B2LID8 · B2LID8_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 inner membrane
Cellular Componentrespirasome
Molecular Functioncytochrome-c oxidase activity
Molecular Functionheme binding
Molecular Functionmetal ion binding
Biological Processoxidative phosphorylation

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 > Ostariophysi > Cypriniformes > Leuciscidae > Pogonichthyinae > Exoglossum

Accessions

  • Primary accession
    B2LID8

Subcellular Location

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

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane6-24Helical
Transmembrane36-58Helical
Transmembrane92-112Helical
Transmembrane132-154Helical
Transmembrane166-193Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-217Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    217
  • Mass (Da)
    23,059
  • Last updated
    2008-06-10 v1
  • Checksum
    7DF036F206D0DC8B
LYLVFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPILIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAVNFITTIINMKPPAISQYQTPLFVWAVLVTAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue217

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EU524057
EMBL· GenBank· DDBJ
ACC92099.1
EMBL· GenBank· DDBJ
Genomic DNA
EU524613
EMBL· GenBank· DDBJ
ACC92655.1
EMBL· GenBank· DDBJ
Genomic DNA
EU524616
EMBL· GenBank· DDBJ
ACC92658.1
EMBL· GenBank· DDBJ
Genomic DNA
JN026609
EMBL· GenBank· DDBJ
AEK03233.1
EMBL· GenBank· DDBJ
Genomic DNA
JN026610
EMBL· GenBank· DDBJ
AEK03234.1
EMBL· GenBank· DDBJ
Genomic DNA
JN026611
EMBL· GenBank· DDBJ
AEK03235.1
EMBL· GenBank· DDBJ
Genomic DNA
JN026612
EMBL· GenBank· DDBJ
AEK03236.1
EMBL· GenBank· DDBJ
Genomic DNA
JN026614
EMBL· GenBank· DDBJ
AEK03238.1
EMBL· GenBank· DDBJ
Genomic DNA
KX145015
EMBL· GenBank· DDBJ
ANY43430.1
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