HAMAP rule MF_01842

General rule information [?]

Accession	MF_01842
Dates	15-DEC-2005 (Created) 19-NOV-2022 (Last updated, Version 16)

Name	Archaemetzincin

Scope

Archaea

Templates

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

amzA

Comments [?]

Function	Probable zinc metalloprotease whose natural substrate is unknown.
Cofactor	Zn(2+) Note: Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.
Subunit	Monomer.
Similarity	Belongs to the peptidase M54 family.

Keywords [?]

Hydrolase
Metal-binding
Metalloprotease
Protease
Zinc

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 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	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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