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HAMAP rule MF_03174

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General rule information [?]

Accession MF_03174
Dates 31-MAY-2013 (Created)
1-JUN-2023 (Last updated, Version 11)
Name MetAP_1_euk
Scope
Eukaryota
Templates P53582 (MAP11_HUMAN); Q01662 (MAP1_YEAST); P0AE18 (MAP1_ECOLI): [Recover all]
case <OC:Eukaryota>
Triggered by
end case


Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
MAP1
case <AnyFeature:TransitM>
Protein name
RecName: Full=Methionine aminopeptidase 1, mitochondrial;
Short=MAP 1;
Short=MetAP 1;
EC 3.4.11.18;
AltName: Full=Peptidase M 1;
else case <AnyFeature:TransitC>
Protein name
RecName: Full=Methionine aminopeptidase 1, chloroplastic;
Short=MAP 1;
Short=MetAP 1;
EC 3.4.11.18;
AltName: Full=Peptidase M 1;
else
Protein name
RecName: Full=Methionine aminopeptidase 1;
Short=MAP 1;
Short=MetAP 1;
EC 3.4.11.18;
AltName: Full=Peptidase M 1;
end case

Comments [?]

case <AnyFeature:PS52013>
Function Cotranslationally 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).
else case <AnyFeature:TransitM> or <AnyFeature:TransitC>
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.
else
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).
end case
Catalytic activity Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18;
case <AnyFeature:PS52013>
Cofactor Zn(2+)
Co(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 zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone
else
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
end case
case <AnyFeature:PS52013>
Subunit Associates with the 60S ribosomal subunit of the 80S translational complex.
Subcellular location Cytoplasm.
end case
Similarity Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

Cross-references [?]

Pfam PF00557; Peptidase_M24; 1;
PRINTS PR00599; MAPEPTIDASE; 1;
NCBIfam TIGR00500; met_pdase_I; 1;
PROSITE PS00680; MAP_1; 1;
PS52013; ZF_C6H2; 0-1; trigger=PRU01357;

Computed features [?]

case not <AnyFeature:PS52013>
General TransitM; -; 0-1; trigger=yes;
end case
case <OC:Viridiplantae> and not (<AnyFeature:PS52013> or <AnyFeature:TransitM>)
General TransitC; -; 0-1; trigger=yes;
end case

Keywords [?]

Aminopeptidase
Hydrolase
Protease
Metal-binding
case <AnyFeature:PS52013>
Cytoplasm
end case

Gene Ontology [?]

case <AnyFeature:PS52013>
GO:0022626; Cellular component: cytosolic ribosome.
else case <AnyFeature:TransitM>
GO:0005739; Cellular component: mitochondrion.
else case <AnyFeature:TransitC>
GO:0009507; Cellular component: chloroplast.
end case
GO:0046872; Molecular function: metal ion binding.
GO:0070006; Molecular function: metalloaminopeptidase activity.
GO:0004239; Molecular function: initiator methionyl aminopeptidase activity.

Features [?]

case <AnyFeature:PS52013>
From: MAP11_HUMAN (P53582)
Key     From     To       Description   Tag   Condition   FTGroup
BINDING     203     203       /ligand="a protein" /ligand_id="ChEBI:CHEBI:16541" /ligand_part="N-terminal L-methionine residue" /ligand_part_id="ChEBI:CHEBI:64731     H  
BINDING     220     220       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3     D  
BINDING     231     231       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3     D  
BINDING     231     231       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic     D  
BINDING     294     294       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic     H  
BINDING     301     301       /ligand="a protein" /ligand_id="ChEBI:CHEBI:16541" /ligand_part="N-terminal L-methionine residue" /ligand_part_id="ChEBI:CHEBI:64731     H  
BINDING     327     327       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic     E  
BINDING     358     358       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="3     E  
BINDING     358     358       /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" /ligand_label="4" /ligand_note="catalytic     E  
else
From: MAP12_HUMAN (Q6UB28)
BINDING     161     161       /ligand="substrate     H  
BINDING     178     178       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     D  
BINDING     189     189       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     D  
BINDING     189     189       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     D  
BINDING     252     252       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     H  
BINDING     259     259       /ligand="substrate     H  
BINDING     284     284       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     E  
BINDING     315     315       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1     E  
BINDING     315     315       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" /ligand_note="catalytic     E  
end case

Additional information [?]

Size range 335-404 amino acids
Related rules None
Fusion None


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