A0A2P1FTB5 · A0A2P1FTB5_9SAUR

  • Protein
    Cytochrome c oxidase subunit 1
  • Gene
    COI
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Colubridae > Colubrinae > Platyceps

Accessions

  • Primary accession
    A0A2P1FTB5

Subcellular Location

Mitochondrion inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane45-66Helical
Transmembrane87-109Helical
Transmembrane129-154Helical
Transmembrane166-193Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-218Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    218
  • Mass (Da)
    23,545
  • Last updated
    2018-05-23 v1
  • Checksum
    C1495FFB07F40C8F
LYLLFGAWSGLVGACLSILMRMELTQPGSLLGSDQIFNVLVTAHAFIMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPALLLLLSSSYVEAGAGTGWTVYPPLSGNLVHSGPSVDLAIFSLHLAGASSILGAINFITTCINMKPKSMPMFNMPLFVWSVLITAIMLLLALPVLAAAITMLLTDRNLNTSFFDPCGGGDPVLFQHLF

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue218

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MG700032
EMBL· GenBank· DDBJ
AVM38494.1
EMBL· GenBank· DDBJ
Genomic DNA
MG700036
EMBL· GenBank· DDBJ
AVM38498.1
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.
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