Detail Information for IndEnz0002008365
IED ID IndEnz0002008365
Enzyme Type ID protease008365
Protein Name Presequence protease, mitochondrial
EC 3.4.24.-
Pitrilysin metalloproteinase 1
Gene Name pitrm1 zgc:55469
Organism Danio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Actinopterygii Actinopteri Neopterygii Teleostei Osteoglossocephalai Clupeocephala Otomorpha Ostariophysi Otophysi Cypriniphysae Cypriniformes (carps and others) Cyprinoidei Danionidae Danioninae Danio Danio rerio (Zebrafish) (Brachydanio rerio)
Enzyme Sequence MFRQSKTIITKLTNLSFQGSWRSRGSSAVEKALKYTVGQKIHNFTVKEVTAVPDLFLTAVKLSHDATGAQYLHAARDDSNNLFSVLFRTTPMDSTGVPHILEHTVLCGSQRFPCRDPFFKMLNRSLSTFMNAFTASDYTMYPFSTQNAKDFQNLLSVYLDAVFFPCLRELDFWQEGWRLEHENPTDPSSPLVFKGVVFNEMKGVFSDNERLYAQHLQNKLLPDHTYSVVSGGEPLAIPELTWEQLKHFHATHYHPSNARFFTYGDLPLEQHLQQIEEEAMSKFERTEPNTAVPPQTPWDKPRMDHVSCRPDALAPDPVKQNTLCMSFLLGDITDTFEMFTLSLLSSLMMSGPNSPFYKALIEPKIGSDFSSSAGFDGSTRQASFTIGLQGMAEDDTETVKHIIAQTIDDIIASGFEEEQIEALLHKIEIQMKHQSTSFGLALASYIASLWNHDGDPVQLLKISESVSRFRQCLKENPRYLQEKVQHYFKNNTHQLTLSMSPDERFLEKQAEAEEQKLQQKIQILSSEDRKDIYEKGLQLLAVQSTTQDASCLPALKVSDIEPIIPYTPVQPGAAGGVPVQYCEQPTNGMVYFRAMSNINSLPEDLKIYVPLFCSVITKMGSGMLDYRQQAQRIELKTGGLSVSPQIIPDTEDLDLYEQGIILSSSCLERNLPDMFQLWSDLFNSPRFDDEERLRVLVMMSAQELSNGISYSGHMYAMTRAARSLTPTADLQESFSGMDQVKFMKRIAEMTDLTSILRKLPRIKRHLFNPENMRCALNATPQKMPDVAAEVERFIGNIAGNRKERKPVRPSVVERALGPEAGAAATRKLISEAHFKPCQMKTYFQLPFNVNFVSECVRTVPFTHADYASLCILGRMMTAKFLHGEIREKGGAYGGGARMGGGGLFSFYSYRDPNSTQTLSAFRGGVEWARAGKFTQQDIDEAKLSVFSAVDAPVAPSDKGLGRFLNGITDEMKQAHRERLFAVTERNLIDVAGRYLGIGQQTCGVAILGPENESIRKDPSWVVK
Enzyme Length 1023
Uniprot Accession Number Q7ZVZ6
Absorption
Active Site ACT_SITE 102; /note=Proton acceptor; /evidence=ECO:0000250|UniProtKB:Q5JRX3
Activity Regulation ACTIVITY REGULATION: Mainly exists in a closed and catalytically competent conformation but a closed-to-open switch allows substrate entry into the catalytic chamber. Substrate binding induces closure and dimerization. A disulfide bond may lock the enzyme in a closed conformation preventing substrate entry into the catalytic chamber, participating in redox regulation of the enzyme. Inhibited by metal-chelating agents. Inhibited by nickel and zinc excess, and slightly activated by manganese. {ECO:0000250|UniProtKB:Q5JRX3}.
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Metalloendopeptidase of the mitochondrial matrix that functions in peptide cleavage and degradation rather than in protein processing. Has an ATP-independent activity. Specifically cleaves peptides in the range of 5 to 65 residues. Shows a preference for cleavage after small polar residues and before basic residues, but without any positional preference. Degrades the transit peptides of mitochondrial proteins after their cleavage. Also degrades other unstructured peptides. {ECO:0000250|UniProtKB:Q5JRX3}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (1); Metal binding (3); Transit peptide (1)
Keywords Disulfide bond;Hydrolase;Metal-binding;Metalloprotease;Mitochondrion;Protease;Reference proteome;Transit peptide;Zinc
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q5JRX3}.
Modified Residue
Post Translational Modification PTM: A disulfide bond locks the enzyme in the closed conformation preventing substrate entry into the catalytic chamber. {ECO:0000250|UniProtKB:Q5JRX3}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 23922661;
Motif
Gene Encoded By
Mass 114,972
Kinetics
Metal Binding METAL 99; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q5JRX3; METAL 103; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q5JRX3; METAL 200; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q5JRX3
Rhea ID
Cross Reference Brenda