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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(s) Eukaryota
Template(s) P53582 (MAP11_HUMAN); Q01662 (MAP1_YEAST); P0AE18 (MAP1_ECOLI); [ Recover all ]
Triggered by
case c? <OC:Eukaryota>
HAMAP; MF_01974 (Get profile general information and statistics)
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>
FUNCTIONCotranslationally 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>
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.
else
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).
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 Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Co(2+); Xref=ChEBI:CHEBI:48828; 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 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 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.
end case
case <AnyFeature:PS52013>
SUBUNITAssociates with the 60S ribosomal subunit of the 80S translational complex.
SUBCELLULAR LOCATIONCytoplasm.
end case
SIMILARITYBelongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.

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

Cross-references [?]

Pfam PF00557; Peptidase_M24; 1;
PRINTS PR00599; MAPEPTIDASE; 1;
NCBIfam TIGR00500; met_pdase_I; 1;
PROSITE PS00680; MAP_1; 1;
PROSITE PS52013; ZF_C6H2; 0-1;
General TransitM; -; 0-1;
General TransitC; -; 0-1;

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)
Key From To Description Tag Condition FTGroup
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 Nter: None Cter: None



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