| IED ID | IndEnz0002012801 |
| Enzyme Type ID | protease012801 |
| Protein Name |
Presequence protease, mitochondrial EC 3.4.24.- Pitrilysin metalloproteinase 1 |
| Gene Name | pitrm1 TNeu116i05.1 |
| Organism | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Silurana Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Enzyme Sequence | MIRQCRAGLRLCRALYQTSYRWHGKSACERALRYAPGESIHGFTVNEVTPVPELFLTAVKLSHDNTGAKYLHVAREDSNNLFSVQFRTTPLDSTGVPHILEHTVLCGSQKYPCRDPFFKMLNRSLSTFMNAFTASDYTMYPFSTQNAKDFQNLLSVYLDAVFFPCLRELDFWQEGWRLEHENPEDPNSPLIFKGIVFNEMKGAFTDNEKVFSQHLQNKLLPDHTYSVVSGGEPLNIPDLTWEQLKQFHATHYHPSNARFFTYGNLPLEIHLKQIHEDALSKFERIDPKTSVPPQERWQSPREYSISCGTDSFASDPEKQTTVSVNFLLSEITDTFEAFTLSLLSSLMVDGPNSPFYKALIEANLGTDFSPDTGFNNYTRETYFSIGLQGINKEDSEKVKAIINKTINEVAEHGIEAERIEALLHKLEIQMKHQSTSFGLTLASYVASCWNHEGDPVDLLKIGDKISRFRECLKENPKFLQDKVKQYFQVSQHRMTLSMSPDEQHYDKEAQLEAEKLTQKVKALSEEERKQIYEKGLELIRLQSKPQDASCLPALKVSDIEPKIPLTDLDITYAGDVPVQYCAQPTNGMVYFRAVSSLNTLPEELKPYVPLFCSVITKLGCGVYNYREQAQQMELTTGGMSVCPHIITDDSNLDTYEQGVVFSSLCLDRNLPDMMHLWSEIFNSPHFDDEERLRVLVRMSAQEMSNGIPDSGHVYASIRAGRTLTPAGELQELFSGMDQVKMIKRIAEMPEMGPILRKLSRIRKYVLLSDNMRCSVNATPQQMPVASKEIEHFLAGISRSKKERKSIRPHVVEKSSSPSSSGSEISRRATRKLVGDPTFKPCQMKTHFSLSFPVNYIGECVRTVPYTHPDYASLRILARIMTAKFLHGEIREKGGAYGGGAKLSFDGIFGFYSYRDPNSLSTLSTFQKAADWAKSGQFTQQDVDEAKLSVFSAVDSPIAPSDKGMNHFLHGISDEMKQKHREQLFAVTHSDLTNASNKYLTAGQCTRGTAILGPENRNIAKDPSWIIR |
| Enzyme Length | 1027 |
| Uniprot Accession Number | Q28BR5 |
| Absorption | |
| Active Site | ACT_SITE 101; /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); Compositional bias (1); Disulfide bond (1); Metal binding (3); Region (1); 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 | - |
| Motif | |
| Gene Encoded By | |
| Mass | 116,221 |
| Kinetics | |
| Metal Binding | METAL 98; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q5JRX3; METAL 102; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000250|UniProtKB:Q5JRX3; METAL 199; /note=Zinc; catalytic; /evidence=ECO:0000250|UniProtKB:Q5JRX3 |
| Rhea ID | |
| Cross Reference Brenda |