ID AMPA_ACAM1 Reviewed; 492 AA. AC B0CCF6; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 02-SEP-2026, entry version 84. DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; DE EC=3.4.11.1 {ECO:0000255|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; DE Short=LAP {ECO:0000255|HAMAP-Rule:MF_00181}; DE EC=3.4.11.10 {ECO:0000255|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00181}; GN Name=pepA {ECO:0000255|HAMAP-Rule:MF_00181}; GN OrderedLocusNames=AM1_2989; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Acaryochloridales; OC Acaryochloridaceae; Acaryochloris. OX NCBI_TaxID=329726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017; RX PubMed=18252824; DOI=10.1073/pnas.0709772105; RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., RA Blankenship R.E., Touchman J.W.; RT "Niche adaptation and genome expansion in the chlorophyll d-producing RT cyanobacterium Acaryochloris marina."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008). CC -!- FUNCTION: Presumably involved in the processing and regular turnover of CC intracellular proteins. Catalyzes the removal of unsubstituted N- CC terminal amino acids from various peptides. {ECO:0000255|HAMAP- CC Rule:MF_00181}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa CC is preferably Leu, but may be other amino acids including Pro CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and CC methyl esters are also readily hydrolyzed, but rates on arylamides CC are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00181}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal amino acid, preferentially leucine, CC but not glutamic or aspartic acids.; EC=3.4.11.10; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00181}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00181}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000255|HAMAP- CC Rule:MF_00181}. 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; CP000828; ABW27985.1; -; Genomic_DNA. DR RefSeq; WP_012163418.1; NC_009925.1. DR AlphaFoldDB; B0CCF6; -. DR SMR; B0CCF6; -. DR STRING; 329726.AM1_2989; -. DR MEROPS; M17.A03; -. DR KEGG; amr:AM1_2989; -. DR eggNOG; COG0260; Bacteria. DR HOGENOM; CLU_013734_5_1_3; -. DR OrthoDB; 9809354at2; -. DR Proteomes; UP000000268; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd00433; Peptidase_M17; 1. DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1. DR InterPro; IPR011356; Leucine_aapep/pepB. DR InterPro; IPR043472; Macro_dom-like. DR InterPro; IPR000819; Peptidase_M17_C. DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept. DR InterPro; IPR008283; Peptidase_M17_N. DR NCBIfam; NF002073; PRK00913.1-2; 1. DR NCBIfam; NF002074; PRK00913.1-4; 1. DR NCBIfam; NF002076; PRK00913.2-3; 1. DR NCBIfam; NF002083; PRK00913.3-5; 1. DR PANTHER; PTHR11963:SF23; CYTOSOL AMINOPEPTIDASE; 1. DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1. DR Pfam; PF00883; Peptidase_M17; 1. DR Pfam; PF02789; Peptidase_M17_N; 1. DR PRINTS; PR00481; LAMNOPPTDASE. DR SUPFAM; SSF52949; Macro domain-like; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00631; CYTOSOL_AP; 1. PE 3: Inferred from homology; KW Aminopeptidase; Cytoplasm; Hydrolase; Manganese; Metal-binding; Protease; KW Reference proteome. FT CHAIN 1..492 FT /note="Probable cytosol aminopeptidase" FT /id="PRO_1000077272" FT ACT_SITE 274 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT ACT_SITE 349 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 262 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 267 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 267 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 286 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 345 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 347 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" FT BINDING 347 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00181" SQ SEQUENCE 492 AA; 51870 MW; AAFF301F74DD17C8 CRC64; MKIQAIETVA ADWSGDYLGI GFFEDSAAID AGLTQLDQSL QDILQDLVSE TEFQGKVGEQ PWTRIAGPGS IRKVMLIGLG SPDAFTLDSL RQAAAAFAKA AQKQKAASAG LQLPSWDDDA AASTQAMAEG IELALHQEIR FKSDPDAKKP GEFPQEVHLL GLANQAAAIE KAQQICAGVI LTRELVAAPA NVVTPSALAE TAAQIAEDHG LTLEVLEREE CEAQGMGAFL GVSLASELPP KFIHLTYKPS GTPRRKLAIV GKGVTFDSGG LNLKVGGSGI ETMKMDMAGS GATLGAAKAI GQLKPDVEVH FIVAAAENMI SGHALHPGDI LTASNGKTIE INNTDAEGRL TLADALVFAE KQGVDAIVDL ATLTGACIVA LGNDIAGMWT PEDSLAEELS QASEQAGEKF WRMPLEEKYF EGLKSPIADM KNTGPRPGGS ITAALFLKQY IENTPWAHLD VAGPVWTEKE NGYLNVGATG FAVRTLVNWV MG //