MAP2_THEON
ID MAP2_THEON Reviewed; 295 AA.
AC B6YTG0; Q2QC91;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=TON_0362;
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=NA1;
RX PubMed=16761197; DOI=10.1007/s10126-005-6124-8;
RA Lee H.S., Kim Y.J., Bae S.S., Jeon J.H., Lim J.K., Jeong B.C., Kang S.G.,
RA Lee J.H.;
RT "Cloning, expression, and characterization of a methionyl aminopeptidase
RT from a hyperthermophilic archaeon Thermococcus sp. NA1.";
RL Mar. Biotechnol. 8:425-432(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
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 ECO:0000269|PubMed:16761197}.
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 ECO:0000269|PubMed:16761197};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:16761197};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:16761197};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:16761197};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250, ECO:0000269|PubMed:16761197};
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. 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 The enzyme is active with cobalt, nickel, manganese and divalent iron
CC ions. {ECO:0000250, ECO:0000269|PubMed:16761197};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.68 mM for L-Met-p-nitroanilide {ECO:0000269|PubMed:16761197};
CC Note=kcat is 168 min(-1) with L-Met-p-nitroanilide as substrate.;
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:16761197};
CC Temperature dependence:
CC Optimum temperature is 80-90 degrees Celsius.
CC {ECO:0000269|PubMed:16761197};
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; DQ144133; ABA26945.1; -; Genomic_DNA.
DR EMBL; CP000855; ACJ15847.1; -; Genomic_DNA.
DR RefSeq; WP_012571319.1; NC_011529.1.
DR AlphaFoldDB; B6YTG0; -.
DR SMR; B6YTG0; -.
DR STRING; 523850.TON_0362; -.
DR MEROPS; M24.035; -.
DR EnsemblBacteria; ACJ15847; ACJ15847; TON_0362.
DR GeneID; 7018028; -.
DR KEGG; ton:TON_0362; -.
DR PATRIC; fig|523850.10.peg.365; -.
DR eggNOG; arCOG01001; Archaea.
DR HOGENOM; CLU_015857_7_0_2; -.
DR OMA; NEIAAHY; -.
DR OrthoDB; 82853at2157; -.
DR Proteomes; UP000002727; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Aminopeptidase; Hydrolase; Metal-binding; Protease.
FT CHAIN 1..295
FT /note="Methionine aminopeptidase"
FT /id="PRO_0000428826"
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; 33013 MW; 743CE50ECD2622D2 CRC64;
MDEREALIKA GEIARQVKKE VISLIKPGTK LYDIAEFVER RIIELGGKPA FPCNLSINEI
AAHYTPYKGD ETVLKEGDYL KVDIGVHVDG YIADTALTFR VGMEEDDLVT AAREALENAI
KVIRAGIKIN EIGKAIEETI RGYGFNPIVN LSGHKIERYK LHAGISIPNI YRPADSYVLK
EGDVIAIEPF ATTGAGQVIE VPPALIFMYL RDRPVRMAQA RRVLMHIKRE YNGLPFAYRW
LQGFMPEGQL KLALAQLDRV GAIYSYPILR EVRGGLVAQF EHTVIVEKEG AYITT
