AC MF_01842; DC Protein; auto TR HAMAP; MF_01842; -; 1; level=0 XX Names: Archaemetzincin XX ID AMZA DE RecName: Full=Archaemetzincin; DE EC=3.4.-.-; GN Name=amzA; XX CC -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is CC unknown. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the CC other seems to have a structural role.; CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the peptidase M54 family. XX DR PROSITE; PS00142; ZINC_PROTEASE; 1; trigger=no DR Pfam; PF07998; Peptidase_M54; 1; trigger=no DR PIRSF; PIRSF005785; Zn-prot_arch; 1; trigger=no XX KW Hydrolase KW Metal-binding KW Metalloprotease KW Protease KW Zinc XX GO GO:0008237; F:metallopeptidase activity GO GO:0006508; P:proteolysis GO GO:0008270; F:zinc ion binding XX FT From: AMZA_METKA (Q8TXW1) FT ACT_SITE 126 FT /note="Proton acceptor" FT Condition: E FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT Condition: H FT BINDING 129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT Condition: H FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /ligand_note="catalytic" FT Condition: H FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: C FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: C FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: C FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Condition: C XX Size: 155-192; Related: None; Template: Q400G9; Q8TXW1; O29917; Scope: Archaea Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: Although it has not been proved in prokaryotes, its function as metalloprotease is probable due to the strong similarities with the AMZ1 and AMZ2 enzymes. See: RX PubMed=15972818; DOI=10.1074/jbc.M504533200; RA Diaz-Perales A., Quesada V., Peinado J.R., Ugalde A.P., Alvarez J., RA Suarez M.F., Gomis-Rueth X., Lopez-Otin C.; RT "Identification and characterization of human archaemetzincin-1 and - RT 2, two novel members of a family of metalloproteases widely RT distributed in archae."; RL J. BiolQ400G9. Chem. 280:30367-30375(2005). The family has been identified in Archaea and described in: RX PubMed=12746556; RA Gomis-Rueth F.X.; RT "Structural aspects of the metzincin clan of metalloendopeptidases."; RL Mol. Biotechnol. 24:157-202(2003). XX # Revision 1.16 2022/11/19 //