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HAMAP rule MF_01974

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General rule information [?]

Accession MF_01974
Dates 31-MAY-2013 (Created)
1-JUN-2023 (Last updated, Version 11)
Name MetAP_1
Scope(s) Bacteria
Template(s) P0AE18 (MAP1_ECOLI); P9WK19 (MAP12_MYCTU); Q9ZCD3 (MAP1_RICPR); [ Recover all ]
Triggered by
case c? <OC:Bacteria>
HAMAP; MF_01974 (Get profile general information and statistics)
end case

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier MAP1
Protein name RecName: Full=Methionine aminopeptidase;
                 Short=MAP;
                 Short=MetAP;
                 EC=3.4.11.18;
AltName: Full=Peptidase M;
Gene name Name=map;

Comments [?]

FUNCTIONRemoves 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 Name=Co(2+); Xref=ChEBI:CHEBI:48828; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; 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.;
SUBUNITMonomer.
SIMILARITYBelongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Keywords [?]


Gene Ontology [?]

GO:0046872; Molecular function:metal ion binding
GO:0070006; Molecular function:metalloaminopeptidase activity
GO:0004239; Molecular function:initiator methionyl aminopeptidase activity

Cross-references [?]

PROSITE PS00680; MAP_1; 1;
Pfam PF00557; Peptidase_M24; 1;
PRINTS PR00599; MAPEPTIDASE; 1;
NCBIfam TIGR00500; met_pdase_I; 1;

Features [?]

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 [?]

Size range 248-305 amino acids
Related rules None
Fusion Nter: None Cter: None



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