HAMAP rule MF_03156
General rule information
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| PURL | https://purl.expasy.org/hamap/rule/MF_03156 |
| Accession | MF_03156 |
| Dates | 22-AUG-2012 (Created)
03-SEP-2024 (Last updated, Version 17) |
| Name | IMPDH_euk |
| Scope(s) |
Eukaryota |
| Template(s) | P50097; P20839; P21620; [ Recover all ] |
| Triggered by |
case c? <OC:Eukaryota>
HAMAP; MF_01964 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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| 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
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| case <OC:Mammalia> | |
| FUNCTION | Catalyzes 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 | |
| FUNCTION | Catalyzes 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 REGULATION | Mycophenolic 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. |
| PATHWAY | Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. |
| SUBUNIT | Homotetramer. |
| case <OC:Vertebrata> | |
| SUBCELLULAR LOCATION | Cytoplasm. Nucleus. |
| else case <OC:Kinetoplastea> and <FTTag:Microbody> | |
| SUBCELLULAR LOCATION | Glycosome. |
| else | |
| SUBCELLULAR LOCATION | Cytoplasm. |
| end case | |
| SIMILARITY | Belongs to the IMPDH/GMPR family. |
Keywords
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| 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
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| 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
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| 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
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| 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
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| Size range | 400-554 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |