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P98005 (COX13_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cytochrome c oxidase polypeptide I+III
EC=1.9.3.1
Alternative name(s):
Cytochrome c aa(3) subunit 1
Short name=A-protein
Short name=Cytochrome caa3
Gene names
Name:caaA
Synonyms:ctaD
Ordered Locus Names:TTHA0312
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus ›

Protein attributes

Sequence length791 AA.
Sequence statusComplete.
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.

Subunit structure

Possibly a heterodimer of A-protein (contains: cytochrome c oxidase subunits I and III) and subunit II. The A-protein could also present a precursor form of subunits I and III.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

In the N-terminal section; belongs to the heme-copper respiratory oxidase family.

In the C-terminal section; belongs to the cytochrome c oxidase subunit 3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 791791Cytochrome c oxidase polypeptide I+III
PRO_0000183464

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane78 – 9821Helical; Potential
Transmembrane111 – 13121Helical; Potential
Transmembrane155 – 17521Helical; Potential
Transmembrane201 – 22121Helical; Potential
Transmembrane244 – 26421Helical; Potential
Transmembrane282 – 30221Helical; Potential
Transmembrane312 – 33221Helical; Potential
Transmembrane347 – 36721Helical; Potential
Transmembrane381 – 40121Helical; Potential
Transmembrane423 – 44321Helical; Potential
Transmembrane464 – 48421Helical; Potential
Transmembrane566 – 58621Helical; Potential
Transmembrane617 – 63721Helical; Potential
Transmembrane657 – 67721Helical; Potential
Transmembrane691 – 71121Helical; Potential
Transmembrane729 – 74921Helical; Potential
Transmembrane771 – 79121Helical; Potential
Region1 – 473473COX1
Region545 – 791247COX3

Sites

Metal binding731Iron (heme A axial ligand) Probable
Metal binding2501Copper B
Metal binding2541Copper B
Metal binding2991Copper B Probable
Metal binding3001Copper B Probable
Metal binding3851Iron (heme A3 axial ligand) Probable
Metal binding3871Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link250 ↔ 2541'-histidyl-3'-tyrosine (His-Tyr) By similarity

Secondary structure

1 .................................................................................. 791
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P98005 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: F4DCF3E8AFF07606

FASTA79189,214
        10         20         30         40         50         60 
MAITAKPKAG VWAVLWDLLT TVDHKKIGLM YTATAFFAFA LAGVFSLLIR TQLAVPNNQF 

        70         80         90        100        110        120 
LTGEQYNQIL TLHGATMLFF FIIQAGLTGF GNFVVPLMLG ARDVALPRVN AFSYWAFLGA 

       130        140        150        160        170        180 
IVLALMSYFF PGGAPSVGWT FYYPFSAQSE SGVDFYLAAI LLLGFSSLLG NANFVATIYN 

       190        200        210        220        230        240 
LRAQGMSLWK MPIYVWSVFA ASVLNLFSLA GLTAATLLVL LERKIGLSWF NPAVGGDPVL 

       250        260        270        280        290        300 
FQQFFWFYSH PTVYVMLLPY LGILAEVAST FARKPLFGYR QMVWAQMGIV VLGTMVWAHH 

       310        320        330        340        350        360 
MFTVGESTLF QIAFAFFTAL IAVPTGVKLF NIIGTLWGGK LQMKTPLYWV LGFIFNFLLG 

       370        380        390        400        410        420 
GITGVMLSMT PLDYQFHDSY FVVAHFHNVL MAGSGFGAFA GLYYWWPKMT GRMYDERLGR 

       430        440        450        460        470        480 
LHFWLFLVGY LLTFLPQYAL GYLGMPRRYY TYNADIAGWP ELNLLSTIGA YILGLGGLVW 

       490        500        510        520        530        540 
IYTMWKSLRS GPKAPDNPWG GYTLEWLTAS PPKAHNFDVK LPTEFPSERP LYDWKKKGVE 

       550        560        570        580        590        600 
LKPEDPAHIH LPNSSFWPFY SAATLFAFFV AVAALPVPNV WMWVFLALFA YGLVRWALED 

       610        620        630        640        650        660 
EYSHPVEHHT VTGKSNAWMG MAWFIVSEVG LFAILIAGYL YLRLSGAATP PEERPALWLA 

       670        680        690        700        710        720 
LLNTFLLVSS SFTVHFAHHD LRRGRFNPFR FGLLVTIILG VLFFLVQSWE FYQFYHHSSW 

       730        740        750        760        770        780 
QENLWTAAFF TIVGLHGLHV VIGGFGLILA YLQALRGKIT LHNHGTLEAA SMYWHLVDAV 

       790 
WLVIVTIFYV W

« Hide

References

« Hide 'large scale' references
[1]"Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence of the fused gene and analysis of the deduced primary structures for subunits I and III of cytochrome caa3."
Mather M.W., Springer P., Hensel S., Buse G., Fee J.A.
J. Biol. Chem. 268:5395-5408(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase."
Buse G., Soulimane T., Dewor M., Meyer H.E., Blueggel M.
Protein Sci. 8:985-990(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: COVALENT BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M84341 Genomic DNA. Translation: AAA27485.1.
AP008226 Genomic DNA. Translation: BAD70135.1.
PIRA46616.
RefSeqYP_143578.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YEVX-ray2.36A/D1-791[»]
ProteinModelPortalP98005.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-59901N.
STRING300852.TTHA0312.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD70135; BAD70135; BAD70135.
GeneID3168081.
KEGGttj:TTHA0312.
PATRIC23955580. VBITheThe93045_0312.

Phylogenomic databases

eggNOGCOG0843.
HOGENOMHOG000085274.
KOK15408.
OMAGFIFNFL.
ProtClustDBCLSK445695.

Enzyme and pathway databases

UniPathwayUPA00705.

Family and domain databases

Gene3D1.20.120.80. 1 hit.
1.20.210.10. 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.
IPR000298. Cyt_c_oxidase_su3.
IPR013833. Cyt_c_oxidase_su3_a-hlx.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
PF00510. COX3. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. COX1. 1 hit.
SSF81452. CytC_oxdse_III. 1 hit.
TIGRFAMsTIGR02891. CtaD_CoxA. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
PS50253. COX3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOX13_THET8
AccessionPrimary (citable) accession number: P98005
Secondary accession number(s): Q5SLI1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 1, 2013
This is version 105 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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