ID   Q8FP84_COREF            Unreviewed;       325 AA.
AC   Q8FP84;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   04-NOV-2026, entry version 142.
DE   RecName: Full=Methionine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE            Short=MAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            Short=MetAP {ECO:0000256|HAMAP-Rule:MF_01974};
DE            EC=3.4.11.18 {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653};
DE   AltName: Full=Peptidase M {ECO:0000256|HAMAP-Rule:MF_01974};
GN   Name=map {ECO:0000256|HAMAP-Rule:MF_01974};
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18711.1, ECO:0000313|Proteomes:UP000001409};
RN   [1] {ECO:0000313|EMBL:BAC18711.1, ECO:0000313|Proteomes:UP000001409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC   {ECO:0000313|Proteomes:UP000001409};
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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.
CC       {ECO:0000256|ARBA:ARBA00002521, ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal amino acids, preferentially methionine,
CC         from peptides and arylamides.; EC=3.4.11.18;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01974,
CC         ECO:0000256|RuleBase:RU003653};
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01974};
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:0000256|HAMAP-Rule:MF_01974};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01974}.
CC   -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC       aminopeptidase type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01974}.
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DR   EMBL; BA000035; BAC18711.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8FP84; -.
DR   STRING; 196164.gene:10742329; -.
DR   MEROPS; M24.A06; -.
DR   KEGG; cef:CE1901; -.
DR   eggNOG; COG0024; Bacteria.
DR   HOGENOM; CLU_015857_1_5_11; -.
DR   OMA; AACHNEI; -.
DR   Proteomes; UP000001409; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004239; F:initiator methionyl aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd01086; MetAP1; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   HAMAP; MF_01974; MetAP_1; 1.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR002467; Pept_M24A_MAP1.
DR   NCBIfam; TIGR00500; met_pdase_I; 1.
DR   PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR43330:SF16; METHIONINE AMINOPEPTIDASE 2; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   PROSITE; PS00680; MAP_1; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP-
KW   Rule:MF_01974};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01974};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01974};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001409}.
FT   DOMAIN          84..312
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         167
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         178
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         178
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         241
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         274
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         305
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
FT   BINDING         305
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01974"
SQ   SEQUENCE   325 AA;  35982 MW;  D1FA34C4771006AD CRC64;
     MMPRGGARRK ALPVPDSPTA PVRLPRGRGT SMVTMSTLRA PLVPGEPTPI RKVPAHIERP
     EYVWKDEVLE AIGEPYVQTP EVIEAMRKTS RIAANALKVA GAAVAPGVTT DEIDRIAHEY
     MCDHGAYPSD LGYRGFTKSV CVSLNEIVCH GIPDTTVIQD GDIVNIDVTA YKHGVHGDCN
     ATFLSGNVSE EHRLLVERTE EALMRSIRAA KPGREINIIG RVIESYAKRF GYNVVRDFTG
     HGIGPTFHNG LIVLHYDSTQ YRDLLVPGMT LTIEPMINLG SLDYEIWDDG WTVQNKDRKF
     TAQFEHTIVI TEDGNEILTL PDENI
//