ID G9ZLN9_9LACO Unreviewed; 323 AA.
AC G9ZLN9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=HMPREF9103_00637 {ECO:0000313|EMBL:EHM00269.1};
OS Lentilactobacillus parafarraginis F0439.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=797515 {ECO:0000313|EMBL:EHM00269.1, ECO:0000313|Proteomes:UP000004625};
RN [1] {ECO:0000313|EMBL:EHM00269.1, ECO:0000313|Proteomes:UP000004625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0439 {ECO:0000313|EMBL:EHM00269.1,
RC ECO:0000313|Proteomes:UP000004625};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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:EHM00269.1}.
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DR EMBL; AGEY01000028; EHM00269.1; -; Genomic_DNA.
DR RefSeq; WP_008211196.1; NZ_JH414926.1.
DR AlphaFoldDB; G9ZLN9; -.
DR STRING; 797515.HMPREF9103_00637; -.
DR PATRIC; fig|797515.3.peg.592; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_5_0_9; -.
DR Proteomes; UP000004625; 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 5..310
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 323 AA; 35921 MW; 38EA7D8F6DA4DBBE CRC64;
MEVFDYEDIQ LIPNKCIIKS RSDADTSIKF GPRTFKIPVV PANMETVIND DLAIWLAQNG
YFYIMHRFQP EKREGFIKMM HEKDLYASIS VGIKDDEYKF IDQLVADNQK PEYITIDVAH
GHSDFVIQMI HYIKDKLPDS FLIAGNLGTP EAVREIENAG ADATKIGIGP GKACITKLKT
GFGTGGWQLA ALRLCSKAAR KPMIADGGIR FNGDIAKSVR FGASMVMIGS LLAGHEQSPG
NVISIDGKKY KQYWGSASEK QKGAYRNVEG RQMLVPYRGE ISDTLFEMQQ DLQSSISYAG
GKELKDIRTV DYVVVKNSIM NGD
//
