ID A0A5C2END3_XANOQ Unreviewed; 490 AA. AC A0A5C2END3; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 27-MAR-2024, entry version 13. DE RecName: Full=Probable cytosol aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE EC=3.4.11.1 {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucine aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; DE Short=LAP {ECO:0000256|HAMAP-Rule:MF_00181}; DE EC=3.4.11.10 {ECO:0000256|HAMAP-Rule:MF_00181}; DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|HAMAP-Rule:MF_00181}; GN Name=pepA {ECO:0000256|HAMAP-Rule:MF_00181, GN ECO:0000313|EMBL:QEO95914.1}; GN ORFNames=XOCgx_0920 {ECO:0000313|EMBL:QEO95914.1}; OS Xanthomonas oryzae pv. oryzicola. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=129394 {ECO:0000313|EMBL:QEO95914.1, ECO:0000313|Proteomes:UP000327049}; RN [1] {ECO:0000313|EMBL:QEO95914.1, ECO:0000313|Proteomes:UP000327049} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GX01 {ECO:0000313|EMBL:QEO95914.1, RC ECO:0000313|Proteomes:UP000327049}; RA Niu X., Carpenter S.C.D., Li Y., Zhu P., Yang X., Huang P., Zhang Z., RA Wang L., Jiang W., Huang S., Bogdanove A.J., Tang J., He Y.; RT "The complete genome sequences of a highly virulence strain of Xanthomonas RT oryzae pv. oryzicola isolated from Guangxi, China."; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00000135, ECO:0000256|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:0000256|ARBA:ARBA00000967, ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00181}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00181}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181}. CC -!- SIMILARITY: Belongs to the peptidase M17 family. CC {ECO:0000256|ARBA:ARBA00009528, ECO:0000256|HAMAP-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; CP043403; QEO95914.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5C2END3; -. DR Proteomes; UP000327049; 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:UniProtKB-KW. 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 PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1. DR PANTHER; PTHR11963:SF23; ZGC:152830; 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 {ECO:0000256|ARBA:ARBA00022438, ECO:0000256|HAMAP- KW Rule:MF_00181}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00181}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00181}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00181}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00181}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00181}. FT DOMAIN 342..349 FT /note="Cytosol aminopeptidase" FT /evidence="ECO:0000259|PROSITE:PS00631" FT ACT_SITE 274 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT ACT_SITE 348 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 262 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 267 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 267 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 285 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 344 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 346 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" FT BINDING 346 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00181" SQ SEQUENCE 490 AA; 51065 MW; B69AE222BBB3DA82 CRC64; MALQFTLNQD APASAAVDCI VVGVFADKTL SPAAQALDSA SQGRLTALVA RGDVAGKTGS TTLLHDLPGV AAPRVLVVGL GDAGKFGVAP YLKAIGDATR ALKTGAVGTA LLTLTELTVK ARDAAWNIRQ AVTVSDHAAY RYTATLGKKK VDETGLTTLA IAGDDARALA VGVATAEGVE FARELGNLPP NYCTPAYLAD TAAAFAGKFP GAEAEILDEA QMEALGMGSL LSVARGSANR PRLIVLKWNG GGDARPYVLV GKGITFDTGG VNLKTQGGIE EMKYDMCGGA TVIGTFVATV KAELPINLVV VVPAVENAID GNAYRPSDVI TSMSGKTIEV GNTDAEGRLI LCDALTYAER FNPEALVDVA TLTGACMVAL GHQTAGLMSK HDDLANELLA AGEHVFDRGW RLPLWDEYQS LLDSTFADVY NIGGRWGGAI TAGCFLSRFT ENQRWAHLDI AGVASDEGKR GMATGRPVGL LTQWLLDRAA //