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Annotation rule MF_03156 |
General rule information
[?]
Accession |
MF_03156 |
Dates |
5-JAN-2012 (Created) 11-FEB-2020 (Last updated, Version 10) |
case <OC:Eukaryota>
end case
Propagated annotation
[?]
Identifier, protein and gene names
[?]
Protein name |
RecName:
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Full=Inosine-5'-monophosphate dehydrogenase;
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Short=IMP dehydrogenase;
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Short=IMPD;
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Short=IMPDH;
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EC 1.1.1.205;
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case <OC:Vertebrata>
else case <OC:Saccharomyces>
end case
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 |
RHEA:11708: H2O + IMP + NAD(+) = H(+) + NADH + XMP
EC 1.1.1.205
|
Cofactor |
K(+) |
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. |
case <OC:Vertebrata>
end case
case <OC:Kinetoplastea> and <FTTag:Microbody>
else
end case
case <OC:Vertebrata>
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.
case <OC:Mammalia>
From: IMDH1_HUMAN (P20839) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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INIT_MET
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1
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1
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Removed
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M
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end case
From: IMDH_TRIFO (P50097) |
NP_BIND (Optional)
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261
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263
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NAD
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D-S-S
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case not <FT:2=D-S-S>
BINDING (Optional)
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261
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261
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NAD
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D
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end case
NP_BIND
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312
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314
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NAD
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G-x-G
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REGION
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358
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360
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IMP binding
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D-G-G
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REGION
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381
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382
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IMP binding
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G-x
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REGION
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405
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409
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IMP binding
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[YI]-x-x-x-[GA]
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ACT_SITE
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319
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319
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Thioimidate intermediate
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C
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ACT_SITE
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418
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418
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Proton acceptor
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R
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METAL
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314
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314
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Potassium; via carbonyl oxygen
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G
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METAL
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316
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316
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Potassium; via carbonyl oxygen
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|
|
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G
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METAL
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319
|
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319
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Potassium; via carbonyl oxygen
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C
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METAL (Optional)
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485
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485
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Potassium; via carbonyl oxygen; shared with tetrameric partner
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E
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METAL (Optional)
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486
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486
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Potassium; via carbonyl oxygen; shared with tetrameric partner
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[GS]
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METAL (Optional)
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487
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487
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Potassium; via carbonyl oxygen; shared with tetrameric partner
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[GH]
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BINDING
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317
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317
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IMP
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S
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BINDING
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431
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431
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IMP
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[EQ]
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case <OC:Kinetoplastea>
From: IMDH_LEIDO (P21620) |
MOTIF
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512
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Cter
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Microbody targeting signal
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Microbody
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[AS]-K-[ML]
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end case
Additional information
[?]
Size range |
400-554 amino acids |
Related rules |
None |
Fusion |
None |