Detail Information for IndEnz0002012140
IED ID IndEnz0002012140
Enzyme Type ID protease012140
Protein Name Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1
EC 3.4.24.-
Protein OSD1
Tat-binding homolog 11
Yeast mitochondrial escape protein 1
Gene Name YME1 OSD1 YTA11 YPR024W YP9367.04
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Enzyme Sequence MNVSKILVSPTVTTNVLRIFAPRLPQIGASLLVQKKWALRSKKFYRFYSEKNSGEMPPKKEADSSGKASNKSTISSIDNSQPPPPSNTNDKTKQANVAVSHAMLATREQEANKDLTSPDAQAAFYKLLLQSNYPQYVVSRFETPGIASSPECMELYMEALQRIGRHSEADAVRQNLLTASSAGAVNPSLASSSSNQSGYHGNFPSMYSPLYGSRKEPLHVVVSESTFTVVSRWVKWLLVFGILTYSFSEGFKYITENTTLLKSSEVADKSVDVAKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKRECQARLDVCMGGKIAEELIYGKDNTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWESWSNKIRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQVCKGEKLDKLKTSTNTVVEGPDSDERKDIGDDKPKIPTMLNA
Enzyme Length 747
Uniprot Accession Number P32795
Absorption
Active Site ACT_SITE 541; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Catalytic subunit of the mitochondrial inner membrane i-AAA protease supercomplex required for mitochondrial inner membrane protein turnover. The protease is probably ATP-dependent. Important to maintain the integrity of the mitochondrial compartment. Required both for the degradation of unassembled subunit 2 of cytochrome c oxidase (COX2) and for efficient assembly of mitochondrial respiratory chain. Binds unfolded substrates in an ATPase-independent manner; binding of folded COX2, a physiological substrate, requires an active ATPase but when COX2 is destabilized an active ATPase is no longer necessary. {ECO:0000269|PubMed:16267274, ECO:0000269|PubMed:16527490}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 321..328; /note=ATP; /evidence=ECO:0000255
Features Active site (1); Chain (1); Compositional bias (3); Helix (5); Metal binding (3); Mutagenesis (7); Nucleotide binding (1); Region (2); Sequence conflict (3)
Keywords 3D-structure;ATP-binding;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Nucleotide-binding;Protease;Reference proteome;Zinc
Interact With P25573
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8355690, ECO:0000269|PubMed:8688560}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8355690, ECO:0000269|PubMed:8688560}; Matrix side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8355690, ECO:0000269|PubMed:8688560}. Note=Although this protein does not have any predicted transmembrane helices it behaves like an integral membrane protein.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D NMR spectroscopy (1)
Cross Reference PDB 2MV3;
Mapped Pubmed ID 10192337; 10453730; 10494627; 10782097; 10882099; 10906275; 10930580; 10996302; 11212342; 11553723; 11737636; 11830665; 11996120; 12172961; 12191771; 12524335; 14690591; 15772085; 16429126; 16725216; 16966379; 17261594; 17492370; 17893242; 17976194; 18298044; 19289147; 19307606; 19536198; 19930686; 20398622; 20629757; 20657548; 20675578; 21300850; 21439406; 21463454; 21926328; 22001671; 22094424; 22292080; 22498346; 22589700; 22663076; 22687516; 22783546; 22808036; 22808334; 22993211; 23036860; 23479443; 23508107; 23910823; 24025448; 24201294; 24648523; 25573113; 25576874; 25688091; 25833713; 25840011; 26182355; 26774473; 27036363; 27068958; 27068967; 27398316; 27488107; 27693354; 29097521; 29138251; 7803857; 8514129; 8861950; 9149530; 9635427; 9683639; 9695811; 9857067; 9891785;
Motif
Gene Encoded By
Mass 81,772
Kinetics
Metal Binding METAL 540; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 544; /note=Zinc; catalytic; /evidence=ECO:0000250; METAL 618; /note=Zinc; catalytic; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda 3.4.24.B19;