ID IMDH_KORCO Reviewed; 476 AA. AC B1L5U5; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000250|UniProtKB:P0ADG7}; DE Short=IMP dehydrogenase {ECO:0000250|UniProtKB:P0ADG7}; DE Short=IMPD {ECO:0000250|UniProtKB:P0ADG7}; DE Short=IMPDH {ECO:0000250|UniProtKB:P0ADG7}; DE EC=1.1.1.205 {ECO:0000250|UniProtKB:P0ADG7}; GN Name=guaB {ECO:0000250|UniProtKB:P0ADG7}; OrderedLocusNames=Kcr_1078; OS Korarchaeum cryptofilum (strain OPF8). OC Archaea; Candidatus Korarchaeota; Korarchaeum. OX NCBI_TaxID=374847; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=OPF8; RX PubMed=18535141; DOI=10.1073/pnas.0801980105; RA Elkins J.G., Podar M., Graham D.E., Makarova K.S., Wolf Y., Randau L., RA Hedlund B.P., Brochier-Armanet C., Kunin V., Anderson I., Lapidus A., RA Goltsman E., Barry K., Koonin E.V., Hugenholtz P., Kyrpides N., Wanner G., RA Richardson P., Keller M., Stetter K.O.; RT "A korarchaeal genome reveals new insights into the evolution of the RT Archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 105:8102-8107(2008). 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:0000250|UniProtKB:P0ADG7}. 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:0000250|UniProtKB:P0ADG7}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000250|UniProtKB:P0ADG7}; 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:0000250|UniProtKB:P0ADG7}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP CC from IMP: step 1/1. {ECO:0000250|UniProtKB:P0ADG7}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0ADG7}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000305}. 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; CP000968; ACB07824.1; -; Genomic_DNA. DR RefSeq; WP_012309721.1; NC_010482.1. DR AlphaFoldDB; B1L5U5; -. DR SMR; B1L5U5; -. DR STRING; 374847.Kcr_1078; -. DR EnsemblBacteria; ACB07824; ACB07824; Kcr_1078. DR GeneID; 6094355; -. DR KEGG; kcr:Kcr_1078; -. DR eggNOG; arCOG00612; Archaea. DR HOGENOM; CLU_022552_2_1_2; -. DR InParanoid; B1L5U5; -. DR OrthoDB; 21361at2157; -. DR PhylomeDB; B1L5U5; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000001686; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. 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 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_0000415693" FT DOMAIN 93..151 FT /note="CBS 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703" FT DOMAIN 152..211 FT /note="CBS 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703" FT ACT_SITE 299 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000250|UniProtKB:P50097" FT ACT_SITE 398 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P9WKI7" FT BINDING 242 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P50097" FT BINDING 292..294 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:P50097" FT BINDING 294 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:0000250|UniProtKB:P50097" 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:0000250|UniProtKB:P50097" FT BINDING 297 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P50097" FT BINDING 299 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:0000250|UniProtKB:P50097" FT BINDING 334..336 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P50097" FT BINDING 357..358 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P50097" FT BINDING 381..385 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P50097" FT BINDING 408 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000250|UniProtKB:P50097" FT BINDING 462 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_note="ligand shared between two tetrameric FT partners" FT /evidence="ECO:0000250|UniProtKB:P50097" SQ SEQUENCE 476 AA; 51195 MW; 6AAC31F930E62260 CRC64; MRIDRFEFAF TFNDVILLPG KTEIEPSNVD LTTRIGNIAL SIPILSSPMD TVTEEEMSIA MARMGGLGIL HRNCSVEEQV NMAKAVKRAE SFIIRDVITV SPEDSVEEAR RLMREHGISG LPVIVGRKLV GIVTRRDVYF AENGSLLVKD IMTKDPITVG PEITPQEARK IMARYKIEKL PVVSESGELI GLVTAKDVFY RESHPFATRD EEGRLRVGAA ISPFDIDRAK TLAPYVDVLV TDVAHFHNEN VISATKRIID EVGVPVIAGN IGTYEAAEEA ITRLDIIGLR VGIGSGSICT TGEVTGVAAP TLYAVASASE AVRKYSKDVA VIADGGIRGP GEAAKAFAMG ADAVMLGYAL AGTKEAPGST MMIGGKMYKI YRGMGSPSAR SKRFAMDRYS KPSKDIAEGI EGLVPYRGDV TTVVDRFVAG LKAAFGYVGA ANISEMKSKA RVALISHSGM SEIAPHDVKP LEKISD //