Domain

Pyruvoyl-dependent histidine/arginine decarboxylase (IPR016104)

Short name: Pyr-dep_his/arg-deCO2ase

Domain relationships

None.

Description

This entry represents a structural domain found in pyruvoyl-dependent histidine decarboxylase (EC:4.1.1.2) and arginine decarboxylase (EC:4.1.1.19). This domain consists of a duplication of a beta-alpha-beta(2) motif that forms a 4-layer alpha/beta/beta/alpha topology, which contains a silk-like beta-sandwich. This domain contains two chains resulting from self-processing of a single-chain precursor. These proteins form heterohexamers [PMID: 11243783, PMID: 12623016].

Histidine decarboxylase catalyses the formation of histamine from histidine. It requires a pyruvoyl group for its activity. Cleavage of the proenzyme PI chain yields two subunits, alpha and beta, which arrange as a hexamer (alpha beta) 6 by nonhydrolytic self-catalysis.

Arginine decarboxylase catalyses the interconversion of arginine and agmatine plus carbon dioxide. It requires a pyruvoyl group for its activity. Archaeoglobus fulgidus contains three copies of this 80-residue domain, all of which are very closely related.

GO terms

Biological Process

GO:0006520 cellular amino acid metabolic process

Molecular Function

GO:0016831 carboxy-lyase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
SUPERFAMILY