Protein Domain : IPR005941

Type:  Family Name:  Succinyl-diaminopimelate desuccinylase, proteobacteria
Description:  Two lysine biosynthesis pathways evolved separately in organisms, the diaminopimelic acid (DAP) and aminoadipic acid (AAA) pathways. The DAP pathway synthesizes L-lysine from aspartate and pyruvate, and diaminopimelic acid is an intermediate. This pathway is utilised by most bacteria, some archaea, some fungi, some algae, and plants. The AAA pathway synthesizes L-lysine from alpha-ketoglutarate and acetyl coenzyme A (acetyl-CoA), and alpha-aminoadipic acid is an intermediate. This pathway is utilised by most fungi, some algae, the bacterium Thermus thermophilus, and probably some archaea, such as Sulfolobus, Thermoproteus, and Pyrococcus. No organism is known to possess both pathways [].There four known variations of the DAP pathway in bacteria: the succinylase, acetylase, aminotransferase, and dehydrogenase pathways. These pathways share the steps converting L-aspartate to L-2,3,4,5- tetrahydrodipicolinate (THDPA), but the subsequent steps leading to the production of meso-diaminopimelate, the immediate precursor of L-lysine, are different [].The succinylase pathway acylates THDPA with succinyl-CoA to generate N-succinyl-LL-2-amino-6-ketopimelate and forms meso-DAP by subsequent transamination, desuccinylation, and epimerization. This pathway is utilised by proteobacteria and many firmicutes and actinobacteria. The acetylase pathway is analogous to the succinylase pathway but uses N-acetyl intermediates. This pathway is limited to certain Bacillus species, in which the corresponding genes have not been identified. The aminotransferase pathway converts THDPA directly to LL-DAP by diaminopimelate aminotransferase (DapL) without acylation. This pathway is shared by cyanobacteria, Chlamydia, the archaeon Methanothermobacter thermautotrophicus, and the plant Arabidopsis thaliana. The dehydrogenase pathway forms meso-DAP directly from THDPA, NADPH, and NH4 _ by using diaminopimelate dehydrogenase (Ddh). This pathway is utilised by some Bacillus and Brevibacterium species and Corynebacterium glutamicum. Most bacteria use only one of the four variants, although certain bacteria, such as C. glutamicum and Bacillus macerans, possess both the succinylase and dehydrogenase pathways.This entry represents succinyl-diaminopimelate desuccinylase (), which hydrolyses N-succinyl-L,L-diaminopimelic acid to L,L-diaminopimelic acid (L,L-DAP). L,L-DAP is required for the bacterial synthesis of lysine and meso-diaminopimelic acid. This group of bacterial sequences belong to the MEROPS peptidase family M20 (clan MH), subfamily M20A (DapE peptidase); they are not strictly peptidases as they are aminohydrolases. Short Name:  DapE_proteobac
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0 Child Features

2 Contains

DB identifier Type Name
IPR011650 Domain Peptidase M20, dimerisation domain
IPR001261 Conserved_site ArgE/DapE/ACY1/CPG2/YscS, conserved site

2 Cross Referencess

Identifier
TIGR01246
MF_01690

0 Found In

2 GO Annotations

GO Term Gene Name
GO:0009014 IPR005941
GO:0009089 IPR005941

2 Ontology Annotations

GO Term Gene Name
GO:0009014 IPR005941
GO:0009089 IPR005941

1 Parent Features

DB identifier Type Name
IPR002933 Family Peptidase M20

3 Proteins

DB identifier UniProt Accession Secondary Identifier Organism Name Length
Araha.11756s0326.1.p PAC:28856409 Arabidopsis halleri 376  
Brdisv1BdTR11A1041523m.p PAC:35693564 Brachypodium distachyon BdTR11a 385  
Zosma07g01200 PAC:50101726 Zostera marina 799  

1 Publications

First Author Title Year Journal Volume Pages PubMed ID
            20418392