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Q85QA3 (COX1_CANGA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. 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
OrganismCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) [Complete proteome]
Taxonomic identifier284593 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces

Protein attributes

Sequence length534 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 – 534534Cytochrome c oxidase subunit 1
PRO_0000183300

Regions

Transmembrane14 – 3623Helical; Potential
Transmembrane57 – 7923Helical; Potential
Transmembrane146 – 16823Helical; Potential
Transmembrane189 – 21123Helical; Potential
Transmembrane237 – 25923Helical; Potential
Transmembrane266 – 28823Helical; Potential
Transmembrane303 – 32523Helical; Potential
Transmembrane338 – 36023Helical; Potential
Transmembrane375 – 39723Helical; Potential
Transmembrane414 – 43623Helical; Potential
Transmembrane451 – 47323Helical; Potential

Sites

Metal binding621Iron (heme A axial ligand) By similarity
Metal binding2411Copper B By similarity
Metal binding2451Copper B By similarity
Metal binding2901Copper B By similarity
Metal binding2911Copper B By similarity
Metal binding3761Iron (heme A3 axial ligand) By similarity
Metal binding3781Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link241 ↔ 2451'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q85QA3 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: DE47C9A2F2D513DF

FASTA53458,737
        10         20         30         40         50         60 
MVQRWLYSTN AKDIAVLYFM IALFSGMAGT AMSMIIRLEL AAPGSQYLAG NNQLFNVLVV 

        70         80         90        100        110        120 
GHAVLMIFFL VMPALIGGFG NYMLPLMIGA SDMAFPRLNN VGFWLIVPAL VCLVTSTLVE 

       130        140        150        160        170        180 
AGAGTGWTVY PPLSSIQAHS GPSVDLAIFA LHLTSISSLL GSINFIVTTL NMRTNGMTMH 

       190        200        210        220        230        240 
KLPLFVWAIF ITAFLLLLSL PVLSAGVTML LLDRNFNTSF FEVAGGGDPI LYQHLFWFFG 

       250        260        270        280        290        300 
HPEVYILIIP GFGIISHIVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYIVGLDAD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGIKI FSWLATIYGG SIRLAVPMLY AIAFLFLFTI GGMTGVALAN 

       370        380        390        400        410        420 
ASLDVAFHDT YYVVGHFHYV LSMGAVFSTI AGYYYWSPQI LGLYYNEKLA QIQFWLIFVG 

       430        440        450        460        470        480 
ANVTFMPMHF LGINGMPRRI PDYPDAFAGW NYVASVGSFI AMISLVLFIY ILYDQFVNGL 

       490        500        510        520        530 
TNKANNKSVL YTKSPDFVES NEIFNLNTIK TSSIEFLLTS PPAVHSFNTP AVQS 

« Hide

References

[1]"The complete mitochondrial genome sequence of the pathogenic yeast Candida (Torulopsis) glabrata."
Koszul R., Malpertuy A., Frangeul L., Bouchier C., Wincker P., Thierry A., Duthoy S., Ferris S., Hennequin C., Dujon B.
FEBS Lett. 534:39-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ511533 Genomic DNA. Translation: CAD54419.1.
RefSeqNP_818778.1. NC_004691.1.

3D structure databases

ProteinModelPortalQ85QA3.
SMRQ85QA3. Positions 2-532.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID807004.
KEGGcgr:CaglfMp04.

Phylogenomic databases

HOGENOMHOG000085274.
KOK02256.
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_CANGA
AccessionPrimary (citable) accession number: Q85QA3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 66 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