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P0C8K9 (COX1_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:COX1
ORF Names:CaalfMp08
Encoded onMitochondrion
OrganismCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast) [Reference proteome]
Taxonomic identifier237561 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesmitosporic SaccharomycetalesCandida

Protein attributes

Sequence length531 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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Cytochrome c oxidase subunit 1
PRO_0000356866

Regions

Transmembrane18 – 3821Helical; Potential
Transmembrane59 – 7921Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane149 – 16921Helical; Potential
Transmembrane185 – 20521Helical; Potential
Transmembrane237 – 25721Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane312 – 33221Helical; Potential
Transmembrane340 – 36021Helical; Potential
Transmembrane385 – 40521Helical; Potential
Transmembrane414 – 43421Helical; Potential
Transmembrane458 – 47821Helical; Potential

Sites

Metal binding641Iron (heme A axial ligand) By similarity
Metal binding2431Copper B By similarity
Metal binding2471Copper B By similarity
Metal binding2921Copper B By similarity
Metal binding2931Copper B By similarity
Metal binding3781Iron (heme A3 axial ligand) By similarity
Metal binding3801Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link243 ↔ 2471'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C8K9 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: EDB63911A328C6AA

FASTA53158,744
        10         20         30         40         50         60 
MSYVTRWLFS TSHKDIGILY LIYGMVSAMV ATGMSVIIRL ELSGPGPMFL HGNNQVFNVL 

        70         80         90        100        110        120 
VTGHAIAMIF LFVMPILIGS FGNYFLPIMI GAVDMAFARL NNISFWCLPP ALVCVIASVL 

       130        140        150        160        170        180 
IETGAGTGWT VYPPLSSISA HSGPSVDLAI FAIHLTSISS LLGAINFIVT TLNMRSIGIH 

       190        200        210        220        230        240 
MIDMPLFVWA IFFTAILLLL SLPVLTAGVT LLLMDRNFNT GFYEVAAGGD PILYEHLFYF 

       250        260        270        280        290        300 
FGHPEVYIII IPGFGIISHV ISTYTKKPIF GQIGMIYAIG SIGLLGFLVW SHHMYVVGLD 

       310        320        330        340        350        360 
IDSRAYFTSA TMVIAIPTGI KIFSWLATLY GGELRLAVPM LFALGFLFLF TIGGLTGVML 

       370        380        390        400        410        420 
SNASIDVAFH DTYYVVGHFH YVLSMGALFS LIAGYYYWGP AMFGLKYNKV LAEVHYWLLF 

       430        440        450        460        470        480 
VSVNIIFLPM HFLGLNGMPR RIPQYPDAFV GWNVVSSWGS IMSVISVLIG LYSVLVQLTN 

       490        500        510        520        530 
GENEREEIQV TPDYLESNNT RDVRDSDLEL ITSRPAQYHT FSELPILIQQ I 

« Hide

References

[1]"Infrequent genetic exchange and recombination in the mitochondrial genome of Candida albicans."
Anderson J.B., Wickens C., Khan M., Cowen L.E., Federspiel N.A., Jones T., Kohn L.M.
J. Bacteriol. 183:865-872(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314 / ATCC MYA-2876.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF285261 Genomic DNA. No translation available.

3D structure databases

ProteinModelPortalP0C8K9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5476.CAF0007377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

CGDCAF0007377. COX1.

Phylogenomic databases

eggNOGCOG0843.
OrthoDBEOG72C58S.

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_CANAL
AccessionPrimary (citable) accession number: P0C8K9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Candida albicans

Candida albicans: entries and gene names