| IED ID | IndEnz0002006200 |
| Enzyme Type ID | protease006200 |
| Protein Name |
Mycofactocin precursor peptide peptidase EC 3.4.14.- |
| Gene Name | mftE MSMEG_1425 |
| Organism | Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
| Taxonomic Lineage | cellular organisms Bacteria Terrabacteria group Actinobacteria Actinomycetia (high G+C Gram-positive bacteria) Corynebacteriales Mycobacteriaceae Mycolicibacterium Mycolicibacterium smegmatis (Mycobacterium smegmatis) Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) |
| Enzyme Sequence | MNSAYHRHVAFPSGLGTSTSRQLHSMVPMVLVPVGSTEQHGPHLPLDTDTRIAAAVAGTVVEQFGAPADRDAVVAPPVAYGASGEHEGFPGTVSIGTAALELLLVEYGRSASKWTSRIVFVNGHGGNVEALAAAVALLRYEGRDAGWVPCSVPDADAHAGHTETSVLLHISPDDVLTDELVCGNTAPLAELMPRMRSGGVAAVSELGILGDPTTATAAEGERIFAEMVNGCADRIKRWQPDRNGLLT |
| Enzyme Length | 247 |
| Uniprot Accession Number | A0QSC0 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=[mycofactocin precursor peptide]-C-terminal glycyl-N-{5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-oxopyrrolidin-3-yl}acetamide + H2O = 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one + [mycofactocin precursor peptide]-C-terminal glycine; Xref=Rhea:RHEA:65504, Rhea:RHEA-COMP:16818, Rhea:RHEA-COMP:16819, ChEBI:CHEBI:15377, ChEBI:CHEBI:83148, ChEBI:CHEBI:150863, ChEBI:CHEBI:156518; Evidence={ECO:0000269|PubMed:30183269}; |
| DNA Binding | |
| EC Number | 3.4.14.- |
| Enzyme Function | FUNCTION: Peptidase involved in the biosynthesis of the enzyme cofactor mycofactocin (MFT) (PubMed:33014324). Catalyzes cleavage of the MftC-modified MftA peptide to liberate its final two residues, which consist of a cross-linked valine-decarboxylated tyrosine dipeptide (named 3-amino-5-[(4-hydroxyphenyl)methyl]-4,4-dimethyl-2-pyrrolidin-2-one or ADHP) (PubMed:30183269). Is required for the in vivo ethanol assimilation in M.smegmatis (PubMed:31113891). {ECO:0000269|PubMed:30183269, ECO:0000269|PubMed:31113891, ECO:0000269|PubMed:33014324}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Erroneous initiation (1); Metal binding (6) |
| Keywords | Hydrolase;Iron;Metal-binding;Protease;Reference proteome;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 25,761 |
| Kinetics | |
| Metal Binding | METAL 38; /note=Divalent metal cation 1; /evidence=ECO:0000250|UniProtKB:P83772; METAL 40; /note=Divalent metal cation 2; via tele nitrogen; /evidence=ECO:0000250|UniProtKB:P83772; METAL 49; /note=Divalent metal cation 1; /evidence=ECO:0000250|UniProtKB:P83772; METAL 49; /note=Divalent metal cation 2; /evidence=ECO:0000250|UniProtKB:P83772; METAL 124; /note=Divalent metal cation 1; via pros nitrogen; /evidence=ECO:0000250|UniProtKB:P83772; METAL 163; /note=Divalent metal cation 2; /evidence=ECO:0000250|UniProtKB:P83772 |
| Rhea ID | RHEA:65504 |
| Cross Reference Brenda |