50441.1}, Lp19_0280
GN {ECO:0000313|EMBL:KZU98396.1}, LPJSA22_02951
GN {ECO:0000313|EMBL:ODO62933.1}, LpLQ80_13990
GN {ECO:0000313|EMBL:AWI41577.1};
OS Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=1590 {ECO:0000313|EMBL:ODO62933.1, ECO:0000313|Proteomes:UP000094892};
RN [1] {ECO:0000313|EMBL:KZU98396.1, ECO:0000313|Proteomes:UP000076882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19.1 {ECO:0000313|EMBL:KZU98396.1,
RC ECO:0000313|Proteomes:UP000076882};
RA Martino M.E.;
RT "Comparative genomics of 54 Lactobacillus plantarum strains reveals genomic
RT uncoupling from niche constraints.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ODO62933.1, ECO:0000313|Proteomes:UP000094892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSA22 {ECO:0000313|EMBL:ODO62933.1,
RC ECO:0000313|Proteomes:UP000094892};
RA Choi H.S.;
RT "Genome sequencing of Lactobacillus plantarum JSA22, isolated from
RT fermented soybean paste.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QHM50441.1, ECO:0000313|Proteomes:UP000465032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM101518 {ECO:0000313|EMBL:QHM50441.1,
RC ECO:0000313|Proteomes:UP000465032};
RA Jeong D.-Y.;
RT "Lactobacillus plantatrum SRCM101518 having antimicrbial activity species
RT isolated from Korea kimchi.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AWI41577.1, ECO:0000313|Proteomes:UP000244922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LQ80 {ECO:0000313|EMBL:AWI41577.1,
RC ECO:0000313|Proteomes:UP000244922};
RA Moriya N., Nakano K., Shiroma A., Shinzato M., Ashimine N., Minami M.,
RA Tamotsu H., Shimoji M., Nakanishi T., Ohki S., Teruya K., Satou K.,
RA Hirano T., Hagi T., Kobayashi M., Nomura M., Kimoto H.N., Tajima K.,
RA Cai Y., Suzuki C.;
RT "Complete Genome Sequence of Lactobacillus plantarum Strain LQ80 Selected
RT for Preparation of Fermented Liquid Feed for Pig.";
RL Submitted (APR-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}.
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DR EMBL; CP028977; AWI41577.1; -; Genomic_DNA.
DR EMBL; LUXM01000005; KZU98396.1; -; Genomic_DNA.
DR EMBL; MCOL01000001; ODO62933.1; -; Genomic_DNA.
DR EMBL; CP028241; QHM50441.1; -; Genomic_DNA.
DR PATRIC; fig|1590.142.peg.2929; -.
DR OMA; AYKEYFG; -.
DR Proteomes; UP000076882; Unassembled WGS sequence.
DR Proteomes; UP000094892; Unassembled WGS sequence.
DR Proteomes; UP000244922; Chromosome.
DR Proteomes; UP000465032; 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: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 7..311
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT ACT_SITE 176
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
FT BINDING 205..228
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
SQ SEQUENCE 325 AA; 35432 MW; E19846BECA12DBE6 CRC64;
MGMEIFDYED IQLIPNKCVI NSRSEADTTV ELGGRRFKIP VVPANMATVI NDEIAKWLAT
NDYFYIMHRF APETRRAFIE TMHAAQLYAS ISVGVKSSEY DFIDDLATNQ IVPEYITIDI
AHGHADSVIA MIKHIKDVLP DSFVIAGNVA TPAAVRDLEN AGADATKVGV GPGKACITKV
KTGFGTGGWQ LAAVRWCAKA ARKPIIADGG VRTNGDIAKS IRFGATMVMI GSMLAGHQES
PGNILKIDGK TYKQYYGSAS ETQKGEHKNV EGKQMLVPYR GRLVDTLNEM QEDLQSSISY
AGGRDLKAIT KCDYVVVKNS IYNGD
//
