MAP2_THEKO
ID MAP2_THEKO Reviewed; 295 AA.
AC Q5JGD1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01975};
DE Short=MAP {ECO:0000255|HAMAP-Rule:MF_01975};
DE Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01975};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01975};
DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01975};
GN Name=map {ECO:0000255|HAMAP-Rule:MF_01975}; OrderedLocusNames=TK1183;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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). {ECO:0000255|HAMAP-Rule:MF_01975}.
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:0000255|HAMAP-Rule:MF_01975};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975};
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:0000255|HAMAP-Rule:MF_01975};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01975}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase archaeal type 2 subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01975}.
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DR EMBL; AP006878; BAD85372.1; -; Genomic_DNA.
DR RefSeq; WP_011250134.1; NC_006624.1.
DR AlphaFoldDB; Q5JGD1; -.
DR SMR; Q5JGD1; -.
DR STRING; 69014.TK1183; -.
DR MEROPS; M24.035; -.
DR EnsemblBacteria; BAD85372; BAD85372; TK1183.
DR GeneID; 3234128; -.
DR KEGG; tko:TK1183; -.
DR PATRIC; fig|69014.16.peg.1157; -.
DR eggNOG; arCOG01001; Archaea.
DR HOGENOM; CLU_015857_7_0_2; -.
DR InParanoid; Q5JGD1; -.
DR OMA; NEIAAHY; -.
DR OrthoDB; 82853at2157; -.
DR PhylomeDB; Q5JGD1; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008235; F:metalloexopeptidase activity; IBA:GO_Central.
DR GO; GO:0035551; P:protein initiator methionine removal involved in protein maturation; IBA:GO_Central.
DR CDD; cd01088; MetAP2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01975; MetAP_2_arc; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR028595; MetAP_archaeal.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002468; Pept_M24A_MAP2.
DR InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00501; met_pdase_II; 1.
DR PROSITE; PS01202; MAP_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Protease; Reference proteome.
FT CHAIN 1..295
FT /note="Methionine aminopeptidase"
FT /id="PRO_0000148980"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 83
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 94
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 94
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 154
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 188
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 281
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
FT BINDING 281
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01975"
SQ SEQUENCE 295 AA; 33021 MW; 4199B9ADA77AD173 CRC64;
MDEREALIKA GEIARQVKKE VVDLIKPGAK LYDIAEFVER RIVELGGKPA FPCNLSINEI
AAHYTPYKGD GTVLKEGDYL KLDIGVHVDG YIADTAVTFR VGMEEDELME AAREALENAI
ATVRAGVMIR DVARAIEETI RGKGFNPIVN LSGHKVERYK LHAGVSVPNV YREADTYVLQ
EGDVFAIEPF ATTGAGQVIE VPPALIFMYL RDRPVRMLQA RRLLMHIKKN YKTLPFAYRW
LQDFLPEGQL KLALAQLEKA GAIYAYPILR EVRGGMVAQF EHTVIVEKEG AYITT
