AC MF_03174; DC Protein; auto c? TR HAMAP; MF_01974; -; 1; level=0 XX Names: MetAP_1_euk XX ID MAP1 case DE RecName: Full=Methionine aminopeptidase 1, mitochondrial; DE Short=MAP 1; DE Short=MetAP 1; DE EC=3.4.11.18; DE AltName: Full=Peptidase M 1; else case DE RecName: Full=Methionine aminopeptidase 1, chloroplastic; DE Short=MAP 1; DE Short=MetAP 1; DE EC=3.4.11.18; DE AltName: Full=Peptidase M 1; else DE RecName: Full=Methionine aminopeptidase 1; DE Short=MAP 1; DE Short=MetAP 1; DE EC=3.4.11.18; DE AltName: Full=Peptidase M 1; end case XX case CC -!- FUNCTION: Cotranslationally removes the N-terminal methionine from CC nascent proteins. The N-terminal methionine is often cleaved when the CC second residue in the primary sequence is small and uncharged (Met- CC Ala-, Cys, Gly, Pro, Ser, Thr, or Val). else case or CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The CC N-terminal methionine is often cleaved when the second residue in the CC primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, CC Thr, or Val). Requires deformylation of the N(alpha)-formylated CC initiator methionine before it can be hydrolyzed. else CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The CC N-terminal methionine is often cleaved when the second residue in the CC primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, CC Thr, or Val). end case CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of N-terminal amino acids, preferentially methionine, CC from peptides and arylamides.; EC=3.4.11.18; case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity CC and a low affinity metal-binding site. The true nature of the CC physiological cofactor is under debate. The enzyme is active with zinc, CC cobalt, manganese or divalent iron ions. Has high activity with zinc; CC zinc cofactor is transferred into the active site region by the ZNG1 CC zinc chaperone. else CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity CC and a low affinity metal-binding site. The true nature of the CC physiological cofactor is under debate. The enzyme is active with CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under CC physiological conditions, and the catalytically relevant metal-binding CC site has been assigned to the histidine-containing high-affinity site. end case case CC -!- SUBUNIT: Associates with the 60S ribosomal subunit of the 80S CC translational complex. CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. XX DR Pfam; PF00557; Peptidase_M24; 1; trigger=no DR PRINTS; PR00599; MAPEPTIDASE; 1; trigger=no DR NCBIfam; TIGR00500; met_pdase_I; 1; trigger=no DR PROSITE; PS00680; MAP_1; 1; trigger=no DR PROSITE; PS52013; ZF_C6H2; 0-1; trigger=yes case not DR General; TransitM; -; 0-1; trigger=yes end case case and not ( or ) DR General; TransitC; -; 0-1; trigger=yes end case XX KW Aminopeptidase KW Hydrolase KW Protease KW Metal-binding case KW Cytoplasm end case XX case GO GO:0022626; C:cytosolic ribosome else case GO GO:0005739; C:mitochondrion else case GO GO:0009507; C:chloroplast end case GO GO:0046872; F:metal ion binding GO GO:0070006; F:metalloaminopeptidase activity GO GO:0004239; F:initiator methionyl aminopeptidase activity XX case FT From: MAP11_HUMAN (P53582) FT BINDING 203 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N-terminal L-methionine residue" FT /ligand_part_id="ChEBI:CHEBI:64731" FT Condition: H FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT Condition: D FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT Condition: D FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT Condition: D FT BINDING 294 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT Condition: H FT BINDING 301 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="N-terminal L-methionine residue" FT /ligand_part_id="ChEBI:CHEBI:64731" FT Condition: H FT BINDING 327 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT Condition: E FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT Condition: E FT BINDING 358 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /ligand_note="catalytic" FT Condition: E else FT From: MAP12_HUMAN (Q6UB28) FT BINDING 161 FT /ligand="substrate" FT Condition: H FT BINDING 178 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: D FT BINDING 189 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: D FT BINDING 189 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT Condition: D FT BINDING 252 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT Condition: H FT BINDING 259 FT /ligand="substrate" FT Condition: H FT BINDING 284 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT Condition: E FT BINDING 315 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Condition: E FT BINDING 315 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT /ligand_note="catalytic" FT Condition: E end case XX Size: 335-404; Related: None; Template: P53582; Q01662; P0AE18; Scope: Eukaryota Fusion: Nter: None Cter: None Duplicate: in ARATH, DANRE, DICDI, HUMAN, MOUSE Plasmid: None Comments: None XX # Revision 1.11 2023/06/01 //