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Database: UniProt
Entry: A0A133XT17_9BACT
LinkDB: A0A133XT17_9BACT
Original site: A0A133XT17_9BACT 
ID   A0A133XT17_9BACT        Unreviewed;       500 AA.
AC   A0A133XT17;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Inosine 5-monophosphate dehydrogenase {ECO:0000313|EMBL:KXB34081.1};
GN   ORFNames=HMPREF1869_01317 {ECO:0000313|EMBL:KXB34081.1};
OS   Bacteroidales bacterium KA00251.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1497953 {ECO:0000313|EMBL:KXB34081.1, ECO:0000313|Proteomes:UP000070662};
RN   [1] {ECO:0000313|EMBL:KXB34081.1, ECO:0000313|Proteomes:UP000070662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00251 {ECO:0000313|EMBL:KXB34081.1,
RC   ECO:0000313|Proteomes:UP000070662};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053;
CC         EC=1.1.1.205; Evidence={ECO:0000256|ARBA:ARBA00024264};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
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:KXB34081.1}.
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DR   EMBL; LSCS01000087; KXB34081.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133XT17; -.
DR   STRING; 1497953.HMPREF1869_01317; -.
DR   PATRIC; fig|1497953.3.peg.1300; -.
DR   OrthoDB; 9805398at2; -.
DR   Proteomes; UP000070662; Unassembled WGS sequence.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
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; IPR015875; IMP_DH/GMP_Rdtase_CS.
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; PF00571; CBS; 1.
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; 1.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000130-3};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070662}.
FT   DOMAIN          169..227
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        322
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT   ACT_SITE        421
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT   BINDING         264..266
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         315..317
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         317
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         319
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         322
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   500 AA;  55656 MW;  15ABE1E21365C6C1 CRC64;
     MAHFLKDTSH TFGEYLLIPG LTTEESTPDR IQLRTPLAKF KPSEEKQSRI NLNIPFVSAI
     MQSVSNHTLA IELARNGGLS FIFSSQPIDK QVEMVRKVKK FKAGFVVSDS NLRPDQTLRD
     VLELTRETGH STIGITDDGT PNGILKGMVT GRDYRLSTDS LDRRIEEFMT PFSKLVYGKK
     GMTLSEANDI IWNHKLNSLP VIDEEGRLLY FVFRKDYDNH KENPLELSHP EDKTLMVGAG
     INSRDYEERV PALIAEGVDA LCIDSSDGYS VWQAKTLDWI RKKYGDEVIV GAGNVVDAEG
     FRFLVNHGAD FVKVGIGGGS ICITREQKGI GRGQASAVID VANARDEYYR ETGIYIPICS
     DGGIVHDYHM VLALAMGADF LMMGRYFARF DESPTQKLKI NGNMVKEYWG EGSNRAKNWQ
     RYDTGGIADK TMKFEEGVDS YVPYAGPMKE NLDQTLSKIR STMSSCGTAT LSELRENAKI
     TLVSATSIVE GGAHDVIQKE
//
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