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P98059 (COX1_RHOCA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 71. 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 BB(3) subunit 1
Cytochrome c oxidase polypeptide I
Gene names
Name:ctaD
Synonyms:ccoN
OrganismRhodobacter capsulatus (Rhodopseudomonas capsulata)
Taxonomic identifier1061 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length532 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. 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 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 – 532532Cytochrome c oxidase subunit 1
PRO_0000183458

Regions

Transmembrane1 – 2121Helical; Potential
Transmembrane27 – 4721Helical; Potential
Transmembrane69 – 8921Helical; Potential
Transmembrane115 – 13521Helical; Potential
Transmembrane143 – 16321Helical; Potential
Transmembrane185 – 20521Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane263 – 28321Helical; Potential
Transmembrane296 – 31621Helical; Potential
Transmembrane328 – 34821Helical; Potential
Transmembrane366 – 38621Helical; Potential
Transmembrane403 – 42321Helical; Potential
Transmembrane442 – 46221Helical; Potential
Transmembrane496 – 51621Helical; Potential

Sites

Metal binding1141Iron (heme B axial ligand) Probable
Metal binding2641Copper B Probable
Metal binding3141Copper B Probable
Metal binding3151Copper B Probable
Metal binding4021Iron (high-spin heme B axial ligand) Probable
Metal binding4041Iron (heme B axial ligand) Probable

Sequences

Sequence LengthMass (Da)Tools
P98059 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 5B00CE8819D2782C

FASTA53258,956
        10         20         30         40         50         60 
MWDYVKLVAL GVVAAIAAYA ASQARDLPYM VNMVEVALAA VIALIWVLRT MGDPKPSKDE 

        70         80         90        100        110        120 
YFDGVIRAGV IATTFWGIVG FLVAVVIAFQ LAFPALNLEF GNGMLNFGRL RPLHTSAVIF 

       130        140        150        160        170        180 
AFGGNALIAS AFYVVQRTSA ARLFGGTALG WFVFWGWQLI IVTAATSYLL GGSQGKEYAE 

       190        200        210        220        230        240 
LNWHLDILVA VVWVAYLIAF LGTIFKRKEP HIYVANWFYL SFIVTIAMLH IVNNLAVPVS 

       250        260        270        280        290        300 
IFGTKSVQLM AGVQDAMTQW WYGHNAVGFF LTAGFLGMMY YFVPKQAERP VYSYKLSIVH 

       310        320        330        340        350        360 
FWALIFLYIW AGPHHLHYTA LPDWASTLGM VMSVILWMPS WGGMINGLMT LSGAWDKLRT 

       370        380        390        400        410        420 
DPVIRMMVVS IGFYGMSTFE GPMMSIKAVN SLSHYTDWTI GHVHSGALGW NGMITFGMLY 

       430        440        450        460        470        480 
FLTPRLWGRS GLYSLKLVSW HFWLATIGIV LYASAMWVTG IMEGLMWREV DAQGFLVNAF 

       490        500        510        520        530 
ADTVAAKFPM YVVRGVGGVL YLLGGLIMAY NLWATVAKQP KTANLAVAVP AE

« Hide

References

[1]"The ccoNOQP gene cluster codes for a cb-type cytochrome oxidase that functions in aerobic respiration of Rhodobacter capsulatus."
Thony-Meyer L., Beck C., Preisig O., Hennecke H.
Mol. Microbiol. 14:705-716(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 938 / 37b4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X80134 Genomic DNA. Translation: CAA56433.1.
PIRS49345. S65858.

3D structure databases

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.
IPR004677. Cyt_c_oxidase_cbb3_su1.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
SUPFAMSSF81442. COX1. 1 hit.
TIGRFAMsTIGR00780. ccoN. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_RHOCA
AccessionPrimary (citable) accession number: P98059
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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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