ID   MAP1_KLEOX              Reviewed;          43 AA.
AC   P41392;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 100.
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   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M5a1;
RX   PubMed=7753028; DOI=10.1007/bf00705649;
RA   Edwards R.A., Merrick M.J.;
RT   "The role of uridylyltransferase in the control of Klebsiella pneumoniae
RT   nif gene regulation.";
RL   Mol. Gen. Genet. 247:189-198(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). Requires deformylation of the N(alpha)-formylated
CC       initiator methionine before it can be hydrolyzed (By similarity).
CC       {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 type 1 subfamily. {ECO:0000305}.
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DR   EMBL; X78685; CAA55352.1; -; Genomic_DNA.
DR   PIR; S54755; S43195.
DR   AlphaFoldDB; P41392; -.
DR   SMR; P41392; -.
DR   STRING; 571.MC52_13175; -.
DR   MEROPS; M24.001; -.
DR   eggNOG; COG0024; Bacteria.
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   SUPFAM; SSF55920; SSF55920; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Metal-binding; Protease.
FT   CHAIN           <1..43
FT                   /note="Methionine aminopeptidase"
FT                   /id="PRO_0000148943"
FT   NON_TER         1
SQ   SEQUENCE   43 AA;  4826 MW;  5E030E6D4A3049E1 CRC64;
     TVKTKDRSLS AQYEHTIVVT DNGCEILTLR KDDTIPAIIS HNE