Detail Information for IndEnz0002008199
IED ID IndEnz0002008199
Enzyme Type ID protease008199
Protein Name Presequence protease 1, chloroplastic/mitochondrial
AtPreP1
PreP 1
EC 3.4.24.-
Zinc metalloprotease 1
AtZnMP1
Gene Name PREP1 ZNMP1 At3g19170 MVI11.6 MVI11.7 MVI11_8
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MLRTVSCLASRSSSSLFFRFFRQFPRSYMSLTSSTAALRVPSRNLRRISSPSVAGRRLLLRRGLRIPSAAVRSVNGQFSRLSVRAVATQPAPLYPDVGQDEAEKLGFEKVSEEFISECKSKAILFKHKKTGCEVMSVSNEDENKVFGVVFRTPPKDSTGIPHILEHSVLCGSRKYPVKEPFVELLKGSLHTFLNAFTYPDRTCYPVASTNTKDFYNLVDVYLDAVFFPKCVDDAHTFQQEGWHYELNDPSEDISYKGVVFNEMKGVYSQPDNILGRIAQQALSPENTYGVDSGGDPKDIPNLTFEEFKEFHRQYYHPSNARIWFYGDDDPVHRLRVLSEYLDMFEASPSPNSSKIKFQKLFSEPVRLVEKYPAGRDGDLKKKHMLCVNWLLSEKPLDLQTQLALGFLDHLMLGTPASPLRKILLESGLGEALVSSGLSDELLQPQFGIGLKGVSEENVQKVEELIMDTLKKLAEEGFDNDAVEASMNTIEFSLRENNTGSFPRGLSLMLQSISKWIYDMDPFEPLKYTEPLKALKTRIAEEGSKAVFSPLIEKLILNNSHRVTIEMQPDPEKATQEEVEEKNILEKVKAAMTEEDLAELARATEELKLKQETPDPPEALRCVPSLNLGDIPKEPTYVPTEVGDINGVKVLRHDLFTNDIIYTEVVFDIGSLKHELLPLVPLFCQSLLEMGTKDLTFVQLNQLIGRKTGGISVYPLTSSVRGKDEPCSKIIVRGKSMAGRADDLFNLMNCLLQEVQFTDQQRFKQFVSQSRARMENRLRGSGHGIAAARMDAMLNIAGWMSEQMGGLSYLEFLHTLEKKVDEDWEGISSSLEEIRRSLLARNGCIVNMTADGKSLTNVEKSVAKFLDLLPENPSGGLVTWDGRLPLRNEAIVIPTQVNYVGKAGNIYSTGYELDGSAYVISKHISNTWLWDRVRVSGGAYGGFCDFDSHSGVFSYLSYRDPNLLKTLDIYDGTGDFLRGLDVDQETLTKAIIGTIGDVDSYQLPDAKGYSSLLRHLLGVTDEERQRKREEILTTSLKDFKDFAQAIDVVRDKGVAVAVASAEDIDAANNERSNFFEVKKAL
Enzyme Length 1080
Uniprot Accession Number Q9LJL3
Absorption
Active Site ACT_SITE 165; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:16601675; ACT_SITE 240; /evidence=ECO:0000305
Activity Regulation ACTIVITY REGULATION: Inactive in the absence of MgCl(2) and CaCl(2) and full activation at 10 mM concentrations of either ion. Completely inhibited by the metal chelator orthophenanthroline, but not affected by phenylmethylsulfonyl fluoride (PMSF) or N-ethylmaleimide (NEM).
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: ATP-independent protease that degrades both mitochondrial and chloroplastic transit peptides after their cleavage. Also degrades other unstructured peptides. Specific for peptides in the range of 10 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, with a bias for positively charged amino acid residues. {ECO:0000269|PubMed:12138166}.
Temperature Dependency BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 28 degrees Celsius. Active from 4 to 40 degrees Celsius.;
PH Dependency BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Active from pH 4 to 10.;
Pathway
nucleotide Binding
Features Active site (2); Beta strand (30); Chain (1); Coiled coil (1); Erroneous initiation (1); Helix (49); Metal binding (3); Modified residue (1); Mutagenesis (18); Transit peptide (1); Turn (9)
Keywords 3D-structure;Acetylation;Alternative splicing;Chloroplast;Coiled coil;Hydrolase;Magnesium;Metal-binding;Metalloprotease;Mitochondrion;Plastid;Protease;Reference proteome;Transit peptide;Zinc
Interact With P17614
Induction
Subcellular Location SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Mitochondrion matrix.
Modified Residue MOD_RES 86; /note=N-acetylvaline; /evidence=ECO:0007744|PubMed:22223895
Post Translational Modification
Signal Peptide
Structure 3D X-ray crystallography (1)
Cross Reference PDB 2FGE;
Mapped Pubmed ID 12938931; 14576160; 14730085; 15028209; 15047901; 15276459; 16207701; 16502469; 16766689; 17081117; 18230142; 18431481; 18538804; 18633119; 18650403; 19423572; 19646442; 19701724; 21333657; 21621546; 21798377; 21995547; 22995300; 24373893; 28627464; 30242930; 32663165; 33229537;
Motif
Gene Encoded By
Mass 121,015
Kinetics
Metal Binding METAL 162; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16601675; METAL 166; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16601675; METAL 262; /note=Zinc; catalytic; /evidence=ECO:0000269|PubMed:16601675
Rhea ID
Cross Reference Brenda