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Database: UniProt
Entry: W7C992_9LIST
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ID   W7C992_9LIST            Unreviewed;       225 AA.
AC   W7C992;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=GMP reductase {ECO:0000256|ARBA:ARBA00015800};
DE            EC=1.7.1.7 {ECO:0000256|ARBA:ARBA00012678};
DE   AltName: Full=Guanosine 5'-monophosphate oxidoreductase {ECO:0000256|ARBA:ARBA00030699};
GN   ORFNames=BCAMP_11035 {ECO:0000313|EMBL:EUJ36029.1};
OS   Brochothrix campestris FSL F6-1037.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX   NCBI_TaxID=1265861 {ECO:0000313|EMBL:EUJ36029.1, ECO:0000313|Proteomes:UP000019243};
RN   [1] {ECO:0000313|EMBL:EUJ36029.1, ECO:0000313|Proteomes:UP000019243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL F6-1037 {ECO:0000313|EMBL:EUJ36029.1,
RC   ECO:0000313|Proteomes:UP000019243};
RA   den Bakker H.C., Allred A., Warchocki S., Wright E.M., Burrell A.,
RA   Nightingale K.K., Kephart D., Wiedmann M.;
RT   "Novel taxa of Listeriaceae from agricultural environments in the United
RT   States.";
RL   Submitted (DEC-2012) 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}.
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};
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:EUJ36029.1}.
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DR   EMBL; AODH01000049; EUJ36029.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7C992; -.
DR   STRING; 1265861.BCAMP_11035; -.
DR   PATRIC; fig|1265861.3.peg.2172; -.
DR   Proteomes; UP000019243; Unassembled WGS sequence.
DR   GO; GO:0003920; F:GMP reductase activity; IEA:UniProtKB-EC.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR   PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR   Pfam; PF00478; IMPDH; 1.
DR   SMART; SM01240; IMPDH; 1.
DR   SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   4: Predicted;
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:EUJ36029.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019243}.
FT   DOMAIN          12..210
FT                   /note="IMP dehydrogenase/GMP reductase"
FT                   /evidence="ECO:0000259|Pfam:PF00478"
SQ   SEQUENCE   225 AA;  24142 MW;  28EC37D0C98B22BF CRC64;
     MEQLASSQLV PDYVTIDIAH GHSNAVIHMI QHLKKHLPET FVIAGNVGTP EAVRELENAG
     ADATKVGIGP GKVCITKIKT GFGTGGWQLA ALRWCAKAAS KPIIADGGIR TNGDIAKSVR
     FGASMVMIGS LFAAHNESPG STIEIAGKFY KEYFGSASEF QKGEKKNVEG KKMHVENKGN
     LKDTLIEMQQ DLQSAISYSG GTKLEAIRNV DYVVVKNSIF NGDNH
//
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