Detail Information for IndEnz0002019078
IED ID IndEnz0002019078
Enzyme Type ID protease019078
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA BMEI1261
Organism Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Alphaproteobacteria Hyphomicrobiales Brucellaceae Brucella/Ochrobactrum group Brucella Brucella melitensis Brucella melitensis bv. 1 Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Enzyme Sequence MKYRKRGWPSCWWPRAAVLPMRRQGVGGAEKIVRIADISGFTGALGKTAEAIETTPAGVEKIVLVGVGEPGKLGNDDWLKIGGAAFSQIGNAERVTLTLALPETTIAGDEAADVALGMVLRSYKFDRYKTRKSEENGEPKHAAKITVCVADTHSARKAFEVAEAVADGVIQARNLVNEPANILGPVEFAEEAEKLEKLGVKVEVLGEKELKKLGMGALLGVAQGSVRPPRLVVMEWHGAKGKEKPIAFVGKGVVFDTGGISIKPAANMEDMKGDMGGAAAVTGLMRALAGRKAKVNAIGVIGLVENMPDGNAQRPGDIVTSMSGQTIEVINTDAEGRLVLADALHYTNDRFKPRFIINLATLTGAVMVALGQYHAGLFSNDDELADQLYDAGQSTGEKLWRLPLGTEYDKMIDSKFADMKNSAGRYGGSITAAQFLKRFVGETPWAHLDVAGTAMGSPANEYNQSWASGFGVRLLDRLVRDQFES
Enzyme Length 485
Uniprot Accession Number Q8YG99
Absorption
Active Site ACT_SITE 263; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 337; /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 51,868
Kinetics
Metal Binding METAL 251; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 256; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 256; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 274; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 333; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 335; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 335; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda