ID A0A7U6L7I7_ENTAV Unreviewed; 250 AA. AC A0A7U6L7I7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 19-JAN-2022, entry version 3. 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_2 {ECO:0000313|EMBL:BBM19457.1}; GN Synonyms=map {ECO:0000256|HAMAP-Rule:MF_01974}; GN ORFNames=G15_3137 {ECO:0000313|EMBL:BBM19457.1}; OS Enterococcus avium (Streptococcus avium). OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=33945 {ECO:0000313|EMBL:BBM19457.1, ECO:0000313|Proteomes:UP000509820}; RN [1] {ECO:0000313|Proteomes:UP000509820} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=G-15 {ECO:0000313|Proteomes:UP000509820}; RA Sugiyama M., Noda M.; RT "antibiotic susceptibility of plant-derived lactic acid bacteria."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. 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; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01974, CC ECO:0000256|RuleBase:RU003653}; 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, ECO:0000256|RuleBase:RU003653}; 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}. 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; AP019814; BBM19457.1; -; Genomic_DNA. DR Proteomes; UP000509820; 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 CDD; cd01086; MetAP1; 1. DR Gene3D; 3.90.230.10; -; 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 Pfam; PF00557; Peptidase_M24; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF55920; SSF55920; 1. DR TIGRFAMs; TIGR00500; met_pdase_I; 1. PE 3: Inferred from homology; KW Aminopeptidase {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01974}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01974, KW ECO:0000256|RuleBase:RU003653}; KW Protease {ECO:0000256|HAMAP-Rule:MF_01974, ECO:0000256|RuleBase:RU003653}. FT DOMAIN 12..239 FT /note="Peptidase_M24" FT /evidence="ECO:0000259|Pfam:PF00557" FT METAL 94 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 105 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 105 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 168 FT /note="Divalent metal cation 2; catalytic; via tele FT nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 201 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 232 FT /note="Divalent metal cation 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT METAL 232 FT /note="Divalent metal cation 2; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 77 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" FT BINDING 175 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01974" SQ SEQUENCE 250 AA; 27097 MW; 2086353ECE602675 CRC64; MVTLKSSREI DQMKESGAIL AGIHKQLRDI IVPGITTKEI NQFVQEKVEA VGATAAQIGF EGYEFATCTS VNDEICHGFP SNYRLKSGDV LKVDFCVDYH GAISDSCWTY AVGEITPEHQ ALMDVTKEAL MIGIAQAQVG NRVGDIGHAI QVYAEGKGYG VVQDFLAHGI GPTIHEEPFF PHFGTAGKGP RLKEGMTITI EPMITTGTWE AGIDGNGWTA RTLDGSFCAQ YEHSIAITKE GPIIMTEQDD //