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HAMAP rule MF_01964

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General rule information [?]

Accession MF_01964
Dates 5-JAN-2012 (Created)
1-JUN-2023 (Last updated, Version 15)
Name IMPDH
Scope(s) Archaea
Bacteria
Template(s) P50097 (IMDH_TRIFO); P0C0H6 (IMDH_STRPY); P49058 (IMDH_BORBU); P0ADG7 (IMDH_ECOLI); P9WKI7 (IMDH_MYCTU); [ Recover all ]
Triggered by
case c? <OC:Bacteria> or <OC:Archaea>
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;
Gene name Name=guaB;

Comments [?]

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.
CATALYTIC ACTIVITY Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; 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.
SIMILARITYBelongs to the IMPDH/GMPR family.

Keywords [?]


Gene Ontology [?]

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: 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:1=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]

Additional information [?]

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



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