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Q6NFM3 (COX1_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. 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
Ordered Locus Names:DIP1864
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length564 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 – 564564Cytochrome c oxidase subunit 1
PRO_0000183438

Regions

Transmembrane43 – 6321Helical; Potential
Transmembrane83 – 10321Helical; 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
Q6NFM3 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2865A8DB72B3CA6E

FASTA56463,291
        10         20         30         40         50         60 
MTAVAPRLEN YAEPTRPAPT GGARKGTLAW KMLTTTDHKL LGMMYIVMSF VWFFVGGLMA 

        70         80         90        100        110        120 
LLIRAELFSP GLQFLSNEQF NQLFTLHGTI MLLAFGTPVV WGFSNYILPL QIGAPDVAFP 

       130        140        150        160        170        180 
RLNAFGFWIT QIGVVAMLAG FLTPGGAADF GWTMYLPLAD SIHSPGVGGD FWIIGVGATG 

       190        200        210        220        230        240 
VGTIASAVNM ITTILCMRAP GMTMFRMPIF CWNIFVASVI VLLIFPLLTA AALGVMYDRK 

       250        260        270        280        290        300 
LGGHIYDPGN GGAILWQHLF WFFGHPEVYV LALPFFGIVS EVIPVFARKP MFGYIGLVFA 

       310        320        330        340        350        360 
TLSIGMLSMA VWAHHMFVTG AILLPFFSFM TFLISVPTGV KFFNWLGTMW RGHISWETPM 

       370        380        390        400        410        420 
TWTMGFLVTF LFGGLTGIML ASPPLDFHIS DTYFVVAHFH YTLFGTVVFA SYAGVYFWFP 

       430        440        450        460        470        480 
KMTGRMLDER LGKIHFWITF VGFHGTFLVQ HWVGNEGMPR RYADYLESDG FTTLNQISTV 

       490        500        510        520        530        540 
FSFLLGVSVI PFIWNVFKSY RYGEIVTVDD PWGYGNSLEW ATSCPPPRHN FTSLPRIRSE 

       550        560 
RPAFELHYPH MVERMRREAH IGHH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248359 Genomic DNA. Translation: CAE50393.1.
RefSeqNP_940201.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NFM3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1864.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE50393; CAE50393; DIP1864.
GeneID2649239.
KEGGcdi:DIP1864.
PATRIC21484962. VBICorDip47633_1848.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK02274.
OMAIGANESH.
OrthoDBEOG6B35XR.

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_CORDI
AccessionPrimary (citable) accession number: Q6NFM3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 79 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