ID A0A0G0HAE9_9BACT Unreviewed; 396 AA.
AC A0A0G0HAE9;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000313|EMBL:KKQ35520.1};
GN ORFNames=US51_C0003G0005 {ECO:0000313|EMBL:KKQ35520.1};
OS Microgenomates group bacterium GW2011_GWA2_37_6.
OC Bacteria.
OX NCBI_TaxID=1618497 {ECO:0000313|EMBL:KKQ35520.1, ECO:0000313|Proteomes:UP000034211};
RN [1] {ECO:0000313|EMBL:KKQ35520.1, ECO:0000313|Proteomes:UP000034211}
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 -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC {ECO:0000256|ARBA:ARBA00005502}.
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:KKQ35520.1}.
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DR EMBL; LBTG01000003; KKQ35520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0HAE9; -.
DR PATRIC; fig|1618497.3.peg.34; -.
DR Proteomes; UP000034211; 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 CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 2.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW Potassium {ECO:0000256|PIRSR:PIRSR000130-4}.
FT DOMAIN 11..384
FT /note="IMP dehydrogenase/GMP reductase"
FT /evidence="ECO:0000259|Pfam:PF00478"
FT BINDING 138..140
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 188..190
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 190
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 192
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 195
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 396 AA; 42000 MW; F0878BF6DD335E93 CRC64;
MDRKKISFPL ALTFDDILLL PGYAGFSRSD ISLETKLTKN ISLKLPFVSA PMDTVTESEL
AIELARLGGI GIIHRNLTVA KQASEVEKVL KTRSATPSKG GQAGQEGLIV GAAVGAGTGF
EERVEALIRA RVSVIVVDSA HGFSKQVIDA TKYISKKYPK MEIIAGNIAT ADGAKALIDA
GADGLRVGMG PGAICTTRVI SGMGVPQVTA LMDTVRVAKK YGVPVIADGG IKYSGDMVKA
LALGASTVMM GSFFASCAEA PGTKVRLLRE QVPSRFQSIF EKNKKTYLFK SYRGMGSTGA
MQKGAKIKSE GEFHGKSYKD RVLIAEGVEG LVPVKGSVKE LTDQAVGGIK SGMYYVGAKD
LNELTKNARF TQITQASLTE SHPHSVLITN AGENYQ
//
