ID   IMDH_CHLP8              Reviewed;         494 AA.
AC   O50316; B3QMJ6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 3.
DT   27-MAR-2024, entry version 133.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964};
DE            Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964};
DE            EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964};
GN   Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964};
GN   OrderedLocusNames=Cpar_0730;
OS   Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS   subsp. thiosulfatophilum).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Chlorobaculum.
OX   NCBI_TaxID=517417;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Petersen B.L., Moeller M.G., Stummann B.M., Henningsen K.W.;
RT   "Clustering of genes with function in the biosynthesis of
RT   bacteriochlorophyll and heme in the green sulfur bacterium Chlorobium
RT   vibrioforme.";
RL   Hereditas 125:93-96(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 263 / NCIMB 8327;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL   Submitted (JUN-2008) 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:0000255|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:0000255|HAMAP-Rule:MF_01964};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP-
CC         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:0000255|HAMAP-Rule:MF_01964}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC       from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964}.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP-
CC       Rule:MF_01964}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB06303.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z83933; CAB06303.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001099; ACF11149.1; -; Genomic_DNA.
DR   PIR; T17196; T17196.
DR   RefSeq; WP_012501982.1; NC_011027.1.
DR   AlphaFoldDB; O50316; -.
DR   SMR; O50316; -.
DR   STRING; 517417.Cpar_0730; -.
DR   KEGG; cpc:Cpar_0730; -.
DR   eggNOG; COG0516; Bacteria.
DR   HOGENOM; CLU_022552_2_2_10; -.
DR   OrthoDB; 9805398at2; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000008811; Chromosome.
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; 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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   CBS domain; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase;
KW   Potassium; Purine biosynthesis; Repeat.
FT   CHAIN           1..494
FT                   /note="Inosine-5'-monophosphate dehydrogenase"
FT                   /id="PRO_0000093694"
FT   DOMAIN          93..154
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   DOMAIN          158..217
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   ACT_SITE        308
FT                   /note="Thioimidate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   ACT_SITE        406
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         301..303
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
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:0000255|HAMAP-Rule:MF_01964"
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:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         306
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         308
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:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         341..343
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         364..365
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         388..392
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         421
FT                   /ligand="IMP"
FT                   /ligand_id="ChEBI:CHEBI:58053"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         475
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         476
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   BINDING         477
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_note="ligand shared between two tetrameric
FT                   partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01964"
FT   CONFLICT        158
FT                   /note="M -> I (in Ref. 1; CAB06303)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        429..431
FT                   /note="AKG -> QR (in Ref. 1; CAB06303)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  53202 MW;  E920D6B0B60C44AC CRC64;
     MDKILYDALT FDDVLLVPAY SNVLPKETVV KSRVTRNIEV NLPLVSAAMD TVTEAELAIA
     LARAGGIGII HKNLSIDVQA RHVAKVKRFE SGIIRNPITL FEDATIQEAI DLMLRHSISG
     IPVVERPTPE GCLLLKGIVT NRDLRMTTSS NEKITTIMTT DLITAQEDID LLAAEEILMQ
     NKIEKLLVID EEGYLKGLIT FKDIQKRKQC PDACKDMHGR LRVGAAVGIR SNTITRVDAL
     VEAGVDVVAV DTAHGHSQAV LDMVATIKEK YPELEVIAGN VATPEAVRDL VKAGADAVKV
     GIGPGSICTT RVVAGVGMPQ LTAIMNCAKE AAKTDTPIIA DGGIKYSGDI SKALAAGADT
     VMMGSIFAGT DESPGETILY EGRRFKAYRG MGSLGAMSEP EGSSDRYFQD ASAETKKYVP
     EGIEGRIPAK GPLDEVVYQL IGGLKSSMGY CGVKNIEELK KNTRFVRITS AGLRESHPHD
     VMITREAPNY STSH
//