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O79672 (COX1_PELSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 1

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:MT-CO1
Synonyms:COI, COXI, MTCO1
Encoded onMitochondrion
OrganismPelomedusa subrufa (African side-necked turtle)
Taxonomic identifier44522 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupTestudinesPleurodiraPelomedusidaePelomedusa

Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Cytochrome c oxidase subunit 1
PRO_0000183386

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane56 – 7621Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane234 – 25421Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane417 – 43721Helical; Potential
Transmembrane453 – 47321Helical; Potential

Sites

Metal binding611Iron (heme A axial ligand) Probable
Metal binding2401Copper B Probable
Metal binding2441Copper B Probable
Metal binding2901Copper B Probable
Metal binding2911Copper B Probable
Metal binding3761Iron (heme A3 axial ligand) Probable
Metal binding3781Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link240 ↔ 2441'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
O79672 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 195105D81C814E81

FASTA51456,977
        10         20         30         40         50         60 
MNLNRWLFST NHKDIGTLYL IFGAWAGMIG TALSLLIRTE LNQPGNLLGS DQTYNVIVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPVMIGGFGN WLVPLMIGAP DMAFPRLNNM SFWLLPPSLL LMLASSAIEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLASNLAHAG ASVDLAIFSL HLAGASSILG AINFITTVIN MKTPNMSFLD 

       190        200        210        220        230        240 
MPLFVWSVLI TAILLLLSLP VLAAGITMLL TDRNLNTTFF DPSGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGIISHIVAY YSTKKEPFGY IGMVWAMTSI GFLGFIVWAH HMFTVGMNVN 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FNWLATIHGG LIKWEAPMLW AFGFIFLFTV GGLTGIVLAN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM AGFTHWFTLF TGYPLHSTWT KIHFTTMFIG 

       430        440        450        460        470        480 
VNLTFFPQHF LGLAGMPRRY SDYPDAYTLW NSISSMGSMI SLTAVVMMTF IIWEAMSSKR 

       490        500        510 
STTTTEQMST NVEWTYLCPP PNHTHVEATH LIRP 

« Hide

References

[1]"Complete mitochondrial genome suggests diapsid affinities of turtles."
Zardoya R., Meyer A.
Proc. Natl. Acad. Sci. U.S.A. 95:14226-14231(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039066 Genomic DNA. Translation: AAD05052.1.
PIRT11103.
RefSeqNP_008434.1. NC_001947.1.

3D structure databases

ProteinModelPortalO79672.
SMRO79672. Positions 3-511.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID808277.

Organism-specific databases

CTD4512.

Phylogenomic databases

HOVERGENHBG003841.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_PELSU
AccessionPrimary (citable) accession number: O79672
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways