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Reviewed, UniProtKB/Swiss-Prot P00400 (COX1_DROYA)

Last modified November 24, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: mt:CoI
Synonyms: CoI
Encoded onMitochondrion
OrganismDrosophila yakuba (Fruit fly)
Taxonomic identifier7245 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length512 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 – 512512Cytochrome c oxidase subunit 1
PRO_0000183329

Regions

Transmembrane16 – 3621 Potential
Transmembrane55 – 7521 Potential
Transmembrane101 – 12121 Potential
Transmembrane144 – 16421 Potential
Transmembrane182 – 20221 Potential
Transmembrane233 – 25321 Potential
Transmembrane267 – 28721 Potential
Transmembrane304 – 32421 Potential
Transmembrane337 – 35721 Potential
Transmembrane379 – 39921 Potential
Transmembrane413 – 43321 Potential
Transmembrane451 – 47121 Potential

Sites

Metal binding601Iron (heme A axial ligand) Probable
Metal binding2391Copper B Probable
Metal binding2431Copper B Probable
Metal binding2891Copper B Probable
Metal binding2901Copper B Probable
Metal binding3751Iron (heme A3 axial ligand) Probable
Metal binding3771Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link239 ↔ 2431'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P00400-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 5B63A3F05FDE227C

FASTA51256,526
        10         20         30         40         50         60 
MSRQWLFSTN HKDIGTLYFI FGAWAGMVGT SLSILIRAEL GHPGALIGDD QIYNVIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWLLPPALSL LLVSSMVENG 

       130        140        150        160        170        180 
AGTGWTVYPP LSSGIAHGGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSTGITLDRM 

       190        200        210        220        230        240 
PLFVWSVVIT ALLLLLSLPV LAGAITMLLT DRNLNTSFFD PAGGGDPILY QHLFWFFGHP 

       250        260        270        280        290        300 
EVYILILPGF GMISHIISQE SGKKETFGSL GMIYAMLAIG LLGFIVWAHH MFTVGMDVDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LSYSPAILWA LGFVFLFTVG GLTGVVLANS 

       370        380        390        400        410        420 
SVDIILHDTY YVVAHFHYVL SMGAVFAIMA GFIHWYPLFT GLTLNNKWLK SQFIIMFIGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DYPDAYTTWN VVSTIGSTIS LLGILFFFYI IWESLVSQRQ 

       490        500        510 
VIYPIQLNSS IEWYQNTPPA EHSYSELPLL TN 

« Hide

References

[1]"The mitochondrial DNA molecular of Drosophila yakuba: nucleotide sequence, gene organization, and genetic code."
Clary D.O., Wolstenholme D.R.
J. Mol. Evol. 22:252-271(1985) [PubMed: 3001325] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 2317.6 Ivory Coast.
[2]"Genes for cytochrome c oxidase subunit I, URF2, and three tRNAs in Drosophila mitochondrial DNA."
Clary D.O., Wolstenholme D.R.
Nucleic Acids Res. 11:6859-6872(1983) [PubMed: 6314262] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03240 Genomic DNA. Translation: CAC14066.1.
PIRODFF1Y. A93488.

3D structure databases

SMRP00400. Positions 4-506.
ModBaseSearch...

Organism-specific databases

FlyBaseFBgn0013179. Dyak\mt:CoI.

Enzyme and pathway databases

BRENDA1.9.3.1. 278535.

Family and domain databases

InterProIPR000883. Cyt_c_oxidase_su1.
[Graphical view]
Gene3DG3DSA:1.20.210.10. COX1. 1 hit.
PANTHERPTHR10422. COX1. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_DROYA
AccessionPrimary (citable) accession number: P00400
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 24, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents