ID A0AAP0G589_9ASPA Unreviewed; 502 AA. AC A0AAP0G589; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; DE Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03156}; DE Short=IMPD {ECO:0000256|HAMAP-Rule:MF_03156}; DE Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_03156}; DE EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; GN ORFNames=KSP39_PZI012728 {ECO:0000313|EMBL:KAK8937348.1}; OS Platanthera zijinensis. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae; OC Orchidoideae; Orchideae; Orchidinae; Platanthera. OX NCBI_TaxID=2320716 {ECO:0000313|EMBL:KAK8937348.1, ECO:0000313|Proteomes:UP001418222}; RN [1] {ECO:0000313|EMBL:KAK8937348.1, ECO:0000313|Proteomes:UP001418222} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Lor287 {ECO:0000313|EMBL:KAK8937348.1}; RX PubMed=35449401; RA Li M.H., Liu K.W., Li Z., Lu H.C., Ye Q.L., Zhang D., Wang J.Y., Li Y.F., RA Zhong Z.M., Liu X., Yu X., Liu D.K., Tu X.D., Liu B., Hao Y., Liao X.Y., RA Jiang Y.T., Sun W.H., Chen J., Chen Y.Q., Ai Y., Zhai J.W., Wu S.S., RA Zhou Z., Hsiao Y.Y., Wu W.L., Chen Y.Y., Lin Y.F., Hsu J.L., Li C.Y., RA Wang Z.W., Zhao X., Zhong W.Y., Ma X.K., Ma L., Huang J., Chen G.Z., RA Huang M.Z., Huang L., Peng D.H., Luo Y.B., Zou S.Q., Chen S.P., Lan S., RA Tsai W.C., Van de Peer Y., Liu Z.J.; RT "Genomes of leafy and leafless Platanthera orchids illuminate the evolution RT of mycoheterotrophy."; RL Nat. Plants 8:373-388(2022). 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:0000256|HAMAP-Rule:MF_03156}. CC -!- CATALYTIC ACTIVITY: CC Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+); 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:0000256|ARBA:ARBA00024264, CC ECO:0000256|HAMAP-Rule:MF_03156, ECO:0000256|RuleBase:RU003928}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000256|ARBA:ARBA00001958, CC ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_03156}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP CC from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_03156, CC ECO:0000256|RuleBase:RU003928}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_03156, CC ECO:0000256|RuleBase:RU003927}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03156}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KAK8937348.1}. 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; JBBWWQ010000010; KAK8937348.1; -; Genomic_DNA. DR Proteomes; UP001418222; Unassembled WGS sequence. DR CDD; cd00381; IMPDH; 1. DR FunFam; 3.20.20.70:FF:000086; IMP dehydrogenase, putative; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. 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; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM01240; IMPDH; 1. DR SUPFAM; SSF54631; CBS-domain pair; 1. DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 3: Inferred from homology; KW CBS domain {ECO:0000256|ARBA:ARBA00023122}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03156}; KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749, ECO:0000256|HAMAP- KW Rule:MF_03156}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03156}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03156}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03156, KW ECO:0000256|RuleBase:RU003927}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_03156}; KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP- KW Rule:MF_03156}. FT DOMAIN 23..492 FT /note="IMP dehydrogenase/GMP reductase" FT /evidence="ECO:0000259|Pfam:PF00478" FT ACT_SITE 321 FT /note="Thioimidate intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT ACT_SITE 417 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 264..266 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 314..316 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 316 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:0000256|HAMAP-Rule:MF_03156" FT BINDING 318 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:0000256|HAMAP-Rule:MF_03156" FT BINDING 319 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 321 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:0000256|HAMAP-Rule:MF_03156" FT BINDING 354..356 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 377..378 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 401..405 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" FT BINDING 429 FT /ligand="IMP" FT /ligand_id="ChEBI:CHEBI:58053" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03156" SQ SEQUENCE 502 AA; 53060 MW; FA0BDFA42441F08E CRC64; MNGAAAAFDD GFTASRLFSQ GFSYTYDDVI FLPHYIDFPA DAVDLSTRLS RNHPLSIPCV ASPMDTVSET SMAVAMASLG GAAIIHCNTI PARQAAIVRS AKSRRIPFAS DPSFFAPSDF VSSAADFGSA SFAIVTESGS SKSKPVGLIS RSDWEALADE DYPVSKYMRQ TPTSIPSNYD FEQVAAFLAG EGLELASLVG VDGEIIDLVC AEDVVRIRGF PKLGVPSLSP DGKFLVGAAI GTREEDKERL THLVKAGVDV VVVDSSQGNS KYQMDMIKHA KNTYPSLDII GGNVVTMAQT QNLIKVGVDG IRVGMGSGSI CTTQEVCAVG RGQATAVYKV ASFANDYDVP VIADGGISYS GHIVKALVLG ASTVMMGSFL AGSHEAPGIY EYQDGHFVKK YRGMGSLEAM TKGSDARYLG DTLKLKVAQG VVGTVVDKGS LLKFIPYTMQ AVKQGLQDLG ASSLPIAHDL LRTDVLQLEV RTGAAQVEGG VHGLASYEKK AF //