Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q02211 (COX1_PHYME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 78. 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
OrganismPhytophthora megasperma (Potato pink rot fungus)
Taxonomic identifier4788 [NCBI]
Taxonomic lineageEukaryotaStramenopilesOomycetesPeronosporalesPhytophthora

Protein attributes

Sequence length492 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 – 492492Cytochrome c oxidase subunit 1
PRO_0000183389

Regions

Transmembrane24 – 4421Helical; Potential
Transmembrane72 – 9221Helical; Potential
Transmembrane109 – 12921Helical; Potential
Transmembrane154 – 17421Helical; Potential
Transmembrane192 – 21221Helical; Potential
Transmembrane243 – 26321Helical; Potential
Transmembrane275 – 29521Helical; Potential
Transmembrane318 – 33821Helical; Potential
Transmembrane346 – 36621Helical; Potential
Transmembrane385 – 40521Helical; Potential
Transmembrane422 – 44221Helical; Potential
Transmembrane467 – 48721Helical; Potential

Sites

Metal binding701Iron (heme A axial ligand) Probable
Metal binding2491Copper B Probable
Metal binding2531Copper B Probable
Metal binding2981Copper B Probable
Metal binding2991Copper B Probable
Metal binding3841Iron (heme A3 axial ligand) Probable
Metal binding3861Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link249 ↔ 2531'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02211 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9214D85A2EE32021

FASTA49254,325
        10         20         30         40         50         60 
MNFKNINKCQ LDWLFSTNHK DIGTLYLIFS AFAGIVGTTL SLLIRMELAQ PGNQIFMGNH 

        70         80         90        100        110        120 
QLYNVVVTAH AFIMVFFLVM PALIGGFGNW FVPLMIGAPD MAFPRMNNIS FWLLPPALLL 

       130        140        150        160        170        180 
LVSSAIVESG AGTGWTVYPP LSSVQAHSGP SVDLAIFSLH LTGISSLLGA INFISTIYNM 

       190        200        210        220        230        240 
RAPGLSFHRL PLFVWSVLIT AFLLLLTLPV LAGAITMLLT DRNLNTSFYD PSGGGDPVLY 

       250        260        270        280        290        300 
QHLFWFFGHP EVYILILPAF GIISQVAAAF AKKNVFGYLG MVYAMLSIGL LGCIVWAHHM 

       310        320        330        340        350        360 
FTVGLDVDTR AYFSAATMII AVPTGIKIFS WLATLWGGSL KFETPLLFVL GFILLFVVGG 

       370        380        390        400        410        420 
VTGVAMSNSG LDIAIHDTYY IVGHFHYVLS MGAVFGIFTG FYFWIGKISG RKYPEILGQI 

       430        440        450        460        470        480 
HFWLFFIGVN ITFFPMHFLG LAGMPRRIPD FPDAMSGWNA VSSFGSYISF FSALFFFYIV 

       490 
YVTLVYGKKT EN 

« Hide

References

[1]"Genic rearrangements in Phytophthora mitochondrial DNA."
Shumard-Hudspeth D.S., Hudspeth M.E.
Curr. Genet. 17:413-415(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 695T.
[2]"Oomycete mtDNA: Phytophthora genes for cytochrome c oxidase use an unmodified genetic code and encode proteins most similar to plants."
Sachay D.J., Hudspeth D.S., Nadler S.A., Hudspeth M.E.
Exp. Mycol. 17:7-23(1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 695T.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04457 Genomic DNA. Translation: AAA32023.2.

3D structure databases

ProteinModelPortalQ02211.
SMRQ02211. Positions 13-481.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_PHYME
AccessionPrimary (citable) accession number: Q02211
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 78 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