Skip Header

Contribute Send feedback
Read comments (?) or add your own

P48867 (COX1_CYACA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 76. 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
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:COX1
Synonyms:COXI
Encoded onMitochondrion
OrganismCyanidium caldarium
Taxonomic identifier2771 [NCBI]
Taxonomic lineageEukaryota › Rhodophyta › Bangiophyceae › Cyanidiales › Cyanidiaceae › Cyanidium

Protein attributes

Sequence length526 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 – 526526Cytochrome c oxidase subunit 1
PRO_0000183319

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane67 – 8721Helical; Potential
Transmembrane104 – 12421Helical; Potential
Transmembrane149 – 16921Helical; Potential
Transmembrane187 – 20721Helical; Potential
Transmembrane238 – 25821Helical; Potential
Transmembrane270 – 29021Helical; Potential
Transmembrane308 – 32821Helical; Potential
Transmembrane341 – 36121Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane417 – 43721Helical; Potential
Transmembrane464 – 48421Helical; Potential

Sites

Metal binding651Iron (heme A axial ligand) Probable
Metal binding2441Copper B Probable
Metal binding2481Copper B Probable
Metal binding2931Copper B Probable
Metal binding2941Copper B Probable
Metal binding3791Iron (heme A3 axial ligand) Probable
Metal binding3811Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link244 ↔ 2481'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P48867 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 5A6CA16E336901B6

FASTA52658,354
        10         20         30         40         50         60 
MSRWIQRWFF STNHKDIGTL YLIFGAFSGL LGASISLLMR IELSHPGNQV LIGNHQLYNV 

        70         80         90        100        110        120 
LVTAHGLLIL FFMVIPTLMG GFGNWFVPLI IGAPDMAFPR LNNISFWLMP PSLILLLASA 

       130        140        150        160        170        180 
FVETGAGTGW TLYPPLSSVQ AHSGGAVDLA IFSLHISGIS SILGASNFIA TIFNIRNPGQ 

       190        200        210        220        230        240 
NLYRIPLFVW SVLVTAFIIL LTFPVLAGAI TILLTDRNFN TSFFDSSGGG DPVLFQHLFW 

       250        260        270        280        290        300 
FFGHPEVYIL VLPAFGIISQ VVSTFSRKPV FGYVGIIYAL ISIRILGSMV WAHHMFTIGM 

       310        320        330        340        350        360 
DVDTRAYFTA ASLLIAVPTG IKVFSWIATM WKGSISLKTP MLFAIGFIIL FTVGGLTGLV 

       370        380        390        400        410        420 
VANSGLDISL HDTYYVVAHF HYVLSIGALF GIFAGFYYWI GKICGKQYSE TLGQIHFWIT 

       430        440        450        460        470        480 
FIGVNLTFFP MHFLGLAGIP RRIPDYPDAY EGWNIVSTYG AKVSIIGTIL FFYVVYLAFT 

       490        500        510        520 
NGLISEPNPW SLRRERLDSS SRTTEWLIAS PPIYHTFNEI PVIKET

« Hide

References

[1]Viehmann S.
Thesis (1995), Justus Liebig University / Frankfurt, Germany
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RK-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z48930 Genomic DNA. Translation: CAA88773.1.
PIRS62763.

3D structure databases

ProteinModelPortalP48867.
SMRP48867. Positions 4-519.
ModBaseSearch...

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. COX1. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_CYACA
AccessionPrimary (citable) accession number: P48867
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: March 6, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents