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Database: UniProt
Entry: A0A0L0QRJ7_VIRPA
LinkDB: A0A0L0QRJ7_VIRPA
Original site: A0A0L0QRJ7_VIRPA 
ID   A0A0L0QRJ7_VIRPA        Unreviewed;       328 AA.
AC   A0A0L0QRJ7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=AFK71_05955 {ECO:0000313|EMBL:KNE21229.1};
OS   Virgibacillus pantothenticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473 {ECO:0000313|EMBL:KNE21229.1, ECO:0000313|Proteomes:UP000036780};
RN   [1] {ECO:0000313|Proteomes:UP000036780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26 {ECO:0000313|Proteomes:UP000036780};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-10053 dsm26.";
RL   Submitted (JUL-2015) 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:KNE21229.1}.
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DR   EMBL; LGTO01000005; KNE21229.1; -; Genomic_DNA.
DR   RefSeq; WP_050350644.1; NZ_LGTO01000005.1.
DR   AlphaFoldDB; A0A0L0QRJ7; -.
DR   GeneID; 66873064; -.
DR   PATRIC; fig|1473.5.peg.4182; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000036780; 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:UP000036780}.
FT   DOMAIN          6..310
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
FT   ACT_SITE        175
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
FT   BINDING         204..227
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01511"
SQ   SEQUENCE   328 AA;  36182 MW;  9FD4948139340846 CRC64;
     MDNVFDYEDI QLIPAKCIVR SRSECDTSVT LGKHTFKLPV VPANMKTIID EKIALMLAEN
     GYFYIMHRFE PEKRAEFIKD MHARGLIASI SVGVKDEEYD FVKQLAADKL IPEYITIDIA
     HGHSESVIKM IKHIKKHLAE SFLIAGNVGT PEAVRELENA GADATKVGIG PGKVCITKIK
     TGFGTGGWQL AALRWCSRAA SKPIIADGGI RTHGDIAKSI RFGATMVMIG SLFAGHEESP
     GETIEKDGKI LKEYFGSASE FQKGERKNVE GKKMLVEHKG SLKDTLQEME QDLQSSISYA
     GGKKLEAIRT VDYVVVKNSI FNGDKIVY
//
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