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HAMAP rule MF_01842

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General rule information [?]

Accession MF_01842
Dates 15-DEC-2005 (Created)
19-NOV-2022 (Last updated, Version 16)
Name Archaemetzincin
Scope(s) Archaea
Template(s) Q400G9 (AMZ1_HUMAN); Q8TXW1 (AMZA_METKA); O29917 (AMZA_ARCFU); [ Recover all ]
Triggered by HAMAP; MF_01842 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier AMZA
Protein name RecName: Full=Archaemetzincin;
                 EC=3.4.-.-;
Gene name Name=amzA;

Comments [?]

FUNCTIONProbable zinc metalloprotease whose natural substrate is unknown.
COFACTOR Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.;
SUBUNITMonomer.
SIMILARITYBelongs to the peptidase M54 family.

Keywords [?]


Gene Ontology [?]

GO:0008237; Molecular function:metallopeptidase activity
GO:0006508; Biological process:proteolysis
GO:0008270; Molecular function:zinc ion binding

Cross-references [?]

PROSITE PS00142; ZINC_PROTEASE; 1;
Pfam PF07998; Peptidase_M54; 1;
PIRSF PIRSF005785; Zn-prot_arch; 1;

Features [?]

From: AMZA_METKA (Q8TXW1)
Key From To Description Tag Condition FTGroup
ACT_SITE 126 126 /note="Proton acceptor" E
BINDING 125 125 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"
H
BINDING 129 129 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"
H
BINDING 135 135 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="1"
/ligand_note="catalytic"
H
BINDING 136 136 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C
BINDING 141 141 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C
BINDING 160 160 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C
BINDING 163 163 /ligand="Zn(2+)"
/ligand_id="ChEBI:CHEBI:29105"
/ligand_label="2"
C

Additional information [?]

Size range 155-192 amino acids
Related rules None
Fusion Nter: None Cter: 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).



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