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Reviewed, UniProtKB/Swiss-Prot P08305 (COX1A_PARDE)

Last modified November 24, 2009. Version 76. 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-alpha
    EC=1.9.3.1
Alternative name(s):
    Cytochrome c oxidase polypeptide I-alpha
    Cytochrome aa3 subunit 1-alpha
Gene names
Name: ctaDI
Synonyms: coi
OrganismParacoccus denitrificans
Taxonomic identifier266 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Paracoccus

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Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Subunit I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Cofactor

Binds 1 copper B ion per subunit.

Binds 2 heme groups per subunit.

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Cell 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 – 554554Cytochrome c oxidase subunit 1-alpha
PRO_0000183455

Regions

Transmembrane26 – 5631 By similarity
Transmembrane81 – 11838 By similarity
Transmembrane127 – 14822 By similarity
Transmembrane175 – 20329 By similarity
Transmembrane215 – 24834 By similarity
Transmembrane260 – 29536 By similarity
Transmembrane301 – 31919 By similarity
Transmembrane331 – 35929 By similarity
Transmembrane367 – 39024 By similarity
Transmembrane399 – 42527 By similarity
Transmembrane436 – 46328 By similarity
Transmembrane478 – 50831 By similarity

Sites

Metal binding911Iron (heme A axial ligand) By similarity
Metal binding2731Copper B By similarity
Metal binding2771Copper B By similarity
Metal binding3221Copper B By similarity
Metal binding3231Copper B By similarity
Metal binding4061Iron (heme A3 axial ligand) By similarity
Metal binding4081Iron (heme A axial ligand) By similarity

Amino acid modifications

Disulfide bond63 ↔ 77 By similarity
Cross-link273 ↔ 2771'-histidyl-3'-tyrosine (His-Tyr) By similarity

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Sequences

Sequence LengthMass (Da)Tools
P08305-1 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 58AD591FBBDCE794

FASTA55462,013
        10         20         30         40         50         60 
MSAQISDSIE EKRGFFTRWF MSTNHKDIGV LYLFTAGLAG LISVTLTVYM RMELQHPGVQ 

        70         80         90        100        110        120 
YMCLEGMRLV ADAAAECTPN AHLWNVVVTY HGILMMFFVV IPALFGGFGN YFMPLHIGAP 

       130        140        150        160        170        180 
DMAFPRLNNL SYWLYVCGVS LAIASLLSPG GSDQPGAGVG WVLYPPLSTT EAGYAMDLAI 

       190        200        210        220        230        240 
FAVHVSGATS ILGAINIITT FLNMRAPGMT LFKVPLFAWA VFITAWMILL SLPVLAGGIT 

       250        260        270        280        290        300 
MLLMDRNFGT QFFDPAGGGD PVLYQHILWF FGHPEVYMLI LPGFGIISHV ISTFARKPIF 

       310        320        330        340        350        360 
GYLPMVLAMA AIAFLGFIVW AHHMYTAGMS LTQQTYFQMA TMTIAVPTGI KVFSWIATMW 

       370        380        390        400        410        420 
GGSIEFKTPM LWALAFLFTV GGVTGVVIAQ GSLDRVYHDT YYIVAHFHYV MSLGALFAIF 

       430        440        450        460        470        480 
AGTYYWIGKM SGRQYPEWAG QLHFWMMFIG SNLIFFPQHF LGRQGMPRRY IDYPVEFSYW 

       490        500        510        520        530        540 
NNISSIGAYI SFASFLFFIG IVFYTLFAGK PVNVPNYWNE HADTLEWTLP SPPPEHTFET 

       550 
LPKPEDWDRA QAHR

« Hide

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References

[1]"Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans."
Raitio M., Jalli T., Saraste M.
EMBO J. 6:2825-2833(1987) [PubMed: 16453796] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: S1657.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X05829 Genomic DNA. Translation: CAA29274.1.
PIRS03809.

3D structure databases

SMRP08305. Positions 14-540.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.9.3.1. 59.

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 nameCOX1A_PARDE
AccessionPrimary (citable) accession number: P08305
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: November 24, 2009
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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