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P05489 (COX1_PARTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 94. 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:COI
Encoded onMitochondrion
OrganismParamecium tetraurelia
Taxonomic identifier5888 [NCBI]
Taxonomic lineageEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaPeniculidaParameciidaeParamecium

Protein attributes

Sequence length645 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 – 645645Cytochrome c oxidase subunit 1
PRO_0000183383

Regions

Transmembrane8 – 2821Helical; Potential
Transmembrane56 – 7621Helical; Potential
Transmembrane90 – 11021Helical; Potential
Transmembrane247 – 26721Helical; Potential
Transmembrane282 – 30221Helical; Potential
Transmembrane337 – 35721Helical; Potential
Transmembrane376 – 39621Helical; Potential
Transmembrane410 – 43021Helical; Potential
Transmembrane438 – 45821Helical; Potential
Transmembrane475 – 49521Helical; Potential
Transmembrane513 – 53321Helical; Potential
Transmembrane555 – 57521Helical; Potential

Sites

Metal binding541Iron (heme A axial ligand) Probable
Metal binding3431Copper B Probable
Metal binding3471Copper B Probable
Metal binding3921Copper B Probable
Metal binding3931Copper B Probable
Metal binding4781Iron (heme A3 axial ligand) Probable
Metal binding4801Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link343 ↔ 3471'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P05489 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: EF034E5B0D927502

FASTA64574,037
        10         20         30         40         50         60 
MNHKRIALNY FYFSMWTGLS GAALATMIRL EMAYPGSPFF KGDSIKYLQV ATAHGLIMVF 

        70         80         90        100        110        120 
FVVVPIFFGG FANFLIPYHV GSKDVAFPRL NSIGFWIQPL GFLLVAKIAF LRTTSWKYYD 

       130        140        150        160        170        180 
KTSFFLQPYN KSLYRDFFNF LTGELSFNPF KKSLDESLFL FLWKPRKKIT NTEYTSFFFN 

       190        200        210        220        230        240 
PLNLSFLDSF FYYSDNLWSL ANKVVSSRRK KIYVTKCSNR AAVTAGWTFI TPFSSNMKYS 

       250        260        270        280        290        300 
GFGAQDVLSV AVVLAGISTT ISLLTLITRR TLVAPGLRNR RVLIPFITIS LLLTLRLLAI 

       310        320        330        340        350        360 
VTPILGAAVL MSLMDRHWQT SFFDFAYGGD PILFQHLFWF FGHPEVYILI IPSFGVANIV 

       370        380        390        400        410        420 
LPFYTMRRMS SKHHMIWAVY VMAYMGFVVW GHHMYLVGLD HRSRNIYSTI TIMICLPATI 

       430        440        450        460        470        480 
KLVNWTLTLA NAAIHVDLVF LFFCSYVFFF LTGGFTGMWL SHVGLNISVH DTFYVVAHFH 

       490        500        510        520        530        540 
LMLAGAAMMG AFTGLYYYYN TFFDVQYSKI FGFLHLVYYS AGIWTTFFPM FFLGFSGLPR 

       550        560        570        580        590        600 
RIHDFPAFFL GWHGLASCGH FLTLAGVCFF FFGIFDSTSE NKSSILANFG IPKIAKRAHL 

       610        620        630        640 
YFFKISYNNY TNEIASELPK VEVRKFIIEN TFGEYECVKL VPVTK 

« Hide

References

[1]"Nucleotide sequence of the mitochondrial genome of Paramecium."
Pritchard A.E., Seilhamer J.J., Mahalingam R., Sable C.L., Venuti S.E., Cummings D.J.
Nucleic Acids Res. 18:173-180(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Stock 51.
[2]"Paramecium mitochondrial DNA sequences and RNA transcripts for cytochrome oxidase subunit I, URF1, and three ORFs adjacent to the replication origin."
Pritchard A.E., Seilhamer J.J., Cummings D.J.
Gene 44:243-253(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15917 Genomic DNA. Translation: CAA34030.1.
M15281 Genomic DNA. Translation: AAA79251.1.
PIRODPP1. A24988.
S07751.

3D structure databases

ProteinModelPortalP05489.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.210.10. 2 hits.
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. 2 hits.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 2 hits.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_PARTE
AccessionPrimary (citable) accession number: P05489
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 14, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways