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Q8FMT1 (COX1_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:CE2418
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length580 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 580580Cytochrome c oxidase subunit 1
PRO_0000183439

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q8FMT1 [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

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: BAC19228.1.
RefSeqNP_739028.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FMT1.
ModBaseSearch...

Protein-protein interaction databases

STRING196164.CE2418.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC19228; BAC19228; BAC19228.
GeneID1032090.
KEGGcef:CE2418.
PATRIC21490967. VBICorEff9312_2388.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000085274.
KOK02274.
OMAIVSHIIS.
ProtClustDBCLSK2519649.

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...

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: May 1, 2013
This is version 78 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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