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peptidase dimerization domain-containing protein
This domain consists of 4 beta strands and two alpha helices which make up the dimerisation surface of members of the M20 family of peptidases [1]. This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification [2]. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. [1]. 9083113. Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P;. Structure 1997;5:337-347. [2]. 7674922. Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. (from Pfam)
M20/M25/M40 family metallo-hydrolase
This family includes a range of zinc metallopeptidases belonging to several families in the peptidase classification [1]. Family M20 are Glutamate carboxypeptidases. Peptidase family M25 contains X-His dipeptidases. [1]. 7674922. Evolutionary families of metallopeptidases. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. (from Pfam)
succinyl-diaminopimelate desuccinylase
succinyl-diaminopimelate desuccinylase catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate
Catalyzes the formation of succinate and diaminoheptanedioate from succinyldiaminoheptanedioate
This HMM describes a proteobacterial subset of succinyl-diaminopimelate desuccinylases. An experimentally confirmed Gram-positive lineage succinyl-diaminopimelate desuccinylase has been described for Corynebacterium glutamicum (SP:Q59284), and a neighbor-joining tree shows the seed members, SP:Q59284, and putative archaeal members such as TrEMBL:O58003 in a single clade. However, the archaeal members differ substantially, share a number of motifs with acetylornithine deacetylases rather than succinyl-diaminopimelate desuccinylases, and are not taken as trusted examples of succinyl-diaminopimelate desuccinylases. This model is limited to proteobacterial members for this reason.
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