A0A5B9BJ80 · A0A5B9BJ80_9MUSC

  • Protein
    Cytochrome c oxidase subunit 1
  • Gene
    CO1
  • 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
Cellular Componentrespiratory chain complex IV
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
      CO1

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • R_CA_1
    • R_CA_5
    • R_HI_3
    • R_HI_33
    • R_HI_45
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila

Accessions

  • Primary accession
    A0A5B9BJ80

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane7-28Helical
Transmembrane48-74Helical
Transmembrane95-117Helical
Transmembrane137-162Helical
Transmembrane174-201Helical
Transmembrane221-242Helical
Transmembrane263-282Helical
Transmembrane294-316Helical
Transmembrane328-350Helical
Transmembrane370-391Helical
Transmembrane403-421Helical
Transmembrane441-464Helical

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
Domain1-495Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    495
  • Mass (Da)
    54,457
  • Last updated
    2019-11-13 v1
  • MD5 Checksum
    98DE56C68134F5F03BAF10A309397EEA
TNHKDIGTLYFIFGAWAGMVGTSLSILIRAELGHPGALIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALTLLLVSSMVENGAGTGWTVYPPLSAGIAHGGASVDLAIFSLHLAGISSILGAVNFITTVINMRSTGITLDRMPLFVWSVVITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGTQLSYSPAILWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNNKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVISTIGSSISLLGILFFFYIIWESLVSQRQVIYPIQLNSSIEWYQNTPPAEHS

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue495

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MN262235
EMBL· GenBank· DDBJ
QED88404.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262236
EMBL· GenBank· DDBJ
QED88405.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262237
EMBL· GenBank· DDBJ
QED88406.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262238
EMBL· GenBank· DDBJ
QED88407.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262239
EMBL· GenBank· DDBJ
QED88408.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262240
EMBL· GenBank· DDBJ
QED88409.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262241
EMBL· GenBank· DDBJ
QED88410.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262242
EMBL· GenBank· DDBJ
QED88411.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262243
EMBL· GenBank· DDBJ
QED88412.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262244
EMBL· GenBank· DDBJ
QED88413.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262245
EMBL· GenBank· DDBJ
QED88414.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262246
EMBL· GenBank· DDBJ
QED88415.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262247
EMBL· GenBank· DDBJ
QED88416.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262248
EMBL· GenBank· DDBJ
QED88417.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262249
EMBL· GenBank· DDBJ
QED88418.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262250
EMBL· GenBank· DDBJ
QED88419.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262251
EMBL· GenBank· DDBJ
QED88420.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262252
EMBL· GenBank· DDBJ
QED88421.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262253
EMBL· GenBank· DDBJ
QED88422.1
EMBL· GenBank· DDBJ
Genomic DNA
MN262254
EMBL· GenBank· DDBJ
QED88423.1
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