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P62514 (COX1_ASHGO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:AMI002W
ORF Names:AgCOX1
Encoded onMitochondrion
OrganismAshbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Reference proteome]
Taxonomic identifier284811 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium ›

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_0000183289

Regions

Transmembrane15 – 3723Helical; Potential
Transmembrane58 – 8023Helical; Potential
Transmembrane147 – 16923Helical; Potential
Transmembrane190 – 21223Helical; Potential
Transmembrane238 – 26023Helical; Potential
Transmembrane267 – 28923Helical; Potential
Transmembrane304 – 32623Helical; Potential
Transmembrane339 – 36123Helical; Potential
Transmembrane376 – 39823Helical; Potential
Transmembrane415 – 43723Helical; Potential
Transmembrane452 – 47423Helical; Potential

Sites

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

Amino acid modifications

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

Sequences

Sequence LengthMass (Da)Tools
P62514 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: BBEC610E44873A2C

FASTA53560,173
        10         20         30         40         50         60 
MYLQRWLFST NAKDIAILYF IFSTFCGLAG TAMSFIIRME LSAPGQQYLQ GQNQLFNVLV 

        70         80         90        100        110        120 
TGHTILMVFF LVMPMLIGGF GNYYLPLMIG ASDMSFARLN NISFWTLPPT LICLLTSTMV 

       130        140        150        160        170        180 
ESGTGTGWTV YPPLSSIQSH SGASVDLAIF SLHLTTISSL LGTINFIVTA LNMRTNGMTL 

       190        200        210        220        230        240 
HKMPLFTWSI LITAVMLLMS LPVLSAGVTM LLMDRNFNTS FFEVQGGGDP ILYQHLFWFF 

       250        260        270        280        290        300 
GHPEVYIMIV PTFGMMSHIV STYSKKPVFG EISMIYTMGS ISLLGFLVWS HHMYVVGLDT 

       310        320        330        340        350        360 
DTRAYFTSAT MIITIPTSIK VFSWLTTIYG GSLRLTTPML YTLSFLFLFT VGGLTGVVLA 

       370        380        390        400        410        420 
NTSLDVAFHD TYYVVTHFHY VLSLGAVFSM FAGYYYWSPT VLGLNYNEKL SQIQFWLIFL 

       430        440        450        460        470        480 
GTNIIFFPMH FLGINGMPRR IPDYPDTFTG WNLVSSFGSM MTIMSLMLFT YIIYDQLMNG 

       490        500        510        520        530 
LTNKVNNKSI NYMKTPDFIE SNNIFLMNTT KSSSIEFMLN SPPTIHSFNT PTIQS

« Hide

References

[1]"The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome."
Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P.
Science 304:304-307(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016821 Genomic DNA. Translation: AAS50169.1.
RefSeqNP_987079.1. NC_005789.1.

3D structure databases

ProteinModelPortalP62514.
SMRP62514. Positions 1-532.
ModBaseSearch...

Protein-protein interaction databases

STRING33169.AGOS_AMI002W.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiAAS50169; AAS50169; AGOS_AMI002W.
GeneID2760766.
KEGGago:AGOS_AMI002W.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK02256.
OrthoDBEOG4BK8C4.
PhylomeDBP62514.

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

Entry information

Entry nameCOX1_ASHGO
AccessionPrimary (citable) accession number: P62514
Secondary accession number(s): Q75G35
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: May 1, 2013
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

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