ID A0A0G0HFZ3_9BACT Unreviewed; 477 AA.
AC A0A0G0HFZ3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000313|EMBL:KKQ41087.1};
GN ORFNames=US58_C0005G0012 {ECO:0000313|EMBL:KKQ41087.1};
OS Candidatus Magasanikbacteria bacterium GW2011_GWA2_37_8.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1619036 {ECO:0000313|EMBL:KKQ41087.1, ECO:0000313|Proteomes:UP000034333};
RN [1] {ECO:0000313|EMBL:KKQ41087.1, ECO:0000313|Proteomes:UP000034333}
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, ECO:0000256|RuleBase:RU003927}.
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:KKQ41087.1}.
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DR EMBL; LBTN01000005; KKQ41087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0HFZ3; -.
DR STRING; 1619036.US58_C0005G0012; -.
DR PATRIC; fig|1619036.3.peg.145; -.
DR Proteomes; UP000034333; 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; cd04601; CBS_pair_IMPDH; 1.
DR CDD; cd00381; IMPDH; 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; IPR005990; IMP_DH.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01302; IMP_dehydrog; 1.
DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 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 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; NAD {ECO:0000256|PIRSR:PIRSR000130-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003927};
KW Potassium {ECO:0000256|PIRSR:PIRSR000130-4}.
FT DOMAIN 93..149
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 153..211
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT BINDING 248..250
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 298..300
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 300
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 302
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 305
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 477 AA; 51187 MW; B4D4838994E526DB CRC64;
MLSIPLALTY DDVLIVPKRS SLTSRSEANT TTRLTKKLNL NIPIVTSNMD TVTESDMAIA
LARLGGIGIL HRFMTIEENA EEVKRVKRAQ NFIVNDPYTI DPEKSVAEAK AYAASIGITG
LMVSNGDRKL RGILSRRDFL FSNGDNKKVS EIMTPREKLI VGHAHTTFNE AKQIFSEHKI
EKLPLVDSED RIVGIITSDD IKHIIDYPLS NCDDDGQLIV GASVGVQGDF VERAEELVKA
GVDVIVIDIA HGHSDAMFKA IAKLREAIGD TQLIAGNIAT ASAALELCEA GVDGLKVGVG
PGTICITRLV TGCGMPQLTA VMETSRIAKR YGVPIIADGG IQRSGDIVKA IGAGADTVMM
GGMFAGTEES PGVVMTKGDR KFKICRGSAS FTVANQRRLI KQSAKEVKEI IPEGVESIVP
FKGPVTDIVN QLIGGLKSGM SYTNSHTIAE LQKNVEFVRM TNAGLKESGS HDVQAIT
//