Detail Information for IndEnz0002016678
IED ID IndEnz0002016678
Enzyme Type ID protease016678
Protein Name Probable cytosol aminopeptidase
EC 3.4.11.1
Leucine aminopeptidase
LAP
EC 3.4.11.10
Leucyl aminopeptidase
Gene Name pepA Tgr7_2140
Organism Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Chromatiales Ectothiorhodospiraceae (purple sulfur bacteria) Thioalkalivibrio Thioalkalivibrio sulfidiphilus Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Enzyme Sequence MEFSVKSGNPEKQRSACVVVGVFDRRKLSSAARVLDKASGGALSTILRRGDMDGEKGQTLWLYNLPNTLCERVLLVGCGKERDFDEPAYRSVIATVARTVNKSGAVEAVNYLTDLPVKGRDTLWKISQAVTITQDSLYSFQQLKSKKEDTQRPLKRIILSVPSRADLLPGEDAVRVATAISVGTKLTRDLANLPGNICNPTYLAEQALQLKKTYKGLKVEILEEADMEKLGMGALLSVSRGSEQPAKLITLEYRGGRKDAKPVVLVGKGITFDTGGISLKPGAEMDEMKFDMCGAASVLGVMKAVAEMMLPINLVGVVAAAENMPDGKATRPGDVVTSMSGQTIEILNTDAEGRLVLCDALSYVERFDPDVVIDIATLTGACIIALGHQATGLLSNHSPLANDLLGAGKQSYDRAWELPLWDEYQEQLKSNFADMANIGGRPAGTITAACFLSRFTKKYKWAHLDIAGVAWKSGKEKGATGRPVPLLMQYLLNKAS
Enzyme Length 496
Uniprot Accession Number B8GTX6
Absorption
Active Site ACT_SITE 280; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; ACT_SITE 354; /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;Reference proteome
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 53,570
Kinetics
Metal Binding METAL 268; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 273; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 273; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 291; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 350; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 352; /note=Manganese 1; /evidence=ECO:0000255|HAMAP-Rule:MF_00181; METAL 352; /note=Manganese 2; /evidence=ECO:0000255|HAMAP-Rule:MF_00181
Rhea ID
Cross Reference Brenda