A0A6B9KL80 · A0A6B9KL80_9SCOM

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
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
      COX1

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Pelagiaria > Scombriformes > Trichiuridae > Trichiurus

Accessions

  • Primary accession
    A0A6B9KL80

Subcellular Location

Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane25-55Helical
Transmembrane76-100Helical
Transmembrane120-143Helical
Transmembrane155-182Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-205Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    205
  • Mass (Da)
    21,799
  • Last updated
    2020-06-17 v1
  • MD5 Checksum
    98D24B3F69B54A8FA36B552D5E73DDDB
VGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTILNMKPAAITQFQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQH

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue205

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MN879340
EMBL· GenBank· DDBJ
QHA33659.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879341
EMBL· GenBank· DDBJ
QHA33660.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879342
EMBL· GenBank· DDBJ
QHA33661.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879343
EMBL· GenBank· DDBJ
QHA33662.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879344
EMBL· GenBank· DDBJ
QHA33663.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879346
EMBL· GenBank· DDBJ
QHA33665.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879347
EMBL· GenBank· DDBJ
QHA33666.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879348
EMBL· GenBank· DDBJ
QHA33667.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879349
EMBL· GenBank· DDBJ
QHA33668.1
EMBL· GenBank· DDBJ
Genomic DNA
MN879350
EMBL· GenBank· DDBJ
QHA33669.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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