ID   MAP2_METFE              Reviewed;         188 AA.
AC   P22624;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Methionine aminopeptidase;
DE            Short=MAP;
DE            Short=MetAP;
DE            EC=3.4.11.18;
DE   AltName: Full=Peptidase M;
DE   Flags: Fragment;
GN   Name=map;
OS   Methanothermus fervidus.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=2180;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2473943; DOI=10.1016/0378-1119(89)90073-5;
RA   Haas E.S., Daniels C.J., Reeve J.N.;
RT   "Genes encoding 5S rRNA and tRNAs in the extremely thermophilic
RT   archaebacterium Methanothermus fervidus.";
RL   Gene 77:253-263(1989).
RN   [2]
RP   SIMILARITY.
RX   PubMed=7899076; DOI=10.1093/nar/23.4.565;
RA   Ouzounis C., Kyrpides N., Sander C.;
RT   "Novel protein families in archaean genomes.";
RL   Nucleic Acids Res. 23:565-570(1995).
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) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         from peptides and arylamides.; EC=3.4.11.18;
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
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.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase archaeal type 2 subfamily. {ECO:0000305}.
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DR   EMBL; M26978; AAA72775.1; -; Genomic_DNA.
DR   PIR; PS0039; PS0039.
DR   AlphaFoldDB; P22624; -.
DR   SMR; P22624; -.
DR   MEROPS; M24.035; -.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.230.10; -; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; SSF55920; 1.
DR   PROSITE; PS01202; MAP_2; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Protease.
FT   CHAIN           1..>188
FT                   /note="Methionine aminopeptidase"
FT                   /id="PRO_0000148974"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         188
SQ   SEQUENCE   188 AA;  20713 MW;  73057519CA497F62 CRC64;
     MEKFKKAGKI ASKVRKKAIK AVKGEMKILD LAEFIENEIE KMGAKPAFPC NISVNEITAH
     YSPPCNDDRK ILPGDLVKID IGVHVDGFIG DTATTVLVEG YEDLKNYNDE LAEKNKKMIE
     AAESALENAI NTIRDGVEIG KIGEVIENTI NKFGFKPISN LTGHTIDRWV LHSGLSIPNV
     KGQNSHKL