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}.
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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
//