IMDH_CHLP8
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 03-AUG-2022, entry version 126.
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}; OrderedLocusNames=Cpar_0730;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; 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;
CC Evidence={ECO:0000255|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: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 PRIDE; O50316; -.
DR EnsemblBacteria; ACF11149; ACF11149; Cpar_0730.
DR KEGG; cpc:Cpar_0730; -.
DR eggNOG; COG0516; Bacteria.
DR HOGENOM; CLU_022552_2_2_10; -.
DR OMA; MGYCGAK; -.
DR OrthoDB; 532857at2; -.
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; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; -; 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 PANTHER; PTHR11911; PTHR11911; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
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
