HAMAP rule MF_01974
General rule information
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Accession | MF_01974 |
Dates | 31-MAY-2013 (Created) 19-NOV-2022 (Last updated, Version 9) |
Name | MetAP_1 |
Scope | Bacteria |
Templates | P0AE18 (MAP1_ECOLI); P9WK19 (MAP12_MYCTU); Q9ZCD3 (MAP1_RICPR): [Recover all] |
case <OC:Bacteria>
Triggered by |
end case
Propagated annotation
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Identifier, protein and gene names
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Identifier |
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Protein name |
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Gene name |
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Comments
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Function | Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed. |
Catalytic activity | Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; |
Cofactor | Co(2+) Zn(2+) Mn(2+) Fe(2+) Note: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. |
Subunit | Monomer. |
Similarity | Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. |
Keywords
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Gene Ontology
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GO:0046872; Molecular function: metal ion binding.
GO:0070006; Molecular function: metalloaminopeptidase activity.
GO:0070084; Biological process: protein initiator methionine removal.
GO:0070006; Molecular function: metalloaminopeptidase activity.
GO:0070084; Biological process: protein initiator methionine removal.
Cross-references
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PROSITE | PS00680; MAP_1; 1; |
Pfam | PF00557; Peptidase_M24; 1; |
PRINTS | PR00599; MAPEPTIDASE; 1; |
TIGRFAMs | TIGR00500; met_pdase_I; 1; |
Features
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From: MAP1_ECOLI (P0AE18) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 97 | 97 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1 | D | 1 | |||||||
BINDING | 108 | 108 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1 | D | 1 | |||||||
BINDING | 108 | 108 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic | D | 1 | |||||||
BINDING | 171 | 171 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic | H | 1 | |||||||
BINDING | 204 | 204 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic | E | 1 | |||||||
BINDING | 235 | 235 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1 | E | 1 | |||||||
BINDING | 235 | 235 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic | E | 1 | |||||||
BINDING | 79 | 79 | /ligand="substrate | H | ||||||||
BINDING | 178 | 178 | /ligand="substrate | H |
Additional information
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Size range | 248-305 amino acids |
Related rules | None |
Fusion | None |