Family

Aspartate decarboxylase (IPR003190)

Short name: Asp_decarbox

Overlapping homologous superfamilies

Family relationships

None.

Description

Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalysed by the enzyme L-aspartate decarboxylase (ADC, EC:4.1.1.11). Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The enzyme is translated as an inactive proenzyme [PMID: 9169598], and is cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment). This model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase. A pyruvoyl cofactor, which is covalently bound to the enzyme, is required for activity. The active site of the tetrameric enzyme is located at the interface of two subunits, with a lysine and a histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit [PMID: 17001646, PMID: 15184017, PMID: 14633979, PMID: 9546220, PMID: 10368289, PMID: 3003510].

GO terms

Biological Process

GO:0006523 alanine biosynthetic process

Molecular Function

GO:0004068 aspartate 1-decarboxylase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
ProDom
PANTHER
CDD
TIGRFAMs
PIRSF
Pfam
HAMAP