S5WMP0 · S5WMP0_9NEOP

  • Protein
    Cytochrome c oxidase subunit 1
  • Gene
    COI
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Catalytic activity

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Energy metabolism; oxidative phosphorylation.

GO annotations

AspectTerm
Cellular Componentmitochondrial inner membrane
Molecular Functioncytochrome-c oxidase activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Biological Processelectron transport coupled proton transport
Biological Processmitochondrial electron transport, cytochrome c to oxygen

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome c oxidase subunit 1
  • EC number

Gene names

    • Name
      COI

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Lepidoptera > Glossata > Ditrysia > Geometroidea > Geometridae > Larentiinae > Sauris

Accessions

  • Primary accession
    S5WMP0

Subcellular Location

Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane45-71Helical
Transmembrane83-110Helical

Keywords

Interaction

Subunit

Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-135Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    135
  • Mass (Da)
    14,479
  • Last updated
    2013-10-16 v1
  • MD5 Checksum
    8A54B1EB6E7E741FD58CFF177E08D388
SFWLLPPSITLLISSSIVENGAGTGWTVYPPLSSNIAHGGTSVDLAIFSLHLAGISSILGAINFITTIINMRLNNMYFDQLPLFVWAVGITAFLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLF

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue135

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KF387948
EMBL· GenBank· DDBJ
AGS94640.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help