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Q8FNQ7 (COX2_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 2

EC=1.9.3.1
Alternative name(s):
Cytochrome aa3 subunit 2
Cytochrome c oxidase polypeptide II
Oxidase aa(3) subunit 2
Gene names
Name:ctaC
Ordered Locus Names:CE2087
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Subunits 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) By similarity.

Catalytic activity

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

Cofactor

Binds 2 copper A ions per subunit By similarity.

Subunit structure

Associates with subunits I, III and IV to form cytochrome c oxidase By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the cytochrome c oxidase subunit 2 family.

Sequence caution

The sequence BAC18897.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 By similarity
Chain29 – 359331Cytochrome c oxidase subunit 2 By similarity
PRO_0000006053

Regions

Transmembrane64 – 8421Helical; Potential
Transmembrane107 – 12721Helical; Potential

Sites

Metal binding2441Copper A1 By similarity
Metal binding2851Copper A1 By similarity
Metal binding2851Copper A2 By similarity
Metal binding2871Copper A2; via carbonyl oxygen By similarity
Metal binding2891Copper A1 By similarity
Metal binding2891Copper A2 By similarity
Metal binding2931Copper A2 By similarity
Metal binding2961Copper A1 By similarity

Amino acid modifications

Lipidation291N-palmitoyl cysteine By similarity
Lipidation291S-diacylglycerol cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FNQ7 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: B5CB70825F161436

FASTA35939,765
        10         20         30         40         50         60 
MEQQNKRGLK RKALLGGVLG SGGLAMAGCE VSPPGGMIGD FLRMGWPSGI TPEAVSMGNF 

        70         80         90        100        110        120 
WSWVWVAAWI IGIIMWGLML TAIFSWNAKK AEKRGEGEFP KQLQYNVPLE LVLTIVPIII 

       130        140        150        160        170        180 
VMVLFFFTVQ TQDRVTALDK NPEVTVNVTA YQWNWKFGYG ELAPEFAPAG GDYDGVDEAR 

       190        200        210        220        230        240 
QASAEASKID PSGNNPIHGN SKKDMSYLHF NQIETLGTTD EVPVLVLPTN TPIEFNLASA 

       250        260        270        280        290        300 
DVAHSFWVPE FLFKRDLYAH PEANKSQRVF QIDEIFEEGA FVGRCAEMCG TYHAMMNFEL 

       310        320        330        340        350 
RTVDRETFAE YIAFRDANPD ATNAQALEHI GEAPYATSTA PFVSDRTGTR DGENFQTPA 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18897.1. Different initiation.
RefSeqNP_738697.1. NC_004369.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196164.CE2087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18897; BAC18897; BAC18897.
GeneID1031940.
KEGGcef:CE2087.
PATRIC21490309. VBICorEff9312_2069.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000245527.
KOK02275.
OrthoDBEOG68SVXT.

Enzyme and pathway databases

BioCycCEFF196164:GJW8-2123-MONOMER.

Family and domain databases

Gene3D1.10.287.90. 1 hit.
2.60.40.420. 2 hits.
InterProIPR001505. Copper_CuA.
IPR008972. Cupredoxin.
IPR002429. Cyt_c_oxidase_su2_C.
IPR011759. Cyt_c_oxidase_su2_TM_dom.
[Graphical view]
PfamPF00116. COX2. 1 hit.
[Graphical view]
SUPFAMSSF49503. SSF49503. 2 hits.
SSF81464. SSF81464. 1 hit.
PROSITEPS00078. COX2. 1 hit.
PS50857. COX2_CUA. 1 hit.
PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX2_COREF
AccessionPrimary (citable) accession number: Q8FNQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: May 14, 2014
This is version 83 of the entry and version 2 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