Detail Information for IndEnz0002005639
IED ID IndEnz0002005639
Enzyme Type ID protease005639
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Ava_2727
Organism Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis)
Taxonomic Lineage cellular organisms Bacteria Terrabacteria group Cyanobacteria/Melainabacteria group Cyanobacteria Nostocales Nostocaceae Trichormus Anabaena variabilis Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis)
Enzyme Sequence MAIQLSDKPLLEWAGDTLAIALFEDAVELTGELASLDEKFAGILKELIAEEEFTGKANSTVFTRVSANIPVRKIILVGLGKTEAFNIDTLRRAAAAVGKVGKKQKSKVIGLSFPLWNNDPTASSQAIAEGVQLALYQDNRFKSDPDDKGSQVETVELLGFAGQEAAINRANQIVSGVILARQLVAAPANSVTPITMAETAQQIAQDYGLQIEILEQEDCEKLGMGAFLGVALASDLPPKFIHLTYKPESTPKRKLAIVGKGLTFDSGGLNIKGAGSGIETMKIDMGGAAATLGAAKAIAQIKPNVEVHFISAVTENMISGKAMHPGDILTASNGKTIEVNNTDAEGRLTLADALVYTDKLGLDAIVDLATLTGANVIALGDDIAGLYTPDDALAGQLEQAASESGEKIWRMPLEEKYFEGLKSGIADMKNTGPRPGGSITAALFLKQFVKDTPWAHLDIAGPVWADKENGYNGPGATGYGVRLLVDWVLSE
Enzyme Length 491
Uniprot Accession Number Q3M9J6
Absorption
Active Site ACT_SITE 272; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 347; /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 51,902
Kinetics
Metal Binding METAL 260; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 265; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 265; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 284; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 343; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 345; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 345; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda