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Database: UniProt
Entry: A0A0J5P2P0_9PAST
LinkDB: A0A0J5P2P0_9PAST
Original site: A0A0J5P2P0_9PAST 
ID   A0A0J5P2P0_9PAST        Unreviewed;       488 AA.
AC   A0A0J5P2P0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
DE            Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964};
DE            Short=IMPD {ECO:0000256|HAMAP-Rule:MF_01964};
DE            Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_01964};
DE            EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
GN   Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964};
GN   ORFNames=RO21_10000 {ECO:0000313|EMBL:KMK50753.1};
OS   Muribacter muris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Muribacter.
OX   NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK50753.1, ECO:0000313|Proteomes:UP000036270};
RN   [1] {ECO:0000313|EMBL:KMK50753.1, ECO:0000313|Proteomes:UP000036270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK50753.1,
RC   ECO:0000313|Proteomes:UP000036270};
RA   Christensen H., Nicklas W., Bisgaard M.;
RT   "Reclassification of Actinobacillus muris as Muribacter muris.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to
CC       xanthosine 5'-phosphate (XMP), the first committed and rate-limiting
CC       step in the de novo synthesis of guanine nucleotides, and therefore
CC       plays an important role in the regulation of cell growth.
CC       {ECO:0000256|HAMAP-Rule:MF_01964}.
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         ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958,
CC         ECO:0000256|HAMAP-Rule:MF_01964};
CC   -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC       inhibitor that prevents formation of the closed enzyme conformation by
CC       binding to the same site as the amobile flap. In contrast, mizoribine
CC       monophosphate (MZP) is a competitive inhibitor that induces the closed
CC       conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor
CC       inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of
CC       bacterial IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964,
CC       ECO:0000256|RuleBase:RU003928}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC       {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_01964,
CC       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:KMK50753.1}.
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DR   EMBL; JWIZ01000071; KMK50753.1; -; Genomic_DNA.
DR   RefSeq; WP_047977640.1; NZ_JWIZ01000071.1.
DR   AlphaFoldDB; A0A0J5P2P0; -.
DR   STRING; 67855.RO21_10000; -.
DR   PATRIC; fig|67855.3.peg.2118; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000036270; Unassembled WGS sequence.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04601; CBS_pair_IMPDH; 1.
DR   CDD; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01964; IMPDH; 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   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.
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};
KW   GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP-
KW   Rule:MF_01964};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01964};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01964};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003927};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01964};
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01964}; Reference proteome {ECO:0000313|Proteomes:UP000036270}.
FT   DOMAIN          94..153
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          154..215
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        306
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   ACT_SITE        402
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-1"
FT   BINDING         249..251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-3"
FT   BINDING         299..301
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-3"
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|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         303
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|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         304
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-2"
FT   BINDING         306
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|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-4"
FT   BINDING         339..341
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-2"
FT   BINDING         362..363
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-2"
FT   BINDING         386..390
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-2"
FT   BINDING         416
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT                   ECO:0000256|PIRSR:PIRSR000130-2"
FT   BINDING         470
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT   BINDING         471
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT   BINDING         472
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
SQ   SEQUENCE   488 AA;  52155 MW;  8CEA41526D048F93 CRC64;
     MSLRVIKEAL TFDDVLLVPA HSTVLPNTAD LSTQLTKTIR LNIPMLSAAM DTVTETKLAI
     SLAQEGGIGF IHKNMSIERQ ADRVRKVKKF ESGIVSEPVT VSPTLTLADL AQIVKKNGFA
     GYPVVDEQDN LVGIITGRDT RFVSDLTKTV ADFMTPKDRL VTVKENATRE EIFRLMHEHR
     VEKVLVVNDD FKLKGMITLK DYQKAESKPN ACKDEFGRLR VGAAVGAGAG NEERIDALVK
     AGVDILLIDS SHGHSEGVLQ RVRETRAKYP DLPIVAGNVA TAEGAIALAD AGASAVKIGI
     GPGSICTTRI VTGVGVPQIT AIADAAAALK ERGIPVIADG GIRYSGDIAK AIAAGASCVM
     VGSMFAGTEE APGEIELYQG RAFKSYRGMG SLGAMSKGSS DRYFQSDNAA DKLVPEGIEG
     RIPYKGYLKE IIHQQMGGLR SCMGLTGCAT IDDLRTKAQF VRISGAGIKE SHVHDVTITK
     EAPNYRMS
//
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