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Q08855 (COX1_RHILE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:coxA
OrganismRhizobium leguminosarum
Taxonomic identifier384 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Catalytic activity

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

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Developmental stage

Free in soil (not as bacteroid).

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538Cytochrome c oxidase subunit 1
PRO_0000183447

Regions

Transmembrane37 – 5721Helical; Potential
Transmembrane84 – 10421Helical; Potential
Transmembrane121 – 14121Helical; Potential
Transmembrane170 – 19021Helical; Potential
Transmembrane208 – 22821Helical; Potential
Transmembrane259 – 27921Helical; Potential
Transmembrane291 – 31121Helical; Potential
Transmembrane329 – 34921Helical; Potential
Transmembrane362 – 38221Helical; Potential
Transmembrane401 – 42121Helical; Potential
Transmembrane438 – 45821Helical; Potential
Transmembrane476 – 49621Helical; Potential

Sites

Metal binding821Iron (heme A axial ligand) Probable
Metal binding2651Copper B Probable
Metal binding2691Copper B Probable
Metal binding3141Copper B Probable
Metal binding3151Copper B Probable
Metal binding4001Iron (heme A3 axial ligand) Probable
Metal binding4021Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link265 ↔ 2691'-histidyl-3'-tyrosine (His-Tyr) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q08855 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 740C8FE6C902D9BF

FASTA53859,133
        10         20         30         40         50         60 
MATSAAAHGE HAEDHGHDEH AHPTGWRRST NHKDIGTLYL IFAIIAGVIG AAMSLAIRAE 

        70         80         90        100        110        120 
LMYPGVEYFH NTHLYNVFVT SHGVIMIFFM VMPAMIGGFG NWFLPLMIGA PDMAFPRMNN 

       130        140        150        160        170        180 
ISFWLLPASF GLLLMSTFVE GEPGANGAGA GWTMYVPLSS SGHPGPAVDL AIFSLHIAGA 

       190        200        210        220        230        240 
SSILGAINFI TTILNMRAPG MTLHKMPLFA WSVLITAFLL LLSLPVLAGA ITMLLTDRNF 

       250        260        270        280        290        300 
GTTFFAPEGG GDPLLYQHLF WFFGHPEVYI LILPGFGMIS HIISTFSRKP VFGYIGMVYA 

       310        320        330        340        350        360 
MAAIGGLGFV VWAHHMYIVG MDLDTEAYFV SATMIIAVPT GIKIFSWIAT MWGGSIEFAT 

       370        380        390        400        410        420 
PMLWALAFIF LFTVGGVTGV VLANASLDRV LHDTYYVVAH FHYVLSLGAI FAIFAGWYYW 

       430        440        450        460        470        480 
FPKMSGYMYN ETLAEAHFWL IFIGVNLIFF PEHFLGISGM PRRYIDYPDA FAGWNLVSSI 

       490        500        510        520        530 
GSYISGFSVL LFIYCVYDAF AKNVPVGDNP WGAGATTLEW TLPSPPPVHE FEVLPRVE 

« Hide

References

[1]"Cytochrome aa3 gene regulation in members of the family Rhizobiaceae: comparison of copper and oxygen effects in Bradyrhizobium japonicum and Rhizobium tropici."
Gabel C., Bittinger M.A., Maier R.J.
Appl. Environ. Microbiol. 60:141-148(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74341 Genomic DNA. Translation: CAA52388.1.
PIRS36424.

3D structure databases

ProteinModelPortalQ08855.
SMRQ08855. Positions 24-538.
ModBaseSearch...
MobiDBSearch...

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. SSF81442. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX1_RHILE
AccessionPrimary (citable) accession number: Q08855
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways