I3VM29 · I3VM29_9TELE

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

Protein has several cofactor binding sites:
Cu cation (UniProtKB | Rhea| CHEBI:23378 )

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
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Perciformes > Scorpaenoidei > Sebastidae > Sebastinae > Sebastes

Accessions

  • Primary accession
    I3VM29

Subcellular Location

Membrane
; Multi-pass membrane protein
Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane6-26Helical
Transmembrane38-60Helical
Transmembrane94-114Helical
Transmembrane134-156Helical
Transmembrane168-195Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-221Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    221
  • Mass (Da)
    23,609
  • Last updated
    2012-09-05 v1
  • Checksum
    A8DB23F004FBC378
GTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFW

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue221

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JX008528
EMBL· GenBank· DDBJ
AFK81017.1
EMBL· GenBank· DDBJ
Genomic DNA
JX008529
EMBL· GenBank· DDBJ
AFK81018.1
EMBL· GenBank· DDBJ
Genomic DNA
JX008530
EMBL· GenBank· DDBJ
AFK81019.1
EMBL· GenBank· DDBJ
Genomic DNA
JX008531
EMBL· GenBank· DDBJ
AFK81020.1
EMBL· GenBank· DDBJ
Genomic DNA
JX008532
EMBL· GenBank· DDBJ
AFK81021.1
EMBL· GenBank· DDBJ
Genomic DNA
JX008533
EMBL· GenBank· DDBJ
AFK81022.1
EMBL· GenBank· DDBJ
Genomic DNA
JX008534
EMBL· GenBank· DDBJ
AFK81023.1
EMBL· GenBank· DDBJ
Genomic DNA
JX008536
EMBL· GenBank· DDBJ
AFK81025.1
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