Detail Information for IndEnz0002014361
IED ID IndEnz0002014361
Enzyme Type ID protease014361
Protein Name Peptidyl-Asp metalloendopeptidase
EC 3.4.24.33
Endopeptidase Asp-N
Gene Name Smlt0970
Organism Stenotrophomonas maltophilia (strain K279a)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Stenotrophomonas Stenotrophomonas maltophilia group Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia) Stenotrophomonas maltophilia (strain K279a)
Enzyme Sequence MLSRSIGKAAGGLVLGLSVAAAAHAAPLFEPVTVISRASANSEPALGKLLATPSTATVQEVRVDAAATAQPQLEFELLGKRVQAVRSKVEALPDGGSIWYGQFRSPSDRLTAATSSGQDDPGNSLILVRSGDTITGSIRKDGKLYRLRPLGNRHVLVEVDESRMPADHPADYNQLPKIPMADNDHIGIAQASSGTPATIRVLVVATNAAVTAYGGNMQSLVQLAVAESNQGYVNSNVGLTLQLAGYETTNYSESGNFTTDLSRFRGTSDGYMDSIHTSRNTTAADVGVLLINNSAYCGLASGIGSTASTAFAAVYWDCATGYYSFAHEIGHLQSARHDIATDSSTSPYAYGHGYRYEPATGTGWRTIMAYNCTRSCPRLNYWSNPNISYNGIPMGNASTADNQRVLVNTKATIAAFR
Enzyme Length 417
Uniprot Accession Number B2FQP3
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;Reference proteome;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 44,141
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