C6GZC1 · C6GZC1_URSSP

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
  • Strain
    • SP234
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Ursidae > Ursus

Accessions

  • Primary accession
    C6GZC1

Subcellular Location

Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-32Helical
Transmembrane52-78Helical
Transmembrane99-123Helical
Transmembrane143-166Helical
Transmembrane178-205Helical
Transmembrane225-246Helical
Transmembrane267-286Helical
Transmembrane298-320Helical
Transmembrane332-354Helical
Transmembrane374-392Helical
Transmembrane404-427Helical
Transmembrane447-468Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-509Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    509
  • Mass (Da)
    55,737
  • Last updated
    2009-09-01 v1
  • Checksum
    E108D64C825DFA5F
WLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGALLGDDQIYNVVVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGISSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXPDAYTTWNTVSSVGSFISLTAVMLMIFMIWEAFASKREVAVVELTSTNIEWLHGCPPPYHTFEEPAYVMLK

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FN390844
EMBL· GenBank· DDBJ
CAY39934.1
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