Detail Information for IndEnz0002005514
IED ID IndEnz0002005514
Enzyme Type ID protease005514
Protein Name Cytochrome c oxidase subunit 6C
Cytochrome c oxidase polypeptide VIc
Gene Name COX6C
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MAPEVLPKPRMRGLLARRLRNHMAVAFVLSLGVAALYKFRVADQRKKAYADFYRNYDVMKDFEEMRKAGIFQSVK
Enzyme Length 75
Uniprot Accession Number P09669
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P04038}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P04038}.
nucleotide Binding
Features Chain (1); Topological domain (2); Transmembrane (1)
Keywords 3D-structure;Direct protein sequencing;Membrane;Mitochondrion;Mitochondrion inner membrane;Reference proteome;Transmembrane;Transmembrane helix
Interact With P42858; P21673
Induction
Subcellular Location SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D Electron microscopy (1)
Cross Reference PDB 5Z62;
Mapped Pubmed ID 11340051; 12969439; 15223; 16169070; 16760263; 17264172; 17298220; 17353931; 17500595; 19064571; 19688755; 19843159; 20195357; 20877624; 21911578; 21958598; 21988832; 22860893; 22902835; 23260140; 23746447; 24344204; 24725412; 25203353; 26496610; 26752685; 28698372; 29505834; 7979252;
Motif
Gene Encoded By
Mass 8,781
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda