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Reviewed, UniProtKB/Swiss-Prot P34838 (COX1_ANOGA)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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: COI
Encoded onMitochondrion
OrganismAnopheles gambiae (African malaria mosquito) [Complete proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

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Protein attributes

Sequence length514 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 514514Cytochrome c oxidase subunit 1
PRO_0000183282

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
Transmembrane415 – 43521 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

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Sequences

Sequence LengthMass (Da)Tools
P34838-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 6459AC46AD258336

FASTA51456,841
        10         20         30         40         50         60 
MSRQWLFSTN HKDIGTLYFI FGAWAGMVGT SLSILIRAEL GHPGAFIGDD QIYNVIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWMLPPSLTL LISSSMVENG 

       130        140        150        160        170        180 
AGTGWTVYPP LSSGIAHAGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSPGITLDRM 

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

       250        260        270        280        290        300 
EVYILILPGF GMISHIITQE SGKKETFGNL GMIYAMLAIG LLGFIVWAHH MFTVGMDVDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LTYSPAMLWA FGFVFLFTVG GLTGVVLANS 

       370        380        390        400        410        420 
SIDIVLHDTY YVVAHFHYVL SMGAVFAIMA GFVHWYPLLT GLTMNPTWLK IQFSIMFVGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DFPDSYLTWN VVSSLGSTIS LFAILYFLFI IWESMITQRT 

       490        500        510 
PAFPMQLSSS IEWYHTLPPA EHTYAELPLL TNNF

« Hide

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References

[1]"The mitochondrial genome of the mosquito Anopheles gambiae: DNA sequence, genome organization, and comparisons with mitochondrial sequences of other insects."
Beard C.B., Hamm D.M., Collins F.H.
Insect Mol. Biol. 2:103-124(1993) [PubMed: 9087549] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: G3.

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Cross-references

Sequence databases

L20934 Genomic DNA. Translation: AAD12191.1. Different initiation.
PIRT09801.

3D structure databases

HSSPHSSP built from PDB template 2OCC based on UniProtKB P00396.
SMRP34838. Positions 4-506.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.9.3.1. 165157.

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...

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Entry information

Entry nameCOX1_ANOGA
AccessionPrimary (citable) accession number: P34838
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

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