ID MAP1_CHLMU Reviewed; 291 AA. AC Q9PL68; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 02-SEP-2026, entry version 138. DE RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01974}; DE Short=MAP {ECO:0000255|HAMAP-Rule:MF_01974}; DE Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01974}; DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01974}; DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01974}; GN Name=map {ECO:0000255|HAMAP-Rule:MF_01974}; OrderedLocusNames=TC_0240; OS Chlamydia muridarum (strain MoPn / Nigg). OC Bacteria; Pseudomonadati; Chlamydiota; Chlamydiia; Chlamydiales; OC Chlamydiaceae; Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=243161; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MoPn / Nigg; RX PubMed=10684935; DOI=10.1093/nar/28.6.1397; RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O., RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S., RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J., RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G., RA Salzberg S.L., Eisen J.A., Fraser C.M.; RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae RT AR39."; RL Nucleic Acids Res. 28:1397-1406(2000). 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. {ECO:0000255|HAMAP- CC 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:0000255|HAMAP-Rule:MF_01974}; CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01974}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01974}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01974}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|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:0000255|HAMAP-Rule:MF_01974}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01974}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01974}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF39111.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE002160; AAF39111.1; ALT_INIT; Genomic_DNA. DR PIR; G81724; G81724. DR RefSeq; WP_010229916.1; NC_002620.2. DR AlphaFoldDB; Q9PL68; -. DR SMR; Q9PL68; -. DR GeneID; 1246409; -. DR KEGG; cmu:TC_0240; -. DR eggNOG; COG0024; Bacteria. DR HOGENOM; CLU_015857_0_0_0; -. DR OrthoDB; 9802055at2; -. DR Proteomes; UP000000800; 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; 3.10.450.50; -; 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 InterPro; IPR004027; SEC_C_motif. DR NCBIfam; TIGR00500; met_pdase_I; 1. DR NCBIfam; NF008970; PRK12318.1; 1. DR PANTHER; PTHR43330; METHIONINE AMINOPEPTIDASE; 1. DR PANTHER; PTHR43330:SF27; METHIONINE AMINOPEPTIDASE; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR Pfam; PF02810; SEC-C; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1. DR SUPFAM; SSF103642; Sec-C motif; 1. DR PROSITE; PS00680; MAP_1; 1. PE 3: Inferred from homology; KW Aminopeptidase; Hydrolase; Metal-binding; Protease; Reference proteome. FT CHAIN 1..291 FT /note="Methionine aminopeptidase" FT /id="PRO_0000148932" FT BINDING 118 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974" FT BINDING 135 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974" FT BINDING 146 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974" FT BINDING 146 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_01974" FT BINDING 209 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_01974" FT BINDING 216 FT /ligand="substrate" FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_01974" FT BINDING 273 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01974" FT BINDING 273 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_01974" SQ SEQUENCE 291 AA; 32646 MW; BAA33E190FC6160E CRC64; MKRNDPCWCG SQKKWKHCHY PTKPERPSDN LRQLYASRYD IIIKTPDQIE KIRKACQVTA RILDALCKAA KEGVTTNELD QLSCNLHKQY NAIPAPLNYG QPPFPKTICT SLNEVICHGI PNDTPLQNGD IMNIDVSCIV DGFYGDCSRM VMIGEVPEIK KKVCEASLEA LNAAIAILEP NLPLYEIGEV IENCAARYGF SVVDQFVGHG VGVRFHENPY VAHHRNSCKI PLAPGMTFTI EPMINVGKKE GFIDPTNHWE ARTCDHQPSA QWEHTVLITD SGYEILTLLD N //