ID IMDH1_XENTR Reviewed; 512 AA. AC F6S675; DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 1. DT 27-MAR-2024, entry version 57. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03156}; DE Short=IMP dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03156}; DE Short=IMPD 1 {ECO:0000255|HAMAP-Rule:MF_03156}; DE Short=IMPDH 1 {ECO:0000255|HAMAP-Rule:MF_03156}; DE EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03156}; GN Name=impdh1; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L., RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R., RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J., RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H., RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K., RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A., RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T., RA Khokha M.K., Richardson P.M., Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(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_03156}. 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_03156}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000255|HAMAP- CC Rule:MF_03156}; 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_03156}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP CC from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_03156}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03156}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03156}. CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03156}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP- CC Rule:MF_03156}. 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; AAMC01092195; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01092196; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F6S675; -. DR SMR; F6S675; -. DR STRING; 8364.ENSXETP00000010049; -. DR PaxDb; 8364-ENSXETP00000049823; -. DR AGR; Xenbase:XB-GENE-957448; -. DR eggNOG; KOG2550; Eukaryota. DR HOGENOM; CLU_022552_2_1_1; -. DR InParanoid; F6S675; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000008143; Genome assembly. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 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:SF74; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE 1; 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; Cytoplasm; GMP biosynthesis; Metal-binding; NAD; Nucleus; KW Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome; Repeat. FT CHAIN 1..512 FT /note="Inosine-5'-monophosphate dehydrogenase 1" FT /id="PRO_0000415678" FT DOMAIN 112..171 FT /note="CBS 1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT DOMAIN 177..235 FT /note="CBS 2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT ACT_SITE 329 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT ACT_SITE 427 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 272..274 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 322..324 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 324 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_03156" FT BINDING 326 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_03156" FT BINDING 327 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 329 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_03156" FT BINDING 362..364 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 385..386 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 409..413 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 439 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000255|HAMAP-Rule:MF_03156" FT BINDING 498 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_03156" FT BINDING 499 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_03156" FT BINDING 500 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_03156" SQ SEQUENCE 512 AA; 55454 MW; 6FAEE3FAE9E12ED0 CRC64; MADYLISGGT GYVPEDGLTA QHLFANSDGL TYNDFLILPG FIDFTADEVD LTSALTRKIT LKTPLISSPM DTVTESDMAI AMALMGGIGI IHHNCTPEFQ ANEVRKKFEQ GFITDPVVMS LNHTVGDVFE AKNRHGFSGI PVTETGKMGS KLVGIVTSRD IDFLTEKDYS TYLSEVMTKR DELVVAPAGV TLKEANEILQ RSKKGKLPIV NDSDELVAII ARTDLKKNRD YPLASKDCRK QLLCGAAIGT REDDKYRLDL LTQAGVDVVV LDSSQGNSVY QINMIHYIKQ KYPELQVVGG NVVTAAQAKN LIDAGVDALR VGMGCGSICI TQEVMACGRP QGTAVYKVAE YARRFGVPVI ADGGIQTVGH VVKALALGAS TVMMGSLLAA TTEAPGEYFF SDGVRLKKYR GMGSLDAMEK NTSSQKRYFS EGDKVKVAQG VSGSIQDKGS IHKFVPYLIA GIQHGCQDIG AKSLSILRSM MYSGELKLEK RTMSAQVEGG VHGLHSYEKR LY //