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HAMAP rule MF_03156

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General rule information [?]

Accession MF_03156
Dates 5-JAN-2012 (Created)
3-SEP-2024 (Last updated, Version 16)
Name IMPDH_euk
Scope(s) Eukaryota
Template(s) P50097 (IMDH_TRIFO); P20839 (IMDH1_HUMAN); P21620 (IMDH_LEIDO); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_01964 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier IMDH
Protein name RecName: Full=Inosine-5'-monophosphate dehydrogenase;
                 Short=IMP dehydrogenase;
                 Short=IMPD;
                 Short=IMPDH;
                 EC=1.1.1.205;
case <OC:Vertebrata>
Gene name Name=IMPDH;
else case <OC:Saccharomyces>
Gene name Name=IMD;
end case

Comments [?]

case <OC:Mammalia>
FUNCTIONCatalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.
else
FUNCTIONCatalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
end case
CATALYTIC ACTIVITY Reaction=IMP + NAD(+) + H2O = XMP + NADH + H(+); Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053; EC=1.1.1.205;
COFACTOR Name=K(+); Xref=ChEBI:CHEBI:29103;
ACTIVITY REGULATIONMycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH.
PATHWAYPurine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1.
SUBUNITHomotetramer.
case <OC:Vertebrata>
SUBCELLULAR LOCATIONCytoplasm. Nucleus.
else case <OC:Kinetoplastea> and <FTTag:Microbody>
SUBCELLULAR LOCATIONGlycosome.
else
SUBCELLULAR LOCATIONCytoplasm.
end case
SIMILARITYBelongs to the IMPDH/GMPR family.

Keywords [?]

case <OC:Vertebrata>
Nucleus
end case
case <OC:Kinetoplastea> and <FTTag:Microbody>
Glycosome
Peroxisome
else
Cytoplasm
end case
GMP biosynthesis
Metal-binding
NAD
Oxidoreductase
Potassium
Purine biosynthesis

Gene Ontology [?]

case <OCellular component:Vertebrata>
GO:0005634; Cellular component:nucleus
end case
GO:0005737; Cellular component:cytoplasm
GO:0003938; Molecular function:IMP dehydrogenase activity
GO:0046872; Molecular function:metal ion binding
GO:0000166; Molecular function:nucleotide binding
GO:0006177; Biological process:GMP biosynthetic process

Cross-references [?]

PROSITE PS51371; CBS; 0-2;
PROSITE PS00487; IMP_DH_GMP_RED; 1;
Pfam PF00571; CBS; 2;
Pfam PF00478; IMPDH; 1;
NCBIfam TIGR01302; IMP_dehydrog; 1;
PIRSF PIRSF000130; IMPDH; 1;

Features [?]

From: IMDH1_HUMAN (P20839)
Key From To Description Tag Condition FTGroup
case <OC:Mammalia>
INIT_MET 1 1 /note="Removed" M
end case
From: IMDH_TRIFO (P50097)
Key From To Description Tag Condition FTGroup
BINDING 261 263 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"		 D-S-S
case not <FT:2=D-S-S>
BINDING 261 261 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"		 D
end case
BINDING 312 314 /ligand="NAD(+)"
/ligand_id="ChEBI:CHEBI:57540"		 G-x-G
BINDING 358 360 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 D-G-G
BINDING 381 382 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 G-x
BINDING 405 409 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 [YI]-x-x-x-[GA]
ACT_SITE 319 319 /note="Thioimidate intermediate" C
ACT_SITE 418 418 /note="Proton acceptor" R
BINDING 314 314 /ligand="K(+)"
/ligand_id="ChEBI:CHEBI:29103"
/ligand_note="ligand shared between two tetrameric partners"
/note="in other chain"		 G
BINDING 316 316 /ligand="K(+)"
/ligand_id="ChEBI:CHEBI:29103"
/ligand_note="ligand shared between two tetrameric partners"
/note="in other chain"		 G
BINDING 319 319 /ligand="K(+)"
/ligand_id="ChEBI:CHEBI:29103"
/ligand_note="ligand shared between two tetrameric partners"
/note="in other chain"		 C
BINDING 485 485 /ligand="K(+)"
/ligand_id="ChEBI:CHEBI:29103"
/ligand_note="ligand shared between two tetrameric partners"		 E
BINDING 486 486 /ligand="K(+)"
/ligand_id="ChEBI:CHEBI:29103"
/ligand_note="ligand shared between two tetrameric partners"		 [GS]
BINDING 487 487 /ligand="K(+)"
/ligand_id="ChEBI:CHEBI:29103"
/ligand_note="ligand shared between two tetrameric partners"		 [GH]
BINDING 317 317 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 S
BINDING 431 431 /ligand="IMP"
/ligand_id="ChEBI:CHEBI:58053"		 [EQ]
From: IMDH_LEIDO (P21620)
Key From To Description Tag Condition FTGroup
case <OC:Kinetoplastea>
MOTIF 512 Cter /note="Microbody targeting signal" Microbody [AS]-K-[ML]
end case

Additional information [?]

Size range 400-554 amino acids
Related rules None
Fusion Nter: None Cter: None



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