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P16262 (COX1_BACP3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. 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:caaB, coi
OrganismBacillus sp. (strain PS3)
Taxonomic identifier2334 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.

Catalytic activity

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

Cofactor

Binds 1 copper B ion per subunit.

Binds 2 heme groups per subunit.

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Miscellaneous

Under slightly air-limited conditions, the cytochrome a3 center of the enzyme is replaced by cytochrome o.

This cytochrome c oxidase shows clear proton pump activity in addition to electron transfer across the membrane.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Sequence caution

The sequence BAA01793.1 differs from that shown. Reason: Frameshift at positions 520 and 540.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2
Chain2 – 616615Cytochrome c oxidase subunit 1
PRO_0000183435

Regions

Transmembrane28 – 4821Helical; Potential
Transmembrane75 – 9521Helical; Potential
Transmembrane102 – 12221Helical; Potential
Transmembrane158 – 17821Helical; Potential
Transmembrane198 – 21821Helical; Potential
Transmembrane243 – 26321Helical; Potential
Transmembrane275 – 29521Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane349 – 36921Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane420 – 44021Helical; Potential
Transmembrane463 – 48321Helical; Potential
Transmembrane553 – 57321Helical; Potential
Transmembrane577 – 59721Helical; Potential

Sites

Metal binding721Iron (heme A axial ligand) Probable
Metal binding2491Copper B Probable
Metal binding2531Copper B Probable
Metal binding2981Copper B Probable
Metal binding2991Copper B Probable
Metal binding3841Iron (heme A3/O axial ligand) Probable
Metal binding3861Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link249 ↔ 2531'-histidyl-3'-tyrosine (His-Tyr) By similarity

Experimental info

Sequence conflict4481V → W in BAA01793. Ref.2
Sequence conflict4701F → I in BAA01793. Ref.2
Sequence conflict506 – 5083AIA → RS in BAA01793. Ref.2
Sequence conflict525 – 5262LD → WT AA sequence Ref.2
Sequence conflict5491Missing AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P16262 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 17DF1E3325014B96

FASTA61668,294
        10         20         30         40         50         60 
MSTIARKKGV GAVLWDYLTT VDHKKIAHLY LISGGFFFLL GGLEALFIRI QLAKPNNDFL 

        70         80         90        100        110        120 
VGGLYNEVLT MHGTTMIFLA AMPLVFAFMN AVVPLQIGAR DVAFPFLNAL GFWMFFFGGL 

       130        140        150        160        170        180 
FLNCSWFLGG APDAGWTSYA SLSLDSKAHH GIDFYTLGLQ ISGFGTIMGA INFLVTIINM 

       190        200        210        220        230        240 
RAPGMTFMRM PMFTWATFVT SALILFAFPP LTVGLIFMMM DRLFGGNFFN PAAGGNTIIW 

       250        260        270        280        290        300 
EHLFWVFGHP EVYILVLPAF GIFSEIFATF SRKRLFGYSS MVFATVLIAF LGFMVWAHHM 

       310        320        330        340        350        360 
FTVGMGPIAN AIFAVATMTI AVPTGVKIFN WLFTMWGGSI KFTTPMHYAV AFIPSFVMGG 

       370        380        390        400        410        420 
VTGVMLASAA ADYQYHDSYF VVAHFHYVIV GGVVFALLAG THYWWPKMFG RMLNETLGKI 

       430        440        450        460        470        480 
TFWLFFIGFH LTFFIQHFLG LTGMPRRVFT YLPHQGWETG NLISTIGAFF IAAATVILLI 

       490        500        510        520        530        540 
NIVVTTAKGE KVPGDAWGDG RTLEWAIASP PPVYNFAQTP LVRGLDAFWL EKMEGKKELT 

       550        560        570        580        590        600 
PAEPLGDIHM PNSSFLPFVI AFGLFVAAFG FTYHNDAGWG LPVAILGLLI TLGSMFLRSV 

       610 
IDDHGFHIHK EEVLEL 

« Hide

References

[1]"Nucleotide sequence of the gene coding for four subunits of cytochrome c oxidase from the thermophilic bacterium PS3."
Ishizuka M., Machida K., Shimada S., Mogi A., Tsuchiya T., Ohmori T., Souma Y., Gonda M., Sone N.
J. Biochem. 108:866-873(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-31.
[2]"Nucleotide sequence of the gene coding for cytochrome oxidase subunit I from the thermophilic bacterium PS3."
Sone N., Yokoi F., Fu T., Ohta S., Metso T., Raitio M., Saraste M.
J. Biochem. 103:606-610(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-552, PROTEIN SEQUENCE OF 2-15.
[3]"Haem O2 can replace haem A in the active site of cytochrome c oxidase from thermophilic bacterium PS3."
Sone N., Fujiwara Y.
FEBS Lett. 288:154-158(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13955 Genomic DNA. Translation: BAA03046.1.
D11038 Genomic DNA. Translation: BAA01793.1. Frameshift.
PIRJX0140.

3D structure databases

ProteinModelPortalP16262.
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_BACP3
AccessionPrimary (citable) accession number: P16262
Secondary accession number(s): Q56248
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 106 of the entry and version 3 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