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A6H4Q6 (COX1_VANPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 44. 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
ORF Names:VapofMp06
Encoded onMitochondrion
OrganismVanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294) (Kluyveromyces polysporus) [Complete proteome]
Taxonomic identifier436907 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeVanderwaltozyma

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 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 – 534534Cytochrome c oxidase subunit 1
PRO_0000356867

Regions

Transmembrane16 – 3621Helical; Potential
Transmembrane64 – 8421Helical; Potential
Transmembrane101 – 12121Helical; Potential
Transmembrane147 – 16721Helical; Potential
Transmembrane183 – 20321Helical; Potential
Transmembrane235 – 25521Helical; Potential
Transmembrane267 – 28721Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane338 – 35821Helical; Potential
Transmembrane372 – 39221Helical; Potential
Transmembrane414 – 43421Helical; Potential
Transmembrane453 – 47321Helical; 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
A6H4Q6 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: F03FDC314A7F20E0

FASTA53459,081
        10         20         30         40         50         60 
MLQRWLYSTN AKDIAVLYFI FSVFCGMAGT GMSMIIRLEL AGPGNQYLGG NHQLFNTLVT 

        70         80         90        100        110        120 
GHAILMVFFL VMPALIGGFG NYLLPLMIGA SDMSYPRLNN ISFWLLPPAL VCLVTSTLVE 

       130        140        150        160        170        180 
SGAGTGWTVY APLSGIQSHS GPSVDLAIFA LHMTSISSLL GAINFIVTTL NMRTNGMSMH 

       190        200        210        220        230        240 
KMPLFVWAIF ITAFLLLLSL PVLSAGVTLL LMDRNFNTSF YEVAGGGDPV LYQHLFWFFG 

       250        260        270        280        290        300 
HPEVYIMIVP AFGVISHIVS TYSKKPVFGE ISMVYAMASI GLLGFLVWSH HMYVVGLDCD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGIKI FSWLATIYGG SIRLAVPMMY AIAFLFLFTL GGFTGVALAN 

       370        380        390        400        410        420 
ASLDVAFHDT YYVVAHFHYV LSMGAVFSMF AGYYYWSPHI LGLNYNEKLA QIQFWLIFVG 

       430        440        450        460        470        480 
VNVIFLPMHF LGINGMPRRI PDYPDAFAGW NYVSSIGSFI AMISLILFIY ILFDQLYNGL 

       490        500        510        520        530 
ENKINNKSVT FMKAPDFVES NNKFNLNTIK TSSIEFLLNS PPAVHSFNTP AVTN 

« Hide

References

[1]"Independent sorting-out of thousands of duplicated gene pairs in two yeast species descended from a whole-genome duplication."
Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.
Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 22028 / DSM 70294.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM698041 Genomic DNA. Translation: CAN85579.1.
RefSeqYP_001331018.1. NC_009638.1.

3D structure databases

ProteinModelPortalA6H4Q6.
SMRA6H4Q6. Positions 2-532.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING436907.A6H4Q6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5329664.
KEGGvpo:VapofMp06.

Phylogenomic databases

eggNOGCOG0843.
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_VANPO
AccessionPrimary (citable) accession number: A6H4Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 44 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