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Q9B6E7 (COX1_YARLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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
OrganismYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) [Reference proteome]
Taxonomic identifier284591 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia

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_0000183431

Regions

Transmembrane21 – 4323Helical; Potential
Transmembrane63 – 8523Helical; Potential
Transmembrane106 – 12823Helical; Potential
Transmembrane153 – 17523Helical; Potential
Transmembrane188 – 21023Helical; Potential
Transmembrane242 – 26423Helical; Potential
Transmembrane271 – 29323Helical; Potential
Transmembrane308 – 33023Helical; Potential
Transmembrane342 – 36423Helical; Potential
Transmembrane379 – 40123Helical; Potential
Transmembrane414 – 43623Helical; Potential
Transmembrane456 – 47823Helical; Potential

Sites

Metal binding671Iron (heme A axial ligand) By similarity
Metal binding2461Copper B By similarity
Metal binding2501Copper B By similarity
Metal binding2951Copper B By similarity
Metal binding2961Copper B By similarity
Metal binding3811Iron (heme A3 axial ligand) By similarity
Metal binding3831Iron (heme A axial ligand) By similarity

Amino acid modifications

Cross-link246 ↔ 2501'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9B6E7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B47B1E3FD4AF9577

FASTA53558,935
        10         20         30         40         50         60 
MSLKLNIQRW LFSTNAKDIA VLYFIFALFS AMIGTGLSAI IRLELANTGS PFLHGNTQAF 

        70         80         90        100        110        120 
NVVITAHAIL MIFFFVMPAL VGGFGNYLMP LMLGASDMAF ARLNNISFWL LVPSLILILT 

       130        140        150        160        170        180 
SALVEAGAGT GWTVYFPLAG IQSHSGPAVD LAIFSLHLSG FSSLLGAINF ITTFINMRTI 

       190        200        210        220        230        240 
GMKYENVPLF AWAVLFTAIL LLLSLPVLAA GLTMGIFDRN FNTSFFEYAG GGDAVLYQHL 

       250        260        270        280        290        300 
FYWWNHPEVY ILIIPGFGII SHAVSAIASK PVFGVQGMIY AMWSIGLLGF CVWSHHMFAV 

       310        320        330        340        350        360 
GLDSDTRAYF TSATMVIAVP TSIKIFSWLA TLYGGTIRLN VTALFALGFI FLFTIGGLTG 

       370        380        390        400        410        420 
VVLANSALDI PFHDSYYVVA HFHYVLSMGA VFSIFCGWYL WSPKILGLHY NERLSHIHFW 

       430        440        450        460        470        480 
LMFIGVNVTF FPMHFLGLQG MPRRINDYPD AFIGWNQVAS LGSIISIVAS IVFIYVVYDQ 

       490        500        510        520        530 
LTNGLHQGNK ALDSQFKPSF MGTNLNVEGY TGPTLEWTVS TPPSLHAFNT PAVLY 

« Hide

References

[1]"The complete mitochondrial genome of Yarrowia lipolytica."
Kerscher S., Durstewitz G., Casaregola S., Gaillardin C., Brandt U.
Comp. Funct. Genomics 2:80-90(2001)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 20460 / W29 / CBS 7504 / IFP29.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ307410 Genomic DNA. Translation: CAC28091.2.
RefSeqNP_075425.2. NC_002659.1.

3D structure databases

ProteinModelPortalQ9B6E7.
SMRQ9B6E7. Positions 7-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING4952.Q9B6E7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID802596.
KEGGyli:YalifMp03.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK02256.
OrthoDBEOG72C58S.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_YARLI
AccessionPrimary (citable) accession number: Q9B6E7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 82 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