5-aminolevulinate synthase presequence (IPR015118)

Short name: 5aminolev_synth_preseq

Overlapping homologous superfamilies


Domain relationships



The N-terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import [PMID: 11566198].

GO terms

Biological Process

GO:0006778 porphyrin-containing compound metabolic process

Molecular Function

GO:0003870 5-aminolevulinate synthase activity
GO:0030170 pyridoxal phosphate binding

Cellular Component

GO:0005759 mitochondrial matrix

Contributing signatures

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