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Reviewed, UniProtKB/Swiss-Prot Q8FMT1 (COX1_COREF)

Last modified June 16, 2009. Version 47. 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
    EC=1.9.3.1
Alternative name(s):
    Cytochrome c oxidase polypeptide I
    Cytochrome aa3 subunit 1
Gene names
Name: ctaD
Ordered Locus Names: CE2418
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

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Protein attributes

Sequence length580 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 copper B per subunit By similarity.

Binds 2 heme groups per subunit By similarity.

Pathway

Energy metabolism; oxidative phosphorylation.

Subunit structure

Associates with subunits II, 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 heme-copper respiratory oxidase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Cytochrome c oxidase subunit 1
PRO_0000183439

Regions

Transmembrane43 – 6321 Potential
Transmembrane90 – 11021 Potential
Transmembrane122 – 14221 Potential
Transmembrane171 – 19121 Potential
Transmembrane214 – 23421 Potential
Transmembrane259 – 27921 Potential
Transmembrane292 – 31221 Potential
Transmembrane316 – 33621 Potential
Transmembrane360 – 38021 Potential
Transmembrane399 – 41921 Potential
Transmembrane434 – 45421 Potential
Transmembrane477 – 49721 Potential

Sites

Metal binding871Iron (heme A axial ligand) Probable
Metal binding2651Copper B Probable
Metal binding2691Copper B Probable
Metal binding3141Copper B Probable
Metal binding3151Copper B Probable
Metal binding3981Iron (heme A3 axial ligand) Probable
Metal binding4001Iron (heme A axial ligand) Probable

Amino acid modifications

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

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Sequences

Sequence LengthMass (Da)Tools
Q8FMT1-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E1C111059A367259

FASTA58064,952
        10         20         30         40         50         60 
MTAVAPRVDG HVAPQRPEPT GHARKGSKAW LMMTTTDHKQ LGIMYIIMSF SFFFLGGLMA 

        70         80         90        100        110        120 
LLIRAELFTP GLQFLSNEQF NQLFTMHGTV MLLLYGTPIV WGFANYVLPL QIGAPDVAFP 

       130        140        150        160        170        180 
RLNAFGFWIT TVGGVAMLAG FLTPGGAADF GWTMYSPLSD SIHSPGIGSD MWIIGVGATG 

       190        200        210        220        230        240 
IGSVASAINM LTTILCLRAP GMTMFRMPVF TWNIFVTSVL ALLIFPLLLA AALGVLYDRK 

       250        260        270        280        290        300 
LGGHIYDPAN GGSILWQHLF WFFGHPEVYV LALPFFGIIS EIIPVFSRKP MFGYIGLVFA 

       310        320        330        340        350        360 
TLSIGALSMA VWAHHMFVTG AVLLPFFSFM TFLISVPTGV KFFNWVGTMW KGHITWETPM 

       370        380        390        400        410        420 
IWAVGFMSTF LFGGLTGIML ASPPLDFHLS DSYFLIAHFH YTLFGTVVFA SCAGVYFWFP 

       430        440        450        460        470        480 
KMTGRMMDER LGKIHFWLTF VGFHGTFMVQ HWLGNMGMPR RYADYLDSDG FTTLNQISTI 

       490        500        510        520        530        540 
FSFLLGLSVI PFVWNVFKSW RYGELVTVDD PWGYGNSLEW ATSCPPPRHN FTSLPRIRSE 

       550        560        570        580 
RPAFELHYPH MIERMRREAH VGEHDLRAET TQSPTPAEVR

« Hide

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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: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

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Cross-references

Sequence databases

BA000035 Genomic DNA. Translation: BAC19228.1.
RefSeqNP_739028.1.

3D structure databases

HSSPHSSP built from PDB template 1FFT based on UniProtKB P18401.
ModBaseSearch...

Genome annotation databases

GeneID1032090.
GenomeReviewsGene locus CE2418 in contig BA000035_GR.
KEGGcef:CE2418.
NMPDRfig|196164.1.peg.2418.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8FMT1.
OMAQ8FMT1. TIIKLRR.

Enzyme and pathway databases

BioCycCEFF196164:CE2418-MON.
BRENDA1.9.3.1. 277326.

Family and domain databases

InterProIPR000883. Cyt_c_oxidase_su1.
IPR014241. Cyt_c_oxidase_su1_bac.
[Graphical view]
Gene3DG3DSA:1.20.210.10. COX1. 1 hit.
PANTHERPTHR10422. COX1. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCOX1_COREF
AccessionPrimary (citable) accession number: Q8FMT1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 47 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