Detail Information for IndEnz0002019081
IED ID IndEnz0002019081
Enzyme Type ID protease019081
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Plut_0954
Organism Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon luteolum)
Taxonomic Lineage cellular organisms Bacteria FCB group Bacteroidetes/Chlorobi group Chlorobi Chlorobia Chlorobiales Chlorobiaceae Chlorobium/Pelodictyon group Pelodictyon Pelodictyon luteolum Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon luteolum)
Enzyme Sequence MKTAATFSALQDLDADLLIFPFSSEGLKKAASPVLEAAGLSDAPLDDFKAAAGDTLVLYPRPGKLRAPRVMLVGTGEAGSLDDWHRAATAAASRAVDLEARRIVFDLPAAGGKAKPGIEAVAETLVEGCLFGAYRFERLKSGKLDKGEKKTAAKGKAKKAEKGIDLLTLRVPASALAAAEKGMASGLVIGSAQEMARNLVNLPGNHLQAEDIARAAAASGKQYGYGVTVLRKKEIESLRMGGLVAVNQGSLNPPTFTVMDYVPKKKAKATIALVGKGVTFDSGGISIKPSEGMGDMKSDMAGAAAVIGAVEAAARLALPVRIIGLIPATDNMPDGNAQKPGDVITTYSGITVEVGNTDAEGRLILADALTYAAQKYSPDAIIDLATLTGACIVALGYQVAGLFSNDDALAGAIEGAARDTGEKVWRLPLWELYDEQIKSDVADVSNTGSRGAGTITAAKFLEKFIDGHKKWAHIDIAGPSFPAKGAAKVNGGSGFGVRLLVELLRKWS
Enzyme Length 508
Uniprot Accession Number Q3B4B5
Absorption
Active Site ACT_SITE 288; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 362; /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 52,743
Kinetics
Metal Binding METAL 276; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 281; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 281; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 299; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 358; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 360; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 360; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda