A0A0U2F1A2 · A0A0U2F1A2_COLMG

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 respiratory 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
      COI

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Strains
    • 11360
    • 11369
    • 11380
    • 11381
    • 11458
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Pycnogonida > Pantopoda > Colossendeidae > Colossendeis

Accessions

  • Primary accession
    A0A0U2F1A2

Subcellular Location

Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane18-48Helical
Transmembrane69-93Helical
Transmembrane113-136Helical
Transmembrane148-175Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-181Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    181
  • Mass (Da)
    19,764
  • Last updated
    2016-03-16 v1
  • Checksum
    C62488B11AC26745
LIRTELGMPGSLIGNDQIYNVLVTAHAFIMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLMLLLMSAFVDSGVGTGWTLYPPLSSNLSHSGPSVDLSIFSLHLAGVSSILGAINFITTIINMRSKGMKFELVPLFVWSILITVVLLLLSLPVLAGAITMLLTDRNFN

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue181

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KT201815
EMBL· GenBank· DDBJ
AKU53140.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201816
EMBL· GenBank· DDBJ
AKU53141.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201817
EMBL· GenBank· DDBJ
AKU53142.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201818
EMBL· GenBank· DDBJ
AKU53143.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201819
EMBL· GenBank· DDBJ
AKU53144.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201820
EMBL· GenBank· DDBJ
AKU53145.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201821
EMBL· GenBank· DDBJ
AKU53146.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201822
EMBL· GenBank· DDBJ
AKU53147.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201954
EMBL· GenBank· DDBJ
AKU53279.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201955
EMBL· GenBank· DDBJ
AKU53280.1
EMBL· GenBank· DDBJ
Genomic DNA
KT201956
EMBL· GenBank· DDBJ
AKU53281.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp