ID IMDH_NITMS Reviewed; 476 AA. AC A9A5Y7; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 77. 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=Nmar_1569; OS Nitrosopumilus maritimus (strain SCM1). OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales; OC Nitrosopumilaceae; Nitrosopumilus. OX NCBI_TaxID=436308; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCM1; RX PubMed=20421470; DOI=10.1073/pnas.0913533107; RA Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J., RA Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J., RA Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T., RA Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M., RA Rosenzweig A.C., Manning G., Stahl D.A.; RT "Nitrosopumilus maritimus genome reveals unique mechanisms for RT nitrification and autotrophy in globally distributed marine crenarchaea."; RL Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010). 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; CP000866; ABX13465.1; -; Genomic_DNA. DR AlphaFoldDB; A9A5Y7; -. DR SMR; A9A5Y7; -. DR STRING; 436308.Nmar_1569; -. DR EnsemblBacteria; ABX13465; ABX13465; Nmar_1569. DR KEGG; nmr:Nmar_1569; -. DR eggNOG; arCOG00612; Archaea. DR HOGENOM; CLU_022552_0_1_2; -. DR InParanoid; A9A5Y7; -. DR OrthoDB; 21361at2157; -. DR PhylomeDB; A9A5Y7; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000000792; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central. 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 GO; GO:0006183; P:GTP biosynthetic process; IBA:GO_Central. 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; GMP biosynthesis; Metal-binding; NAD; Oxidoreductase; KW Potassium; Purine biosynthesis; Reference proteome; Repeat. FT CHAIN 1..476 FT /note="Inosine-5'-monophosphate dehydrogenase" FT /id="PRO_0000415694" FT DOMAIN 92..150 FT /note="CBS 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT DOMAIN 151..207 FT /note="CBS 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT ACT_SITE 301 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 244 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 294..296 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 296 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 298 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 299 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" 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:0000255|HAMAP-Rule:MF_01964" FT BINDING 334..336 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 357..358 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 381..385 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 413 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01964" FT BINDING 467 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 468 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 476 AA; 50130 MW; 19BE67B0C7883900 CRC64; MEFKEGLTFD DVLLVPKYSD ITSRSQTDLT TKLSRNITIN IPFVSANMDT VTESSMAVAM ARAGGIGIIH RFLTIQEQAN EVLKVKRSGS VMIENPYSIS SDKSIQDALD YAEDKEISGL LVVDSNSKLV GIVTERDLLF AGSNGTIADV MTKDVVTAKP GVSLDEAKDI LHKHRIEKLP IVDDSGIIQG LITSKDITNN TDYPNASKDK KGRPLVGAAV GVKGDFLERS ESLLNAGADV LVVDIAHGHS ENAISTVRNI KKAFPDCELI AGNIATAQGA EDLIKAGVDA VKVGVGSGSI CITRVITGSG VPQLTAVMDC AKIGNDHGIP IISDGGTRTS GDATKALAAG ASSVMVGSML GGTDESPGTV LTKNGKRFKV YRGMASLAAS IGRKSKETGS ISLEDDLNDY VAEGVEAMVP YKGTVTDILK QLAGGVRSGL SYCGAHTIPQ MQQNAEFIKM SRAGFAESQP HDVLLM //