A0A7T6ZR05 · A0A7T6ZR05_9SAUR

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 Componentrespiratory 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
      COX1

Encoded on

  • Mitochondrion

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Colubridae > Natricinae > Pseudagkistrodon

Accessions

  • Primary accession
    A0A7T6ZR05

Subcellular Location

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

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane21-40Helical
Transmembrane60-86Helical
Transmembrane107-129Helical
Transmembrane149-174Helical
Transmembrane186-213Helical
Transmembrane246-264Helical
Transmembrane276-294Helical
Transmembrane306-329Helical
Transmembrane341-362Helical
Transmembrane374-396Helical
Transmembrane417-436Helical
Transmembrane456-479Helical

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-514Cytochrome oxidase subunit I profile

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    536
  • Mass (Da)
    59,857
  • Last updated
    2021-06-02 v1
  • Checksum
    9B045786268DDB65
MLPVFMTRWLFSTNHKDIGTLYLLFGAWSGLIGACLSILMRMELTQPGTLFGSDQIFNVLVTAHAFIMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPALLLLLSSSYVEAGAGTGWTVYPPLSGNLAHSGPSVDLAIFSLHLAGASSILGAINFITTCINMKPKSMPMFNIPLFVWSVLITAIMLLTALPVLAAAITMLLTDRNLNTSFFDPSGGGDPVLFQHLFWFFGHPEVYILILPGFGIISSIITFYTGKKNTFGYTSMIWAMMSIAILGFVVWAHHMFTVGLDIDSRAYFTAATMIIAIPTGIKVFGWLATLTGGQIKWQTPVYWALGFIFLFTVGGMTGIILANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGLTHWFPLFTGYSLNQTMTKTQFWVMFIGVNLTFFPQHFLGLSGMPRRYSDFPDAFTLWNTISSIGSTISLMAVLMSLFIVWEALSYKRELAQSMGKKTHIEWFFGTPPPHHTHTEPTFMLNNVFAPIRNFITYMEWPWPEK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MW327508
EMBL· GenBank· DDBJ
QQK90409.1
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