ID IMDH_CHLTE Reviewed; 494 AA. AC Q8KCW4; DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 128. 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=CT1293; OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) OS (Chlorobium tepidum). OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae; OC Chlorobaculum. OX NCBI_TaxID=194439; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS; RX PubMed=12093901; DOI=10.1073/pnas.132181499; RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M., RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V., RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M., RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A., RA Fraser C.M.; RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, RT anaerobic, green-sulfur bacterium."; RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE006470; AAM72523.1; -; Genomic_DNA. DR RefSeq; NP_662181.1; NC_002932.3. DR RefSeq; WP_010932962.1; NC_002932.3. DR AlphaFoldDB; Q8KCW4; -. DR SMR; Q8KCW4; -. DR STRING; 194439.CT1293; -. DR EnsemblBacteria; AAM72523; AAM72523; CT1293. DR KEGG; cte:CT1293; -. DR PATRIC; fig|194439.7.peg.1178; -. DR eggNOG; COG0516; Bacteria. DR HOGENOM; CLU_022552_2_1_10; -. DR OrthoDB; 9805398at2; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000001007; 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; Reference proteome; Repeat. FT CHAIN 1..494 FT /note="Inosine-5'-monophosphate dehydrogenase" FT /id="PRO_0000093693" 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" SQ SEQUENCE 494 AA; 53019 MW; CD4C06DBBCB724DE CRC64; MDKILYDALT FDDVLLVPAY SNVLPKETVV KSRLTRQIEV NIPLVSAAMD TVTEAELAIA LARAGGIGII HKNLSIDEQA RQVAKVKRFE SGIIRNPIHL FEDATIQDAI DLMIRHSISG IPVVEHPTPE GCLLLKGIVT NRDLRMTASS DEKITTIMTT NLVTAKEGID LLTAEDILMR NKIEKLLIID DNGYLKGLIT FKDIQKRKQC PDACKDSQGR LRAGAAVGIR ANTMSRVDAL VAAGVDVVAV DTAHGHSQAV LDMVATIKQK YPELQVIAGN VATPEAVRDL VKAGADAVKV GIGPGSICTT RIVAGVGMPQ LTAIMKCAEE AKKTDIPLIA DGGIKYSGDI AKALAAGADS VMMGSVFAGT DESPGETILY EGRRFKAYRG MGSLGAMSEP EGSSDRYFQD VSAETKKYVP EGIEGRIPAK GKLDEVVYQL IGGLKSAMGY CGVRTITELK ENTRFVRITS AGLRESHPHD VMITKEAPNY STSA //