Detail Information for IndEnz0002019211
IED ID IndEnz0002019211
Enzyme Type ID protease019211
Protein Name Mitochondrial inner membrane protease ATP23
EC 3.4.24.-
Gene Name ATP23 CAGL0M10593g
Organism Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Nakaseomyces Nakaseomyces/Candida clade Candida glabrata (Yeast) (Torulopsis glabrata) Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Enzyme Sequence MAGESFEWWRRTMQYQTGLGLTADEKARYEKDYAVYNREKQCKSCYEYRDWMLKYSPTVRFMIQQISKLNGNASDGKVLNFDESKIICDECPDWKSGGFHPEIGILLCQNRLKDKWHLEDTLSHELVHYFDNLKWQIDWLNLKQHACSEIRASALSGECRFSREFARLGFSMNFGRGHQDCAKRRAIISVMGNPNCKDKEHATKVVEEVWDSCFYDTRPFEEIYR
Enzyme Length 225
Uniprot Accession Number Q6FIY7
Absorption
Active Site ACT_SITE 125; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Has a dual role in the assembly of mitochondrial ATPase. Acts as a protease that removes N-terminal residues of mitochondrial ATPase CF(0) subunit 6 at the intermembrane space side. Also involved in the correct assembly of the membrane-embedded ATPase CF(0) particle, probably mediating association of subunit 6 with the subunit 9 ring (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Metal binding (2)
Keywords Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Mitochondrion inner membrane;Protease;Reference proteome
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side. Note=Associates loosely with the inner membrane. {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 26,631
Kinetics
Metal Binding METAL 124; /note=Divalent metal cation; catalytic; /evidence=ECO:0000250; METAL 128; /note=Divalent metal cation; catalytic; /evidence=ECO:0000250
Rhea ID
Cross Reference Brenda