ID A0A0G1NN50_9BACT Unreviewed; 479 AA.
AC A0A0G1NN50;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GMP reductase {ECO:0000256|ARBA:ARBA00015800};
DE EC=1.7.1.7 {ECO:0000256|ARBA:ARBA00012678};
GN ORFNames=UX31_C0010G0007 {ECO:0000313|EMBL:KKU21876.1};
OS Candidatus Nomurabacteria bacterium GW2011_GWA1_46_11.
OC Bacteria; Candidatus Nomurabacteria.
OX NCBI_TaxID=1618732 {ECO:0000313|EMBL:KKU21876.1, ECO:0000313|Proteomes:UP000034107};
RN [1] {ECO:0000313|EMBL:KKU21876.1, ECO:0000313|Proteomes:UP000034107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU21876.1}.
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DR EMBL; LCLS01000010; KKU21876.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1NN50; -.
DR PATRIC; fig|1618732.3.peg.453; -.
DR Proteomes; UP000034107; Unassembled WGS sequence.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
DR CDD; cd02205; CBS_pair_SF; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005991; GUAB1.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01303; IMP_DH_rel_1; 1.
DR PANTHER; PTHR43170; GMP REDUCTASE; 1.
DR PANTHER; PTHR43170:SF5; GMP REDUCTASE; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS51371; CBS; 2.
PE 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Potassium {ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine salvage {ECO:0000256|ARBA:ARBA00022726}.
FT DOMAIN 95..152
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 154..214
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 246..248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 297..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 299
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 301
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 304
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
SQ SEQUENCE 479 AA; 52061 MW; 0B99AAE561147D78 CRC64;
MRFLHTEDEG KEVTYEDAFL VPQYSEVRSR MDVDITPPDE TGATIPIVVA NMTSAAGKRM
AETVTRRGGL VMLTQDMPLE KIKEVVMYLK TRHPVFETPV VLEESESVQT ALNLVHKRSH
GGIVIVDKEN KPVGIFTETD AKGKDRFTPL KNVMATDIIS SGENTTPEEA FEKLYQSHVS
LLPIIKNSGE LLGVMTKEGA VRSKIYKPAL NTKSEFITAV AMGVSNGTEE RAKALMDMGV
DIFMVDTAHG HSKRLIDAVK TVRHTIGKDK IIYAGTVVTA QGVEDLVNAG ANIVKVGIGS
GGSCITRVAT GNGRPQLSAT IECSKQARRM GAHIWADGGI RQPRDLALAI AAGAASTMFA
TIFVGTHESP GDIQRDEDGN LYKVNFGMAS GRAVRERFKD QKPIDLAMRQ YFEEGISEGK
IYLKEGTTGV EDIIDRLVAG LRSAMSYAGA TNLNEFHEKA IIGIQTNAAL KEGEPLLEH
//
