Detail Information for IndEnz0002016374
IED ID IndEnz0002016374
Enzyme Type ID protease016374
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Pfl01_0989
Organism Pseudomonas fluorescens (strain Pf0-1)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas fluorescens group (fluorescent pseudomonads) Pseudomonas fluorescens Pseudomonas fluorescens (strain Pf0-1)
Enzyme Sequence MELVVKSVSPETLKTATLVVAVGEGRKLGAAARQVDELSGGAISAVLKRGDLAGKVGQSLLLHSLPNLKAERVLLVGVGKDEELGDRPFRKIVAGILNTLKGLGGSDAVLALDEIIVKNRDSYGKTRLLAETLVDGEYTFDQFKSQKAEPRALKKITLLTIKAAQAEVQRAVNHATAIANGMAFTRNLGNLPPNICHPTFLGEQAKNLGKEFKDLKVEVLDEKKIKSLGMGSFYAVGQGSAQPPRLIVMQYNGGKKSEKPYALVGKGITFDTGGISLKPGAGMDEMKYDMGGAASVFGTLRAVLELKLPINLVCILACAENMPSGTASRPGDIVTTMSGQTVEILNTDAEGRLVLCDALTYSERFKPQAVIDIATLTGACVVALGAHTSGLLGNNDELIEQLLSAGKAADDRAWQLPLFDEYQEQLDSPFADIANIGGPKAGTITAACFLSRFTKNLNWAHLDIAGTAWTSGGKDKGATGRPVPLLTQYLLDRAKA
Enzyme Length 496
Uniprot Accession Number Q3KHM4
Absorption
Active Site ACT_SITE 278; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 352; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.; EC=3.4.11.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00181}; CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.; EC=3.4.11.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00181};
DNA Binding
EC Number 3.4.11.1; 3.4.11.10
Enzyme Function FUNCTION: Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. {ECO:0000255|HAMAP-Rule:MF_00181}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Metal binding (7)
Keywords Aminopeptidase;Cytoplasm;Hydrolase;Manganese;Metal-binding;Protease
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00181}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 52,570
Kinetics
Metal Binding METAL 266; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 271; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 271; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 289; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 348; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 350; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 350; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda