ID A0A0R1UNS2_9LACO Unreviewed; 324 AA.
AC A0A0R1UNS2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=FC21_GL000956 {ECO:0000313|EMBL:KRL94913.1};
OS Limosilactobacillus equigenerosi DSM 18793 = JCM 14505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1423742 {ECO:0000313|EMBL:KRL94913.1, ECO:0000313|Proteomes:UP000051084};
RN [1] {ECO:0000313|EMBL:KRL94913.1, ECO:0000313|Proteomes:UP000051084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18793 {ECO:0000313|EMBL:KRL94913.1,
RC ECO:0000313|Proteomes:UP000051084};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL94913.1}.
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DR EMBL; AZGC01000026; KRL94913.1; -; Genomic_DNA.
DR RefSeq; WP_056995468.1; NZ_AZGC01000026.1.
DR AlphaFoldDB; A0A0R1UNS2; -.
DR STRING; 417373.GCA_001570685_00293; -.
DR PATRIC; fig|1423742.4.peg.997; -.
DR OrthoDB; 9805398at2; -.
DR Proteomes; UP000051084; 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:UP000051084}.
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; 35331 MW; 6EA7AE3D93824EA5 CRC64;
METFDYDDIQ LIPNKCVIKS RSEAGTTVKF GPRTFKLPVV PANMASVIDE TVAIWLAEND
YYYVMHRFEP ADRLAFVQRM HDRGLYASIS VGIKASEYQL IDELAAQNLV PEYITIDVAH
GHSEYVIQMI KYIKESLPDS FVTAGNVATP EAVRDLENAG ADATKVGVGP GKACITKLKT
GFGTGGWQLA ALRLCSKAAR KPLIADGGIR HHGDIAKSVR FGASMVMIGS LLAGHLESPG
QLITIDGKQY KQYWGSASET QKGAYRNVEG KQMLVPFKGS LADTLVEMQE DLQSSISYAG
GRDLAAITKV DYVVVKNSIL NGDY
//
