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P48868 (COX1_WICCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. 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:COX1
Encoded onMitochondrion
OrganismWickerhamomyces canadensis (Yeast) (Pichia canadensis)
Taxonomic identifier1156965 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPhaffomycetaceaeWickerhamomyces

Protein attributes

Sequence length535 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 – 535535Cytochrome c oxidase subunit 1
PRO_0000183341

Regions

Transmembrane17 – 3721Helical; Potential
Transmembrane58 – 7821Helical; Potential
Transmembrane104 – 12421Helical; Potential
Transmembrane147 – 16721Helical; Potential
Transmembrane184 – 20421Helical; Potential
Transmembrane236 – 25621Helical; Potential
Transmembrane268 – 28821Helical; Potential
Transmembrane311 – 33121Helical; Potential
Transmembrane339 – 35921Helical; Potential
Transmembrane373 – 39321Helical; Potential
Transmembrane413 – 43321Helical; Potential
Transmembrane453 – 47321Helical; Potential

Sites

Metal binding631Iron (heme A axial ligand) Probable
Metal binding2421Copper B Probable
Metal binding2461Copper B Probable
Metal binding2911Copper B Probable
Metal binding2921Copper B Probable
Metal binding3771Iron (heme A3 axial ligand) Probable
Metal binding3791Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link242 ↔ 2461'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P48868 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 97F7C4EFAD1AD50A

FASTA53559,025
        10         20         30         40         50         60 
MYIQRWLYST NAKDIAILYF IFAIFSGVIG STMSLIIRLE LAAPGNQILH GNHQLFNVLV 

        70         80         90        100        110        120 
VGHALLMIFF LVMPGLVGGF GNYMLPLLIG ASDMSFARLN NISFWLLPPA LVCLVASTLI 

       130        140        150        160        170        180 
ESWAGTGWTI YPPLSGIQAH SSPSVDLGIF AIHLTSISSL LGAINFIATS YNMRTNGMSY 

       190        200        210        220        230        240 
SKMPLFVWAI IITAVMLLLS LPVLTAGVTM LLMDRNFNTS FFEVAGGGDP VLYQHLFWFF 

       250        260        270        280        290        300 
GHPEVYILIV PGFGIISHIV STYSKKPVFG EISMVYAMAS IAFLGFLVWS HHMYIVGLDA 

       310        320        330        340        350        360 
DTRAYFTSST MVIAVPTGIK IFSWLATLYG GSIRLAVPML YAIAFLFLFT IGGLTGVALA 

       370        380        390        400        410        420 
NASLDVAFHD TYYVVGHFHY VLSMGAIFSL FAGYYYWSPQ ILGLYFNERL AQIQFWLIFV 

       430        440        450        460        470        480 
GANVIFMPMH FLGLQGMPRR IPDYPDAYAG WNYVSSIGSV IAIISLALFI YIIYDQLING 

       490        500        510        520        530 
LTNKIDNKSV VYSKAPDFVE SNTIFANNSI KSASIEFLLN SPPAIHSFNT PAVQS 

« Hide

References

[1]"The complete mitochondrial DNA sequence of Hansenula wingei reveals new characteristics of yeast mitochondria."
Sekito T., Okamoto K., Kitano H., Yoshida K.
Curr. Genet. 28:39-53(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31785 Genomic DNA. Translation: BAA06563.2.
PIRS58740.
RefSeqNP_038208.1. NC_001762.1.

3D structure databases

ProteinModelPortalP48868.
SMRP48868. Positions 1-533.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID800565.

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_WICCA
AccessionPrimary (citable) accession number: P48868
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: August 30, 2002
Last modified: May 14, 2014
This is version 87 of the entry and version 2 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