Detail Information for IndEnz0002014360
IED ID IndEnz0002014360
Enzyme Type ID protease014360
Protein Name Peptidyl-Asp metalloendopeptidase
EC 3.4.24.33
Endopeptidase Asp-N
Gene Name Smal_0815
Organism Stenotrophomonas maltophilia (strain R551-3)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Stenotrophomonas Stenotrophomonas maltophilia group Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia) Stenotrophomonas maltophilia (strain R551-3)
Enzyme Sequence MLSRSIGKAAGGLVLGLSVAAAAHAAPLFEPVTVLSRAAAGSEPALGKLLATPSTATVQEVRVDAAATAQPQLEFELLGQRVQAVRSKVESLPDGGSIWYGQFRSPSDRLTAATSNGQDDPGNSVILVRSGNTVTGSIRKDGKLYRLRPLGNRHVLVEVDESRMPADHPADYNQLPKIPMGNNDRIGIAQASSGTPATIRVLVVATNAAVAAYGGNMQSLVQLAVAESNQGYVNSNVGITLQLAGYETTSYTESGNFTTDLTRFRNTSDGYMDSIHTSRNNTAADVGVLLINNTSYCGLASGIGSTASTAFAAVYWDCATGYYSFAHEIGHLQSARHDIASDPSTSPYAYGHGYRYEPASGSRWRTIMAYDCSAGCPRLNYWSNPNISYNGVPMGIASSADNQRVLVNTKATIAAFR
Enzyme Length 417
Uniprot Accession Number B4SLL0
Absorption
Active Site ACT_SITE 328; /evidence="ECO:0000250|UniProtKB:O75173, ECO:0000255|PROSITE-ProRule:PRU10095"
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Cleavage of Xaa-|-Asp, Xaa-|-Glu and Xaa-|-cysteic acid bonds.; EC=3.4.24.33; Evidence={ECO:0000250|UniProtKB:Q9R4J4};
DNA Binding
EC Number 3.4.24.33
Enzyme Function FUNCTION: Metalloprotease, specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues. {ECO:0000250|UniProtKB:Q9R4J4}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (3); Signal peptide (1)
Keywords Hydrolase;Metal-binding;Metalloprotease;Protease;Signal;Zinc
Interact With
Induction
Subcellular Location
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..25; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 44,067
Kinetics
Metal Binding METAL 327; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:O75173, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 331; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:O75173, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 337; /note="Zinc; catalytic"; /evidence="ECO:0000250|UniProtKB:O75173, ECO:0000255|PROSITE-ProRule:PRU10095"
Rhea ID
Cross Reference Brenda