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IPR002433

Description

IPR002433 is a Ornithine decarboxylase.

<p>These enzymes are collectively known as group IV decarboxylases [[cite:PUB00001452]]. Pyridoxal-dependent decarboxylases acting on ornithine, lysine, arginine and related substrates can be classified into two different families on the basis of sequence similarities [[cite:PUB00003632], [cite:PUB00001452]]. Members of this family while most probably evolutionary related, do not share extensive regions of sequence similarities. The proteins contain a conserved lysine residue which is known, in mouse ODC [[cite:PUB00002726]], to be the site of attachment of the pyridoxal-phosphate group. The proteins also contain a stretch of three consecutive glycine residues and has been proposed to be part of a substrate- binding region [[cite:PUB00002116]].<p>The ornithine decarboxylases catalyse the transformation of ornithine into putrescine. Phylogenetic analysis of the mRNAs from several mammalian species suggests that ODC is encoded by orthologous genes in the different species. Analysis of divergence patterns in a number of subregions showed that the domains have evolved in a noncoordinate fashion. Evolution of each subregion has been episodic, with periods of both rapid and slow divergence, possibly indicating the existence of selection pressures that were exerted in a time- and domain-specific manner during mammalian speciation. The active form of mammalian ODC is a homodimer of 53kDa subunits (the monomer retains no enzymatic activity).<i>In vitro</i>hybridisation and cross- linkage analysis have suggested that the active site of ODC is formed at the interface of the two monomers via the interaction of the cysteine-360- containing region of one subunit with the lysine-69-containing region of the other [[cite:PUB00002726]].</p> <p>This family also includes antizyme inhibitors (AZINs), which are ODC-homologous proteins lacking catalytic activity. They bind and inhibit the ODC antizyme [[cite:PUB00089255]]. Other members of this group are: Decarboxylase flvG from the fungus Aspergillus flavus, involved in the biosynthesis of flavunoidine, an alkaloidal terpenoid [[cite:PUB00100359]]; Amino acid decarboxylase lolD2 from the endophyte fungus Epichloe uncinata, involved in the biosynthesis of loline alkaloids, which are potent insecticidal agents [[cite:PUB00100377]] and 2-[(L-alanin-3-ylcarbamoyl)methyl]-2-hydroxybutanedioate decarboxylase from Staphylococcus aureus, which catalyses the second step in staphyloferrin B biosynthesis [[cite:PUB00092857]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .

GO term Namespace Name Definition Relationships
Biological process Polyamine biosynthetic process The chemical reactions and pathways resulting in the formation of polyamines, any organic compound containing two or more amino groups.

Co-occuring domains 1

A list of co-occurring predicted domains within the L. japonicus gene space:

Predicted domain Source Observations Saturation (%)
cd00622 CDD 1 33.33