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P33517 (COX1_RHOSH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 aa3 subunit 1
Cytochrome c oxidase polypeptide I
Gene names
Name:ctaD
OrganismRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifier1063 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Rhodobacter

Protein attributes

Sequence length566 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 – 566566Cytochrome c oxidase subunit 1
PRO_0000183459

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane97 – 11721Helical; Potential
Transmembrane141 – 16121Helical; Potential
Transmembrane189 – 20921Helical; Potential
Transmembrane227 – 24721Helical; Potential
Transmembrane278 – 29821Helical; Potential
Transmembrane310 – 33021Helical; Potential
Transmembrane348 – 36821Helical; Potential
Transmembrane381 – 40121Helical; Potential
Transmembrane420 – 44021Helical; Potential
Transmembrane455 – 47521Helical; Potential
Transmembrane499 – 51921Helical; Potential

Sites

Metal binding1021Iron (heme A axial ligand) Probable
Metal binding2841Copper B Probable
Metal binding2881Copper B Probable
Metal binding3331Copper B Probable
Metal binding3341Copper B Probable
Metal binding4191Iron (heme A3 axial ligand) Probable
Metal binding4211Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link284 ↔ 2881'-histidyl-3'-tyrosine (His-Tyr) By similarity

Secondary structure

1 ....................................................................... 566
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33517 [UniParc].

Last modified January 17, 2003. Version 2.
Checksum: 65A74DBCC5C550B0

FASTA56663,147
        10         20         30         40         50         60 
MADAAIHGHE HDRRGFFTRW FMSTNHKDIG VLYLFTGGLV GLISVAFTVY MRMELMAPGV 

        70         80         90        100        110        120 
QFMCAEHLES GLVKGFFQSL WPSAVENCTP NGHLWNVMIT GHGILMMFFV VIPALFGGFG 

       130        140        150        160        170        180 
NYFMPLHIGA PDMAFPRMNN LSYWLYVAGT SLAVASLFAP GGNGQLGSGI GWVLYPPLST 

       190        200        210        220        230        240 
SESGYSTDLA IFAVHLSGAS SILGAINMIT TFLNMRAPGM TMHKVPLFAW SIFVTAWLIL 

       250        260        270        280        290        300 
LALPVLAGAI TMLLTDRNFG TTFFQPSGGG DPVLYQHILW FFGHPEVYII VLPAFGIVSH 

       310        320        330        340        350        360 
VIATFAKKPI FGYLPMVYAM VAIGVLGFVV WAHHMYTAGL SLTQQSYFMM ATMVIAVPTG 

       370        380        390        400        410        420 
IKIFSWIATM WGGSIELKTP MLWALGFLFL FTVGGVTGIV LSQASVDRYY HDTYYVVAHF 

       430        440        450        460        470        480 
HYVMSLGAVF GIFAGIYFWI GKMSGRQYPE WAGKLHFWMM FVGANLTFFP QHFLGRQGMP 

       490        500        510        520        530        540 
RRYIDYPEAF ATWNFVSSLG AFLSFASFLF FLGVIFYTLT RGARVTANNY WNEHADTLEW 

       550        560 
TLTSPPPEHT FEQLPKREDW ERAPAH

« Hide

References

[1]"Cloning, sequencing and deletion from the chromosome of the gene encoding subunit I of the aa3-type cytochrome c oxidase of Rhodobacter sphaeroides."
Shapleigh J.P., Gennis R.B.
Mol. Microbiol. 6:635-642(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Ga.
[2]Shapleigh J.P., Gennis R.B.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 436-439 AND 518-521.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X62645 Genomic DNA. Translation: CAA44514.2.
PIRS20534.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M56X-ray2.30A/G1-566[»]
1M57X-ray3.00A/G1-566[»]
2GSMX-ray2.00A/C1-566[»]
3DTUX-ray2.15A/C1-566[»]
3FYEX-ray2.15A/C1-566[»]
3FYIX-ray2.20A/C1-566[»]
ProteinModelPortalP33517.
SMRP33517. Positions 14-560.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-38013N.
IntActP33517. 3 interactions.

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.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. COX1. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33517.

Entry information

Entry nameCOX1_RHOSH
AccessionPrimary (citable) accession number: P33517
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 17, 2003
Last modified: April 3, 2013
This is version 97 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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