ID   A0A1H7J199_9LACT        Unreviewed;       343 AA.
AC   A0A1H7J199;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=SAMN04488099_10552 {ECO:0000313|EMBL:SEK68509.1};
OS   Alkalibacterium pelagium.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alkalibacterium.
OX   NCBI_TaxID=426702 {ECO:0000313|EMBL:SEK68509.1, ECO:0000313|Proteomes:UP000199081};
RN   [1] {ECO:0000313|Proteomes:UP000199081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19183 {ECO:0000313|Proteomes:UP000199081};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNZU01000005; SEK68509.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7J199; -.
DR   STRING; 426702.SAMN04488099_10552; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000199081; 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:UP000199081}.
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   343 AA;  37764 MW;  D26CFFE258A2D320 CRC64;
     MKVFDYEDIQ LIPAKSIVRS RSECDTSITL GKHTFAMPVV PANMQTVVDE ELSIWLAENN
     YFYVMHRFEE ETRINFIRTM HDRGLYASIS LGVKTDEYDF VKELAEKDLA PDYITIDVAH
     GHSDLVIDMI RHVKHHLPET FLIAGNVGTP EAVRELENAG ADATKVGIGP GKVCTTKLKT
     GFGTGGWQLA ALSHCSKAAR KPLIADGGIR THGDIAKSIR FGATMVMIGS LFAGHDQSPG
     KMVTIDGRPY KEYFGSASSH QKGERKNVEG KKMLTEYKGD IADTLLEMKQ DLQSSISYAG
     GNDIESLRKV DYVIVKNSIM NGENYNASGI DVPDSFASSN FTS
//