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P50676 (COX1_THEVL) 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 aa3 subunit 1
Cytochrome c oxidase polypeptide I
Oxidase aa(3) subunit 1
Gene names
Name:ctaD
OrganismThermosynechococcus vulcanus (Synechococcus vulcanus)
Taxonomic identifier32053 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length552 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.

Cofactor

Binds 1 copper B ion per subunit.

Binds 2 heme groups per subunit.

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Cell 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 – 552552Cytochrome c oxidase subunit 1
PRO_0000183460

Regions

Transmembrane35 – 5521Helical; Potential
Transmembrane85 – 10521Helical; Potential
Transmembrane120 – 14021Helical; Potential
Transmembrane164 – 18421Helical; Potential
Transmembrane211 – 23121Helical; Potential
Transmembrane252 – 27221Helical; Potential
Transmembrane284 – 30421Helical; Potential
Transmembrane321 – 34121Helical; Potential
Transmembrane355 – 37521Helical; Potential
Transmembrane390 – 41021Helical; Potential
Transmembrane426 – 44621Helical; Potential
Transmembrane470 – 49021Helical; Potential

Sites

Metal binding821Iron (heme A axial ligand) Probable
Metal binding2581Copper B Probable
Metal binding2621Copper B Probable
Metal binding3071Copper B Probable
Metal binding3081Copper B Probable
Metal binding3931Iron (heme A3 axial ligand) Probable
Metal binding3951Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link258 ↔ 2621'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P50676 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: EC6FDF34497CD061

FASTA55261,521
        10         20         30         40         50         60 
MAQAQLPLDT PLSLPEHPKA WKWYDYFTFN VDHKVIGIQY LVTAFIFYLI GGLMAVAMRT 

        70         80         90        100        110        120 
ELATADSDFL DPNLYNAFLT NHGTIMIFLW VVPAAIGGFG NYLVPLMIGA RDMAFPRLNA 

       130        140        150        160        170        180 
LAFWLNPPAG ALLLASFLFG GAQAGWTSYP PLSTITATTA QSMWILAIIL VGTSSILGSV 

       190        200        210        220        230        240 
NFIVTIWKMK VPSMRWNQLP LFCWAMLATS LLALVSTPVL AAGLILLLFD INFGTSFYKP 

       250        260        270        280        290        300 
DAGGNVVIYQ HLFWFYSHPA VYLMILPIFG IMSEVIPVHA RKPIFGYQAI AYSSLAICCV 

       310        320        330        340        350        360 
GLFVWVHHMF TSGTPPWMRM FFTISTLIVA VPTGVKIFSW VATLWGGKIR LNSAMLFAIG 

       370        380        390        400        410        420 
LMSMFVLGGL SGVTLGTAPV DIHVHDTYYV VAHFHYVLFG GSVFGLYAGI YHWFPKMTGR 

       430        440        450        460        470        480 
LLDERLGILH FVLTLIGTNW TFLPMHELGL KGMPRRVAMY DPQFEPVNLI CTIGAFVLAF 

       490        500        510        520        530        540 
SIIPFLINII WSWNKGKIAG DNPWGGLTLE WTTSSPPLIE NWEVLPVVTK GPYDYGIERR 

       550 
QESTDEDHDE QE 

« Hide

References

[1]"The genes in the thermophilic cyanobacterium Synechococcus vulcanus encoding cytochrome-c oxidase."
Sone N., Tano H., Ishizuka M.
Biochim. Biophys. Acta 1183:130-138(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D16254 Genomic DNA. Translation: BAA41041.1.

3D structure databases

ProteinModelPortalP50676.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_THEVL
AccessionPrimary (citable) accession number: P50676
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
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 programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways