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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//