P14544 · COX1_LEITA

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:
heme (UniProtKB | Rhea| CHEBI:30413 )

Note: Binds 2 heme A groups non-covalently per subunit.
Cu cation (UniProtKB | Rhea| CHEBI:23378 )

Note: Binds a copper B center.

Pathway

Energy metabolism; oxidative phosphorylation.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site41Ca2+ (UniProtKB | ChEBI)
Binding site46Ca2+ (UniProtKB | ChEBI)
Binding site64Fe (UniProtKB | ChEBI) of Fe(II)-heme a (UniProtKB | ChEBI); low-spin; axial binding residue
Binding site243Cu cation B (UniProtKB | ChEBI)
Binding site247O2 (UniProtKB | ChEBI)
Binding site292Cu cation B (UniProtKB | ChEBI)
Binding site293Cu cation B (UniProtKB | ChEBI)
Binding site370Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 2
Binding site371Mg2+ (UniProtKB | ChEBI); ligand shared with subunit 2
Binding site378Fe (UniProtKB | ChEBI) of heme a3 (UniProtKB | ChEBI); high-spin; axial binding residue
Binding site380Fe (UniProtKB | ChEBI) of Fe(II)-heme a (UniProtKB | ChEBI); low-spin; axial binding residue

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
  • Alternative names
    • Cytochrome c oxidase polypeptide I

Gene names

    • Name
      COI

Encoded on

  • Mitochondrion

Organism names

Accessions

  • Primary accession
    P14544

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane18-38Helical
Transmembrane42-62Helical
Transmembrane66-86Helical
Transmembrane100-120Helical
Transmembrane148-168Helical
Transmembrane186-206Helical
Transmembrane222-242Helical
Transmembrane246-266Helical
Transmembrane269-289Helical
Transmembrane306-326Helical
Transmembrane340-360Helical
Transmembrane379-399Helical
Transmembrane402-422Helical
Transmembrane460-480Helical
Transmembrane484-504Helical
Transmembrane520-540Helical

Keywords

PTM/Processing

Features

Showing features for chain, cross-link.

TypeIDPosition(s)Description
ChainPRO_00001833501-549Cytochrome c oxidase subunit 1
Cross-link243↔2471'-histidyl-3'-tyrosine (His-Tyr)

Interaction

Subunit

Component of the cytochrome c oxidase (complex IV, CIV), a multisubunit enzyme composed of a catalytic core of 3 subunits and several supernumerary subunits. The complex exists as a monomer or a dimer and forms supercomplexes (SCs) in the inner mitochondrial membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII).

Structure

Family & Domains

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    549
  • Mass (Da)
    63,272
  • Last updated
    1990-01-01 v1
  • Checksum
    F6DD04815A4917C2
MFWLCLVCLSVSHKMIGLCYLLVAILSGFVGYVYSLFIRLELSLIGCGILFGDYQFYNVLITSHGLIMVFAFIMPVMMGGLVNYFIPVMAGFPDMVFPRLNNMSFWMYLAGFGCVVNGFLTEEGMGVGWTLYPTLICIDFHSSLACDFVMFAVHLLGISSILNSINLLGTLFCCRRKFFSFLSWSLFIWAALITAILLIITLPVLAGGVTLILCDRNFNTSFYDVVGGGDLILFQHIFWFFGHPEVYIILLPVFGLISTIVEVIGFRCVFSTVAMIYSMILIAILGMFVWAHHMFVVGMDVDSRAYFGGVSILIGLPTCVKLFNWIYSFLYTDMIITFEVYFVIMFIFMFLIGAVTGLFLSNVGIDIMLHDTYFVVGHFHYVLSLGAVVGFFTGFIHFLAKWLPIELYLFWMFYFISTLFIGSNMLFFPMHSLGMYAFPRRISDYPVSFLFWSSFMLYGMLLLASLILFLCALFCVFLFWDYCLFFVSLFVFSLYCFFYFSTWLPCVMVLYLLLVDFAHIVLDYLFLILCFCFVFFIFFWQSLFLFFYI

Sequence databases

Similar Proteins

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