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P00402 (COX1_EMEND) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:cox1
Synonyms:oxiA
Encoded onMitochondrion
OrganismEmericella nidulans (Aspergillus nidulans)
Taxonomic identifier162425 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length567 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 – 567567Cytochrome c oxidase subunit 1
PRO_0000183331

Regions

Transmembrane56 – 7621Helical; Potential
Transmembrane103 – 12321Helical; Potential
Transmembrane139 – 15921Helical; Potential
Transmembrane185 – 20521Helical; Potential
Transmembrane221 – 24121Helical; Potential
Transmembrane274 – 29421Helical; Potential
Transmembrane306 – 32621Helical; Potential
Transmembrane344 – 36421Helical; Potential
Transmembrane377 – 39721Helical; Potential
Transmembrane416 – 43621Helical; Potential
Transmembrane451 – 47121Helical; Potential
Transmembrane491 – 51121Helical; Potential

Sites

Metal binding1011Iron (heme A axial ligand) Probable
Metal binding2801Copper B Probable
Metal binding2841Copper B Probable
Metal binding3291Copper B Probable
Metal binding3301Copper B Probable
Metal binding4151Iron (heme A3 axial ligand) Probable
Metal binding4171Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link280 ↔ 2841'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
P00402 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 9163AAEA8C02F6A6

FASTA56762,621
        10         20         30         40         50         60 
MIIDLNTNNV LGKKFSTSTK KENIKQIESS SFLTFKQPTE WQERWYLSSN AKDIGTLYLM 

        70         80         90        100        110        120 
FALFSGLLGT AFSVLIRLEL SGPGVQYIAD NQLYNSIITA HAIMMIFFMV MPALIGGFGN 

       130        140        150        160        170        180 
FLLPLLVGGP DMAFPRLNNI SFWLLVPSLL LFVFSATIEN GAGTGWTLYP PLSGIQSHSG 

       190        200        210        220        230        240 
PSVDLAIFGL HLSGISSMLG AMNFITTILN MRSPGIRLHK LALFGWAVII TAVLLLLSLP 

       250        260        270        280        290        300 
VLAGGITMVL TDRNFNTSFF EVAGGGDPIL FQHLFWFFGH PEVYILIIPG FGIISTVIAA 

       310        320        330        340        350        360 
GSGKNVFGYL GMVYAMMSIG VLGFLVWSHH MYTVGLDVDT RAYFTAATLI IAVPTGIKIF 

       370        380        390        400        410        420 
SWLATCYGGS LHLTPPMLFA LGFVVLFTIG GLSGVVLANA SLDVAFHDTY YVVAHFHYVL 

       430        440        450        460        470        480 
SMGAVFALFS GWYLWIPKLL GLSYDQFAAK VHFWILFIGV NLTFFPQHFL GLQLMPRRIS 

       490        500        510        520        530        540 
DYPDAFYGWN LLSSIGSIIS VVATWYFLTI IYKQLTEGKA VSRYPWLTPQ LFSDTFQVLF 

       550        560 
TRNNSSLEWC LTSPPKPHAF ASLPLQS

« Hide

References

[1]"Three variant introns of the same general class in the mitochondrial gene for cytochrome oxidase subunit 1 in Aspergillus nidulans."
Waring R.B., Brown T.A., Ray J.A., Scazzocchio C., Davies R.W.
EMBO J. 3:2121-2128(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: yA2 pyroA4 cnxC3.
[2]"Nucleotide sequence of Aspergillus nidulans mitochondrial genes coding for ATPase subunit 6, cytochrome oxidase subunit 3, seven unidentified proteins, four tRNAs and L-rRNA."
Netzker R., Koechel H.G., Basak N., Kuentzel H.
Nucleic Acids Res. 10:4783-4794(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-133.
Strain: pabaA1 biA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X00790 Genomic DNA. Translation: CAB38220.1.
PIRODAS1. A22735.

3D structure databases

ProteinModelPortalP00402.
SMRP00402. Positions 44-560.
ModBaseSearch...

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. COX1. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_EMEND
AccessionPrimary (citable) accession number: P00402
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: September 26, 2001
Last modified: April 3, 2013
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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