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P98005

- COX13_THET8

UniProt

P98005 - COX13_THET8

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Protein

Cytochrome c oxidase polypeptide I+III

Gene

caaA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Cu2+Note: Binds 1 copper B ion per subunit.
  • hemeNote: Binds 2 heme groups per subunit.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi73 – 731Iron (heme A axial ligand)Curated
Metal bindingi250 – 2501Copper B
Metal bindingi254 – 2541Copper B
Metal bindingi299 – 2991Copper BCurated
Metal bindingi300 – 3001Copper BCurated
Metal bindingi385 – 3851Iron (heme A3 axial ligand)Curated
Metal bindingi387 – 3871Iron (heme A axial ligand)Curated

GO - Molecular functioni

  1. copper ion binding Source: InterPro
  2. cytochrome-c oxidase activity Source: UniProtKB-EC
  3. heme binding Source: InterPro
  4. iron ion binding Source: InterPro

GO - Biological processi

  1. aerobic respiration Source: InterPro
  2. oxidative phosphorylation Source: UniProtKB-UniPathway
  3. respiratory electron transport chain Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Hydrogen ion transport, Ion transport, Respiratory chain, Transport

Keywords - Ligandi

Copper, Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-326-MONOMER.
UniPathwayiUPA00705.

Protein family/group databases

TCDBi3.D.4.4.3. the proton-translocating cytochrome oxidase (cox) superfamily.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:caaA
Synonyms:ctaD
Ordered Locus Names:TTHA0312
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
ProteomesiUP000000532: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei29 – 4921HelicalSequence AnalysisAdd
BLAST
Transmembranei78 – 9821HelicalSequence AnalysisAdd
BLAST
Transmembranei111 – 13121HelicalSequence AnalysisAdd
BLAST
Transmembranei155 – 17521HelicalSequence AnalysisAdd
BLAST
Transmembranei201 – 22121HelicalSequence AnalysisAdd
BLAST
Transmembranei244 – 26421HelicalSequence AnalysisAdd
BLAST
Transmembranei282 – 30221HelicalSequence AnalysisAdd
BLAST
Transmembranei312 – 33221HelicalSequence AnalysisAdd
BLAST
Transmembranei347 – 36721HelicalSequence AnalysisAdd
BLAST
Transmembranei381 – 40121HelicalSequence AnalysisAdd
BLAST
Transmembranei423 – 44321HelicalSequence AnalysisAdd
BLAST
Transmembranei464 – 48421HelicalSequence AnalysisAdd
BLAST
Transmembranei566 – 58621HelicalSequence AnalysisAdd
BLAST
Transmembranei617 – 63721HelicalSequence AnalysisAdd
BLAST
Transmembranei657 – 67721HelicalSequence AnalysisAdd
BLAST
Transmembranei691 – 71121HelicalSequence AnalysisAdd
BLAST
Transmembranei729 – 74921HelicalSequence AnalysisAdd
BLAST
Transmembranei771 – 79121HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-KW
  3. respiratory chain Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 791791Cytochrome c oxidase polypeptide I+IIIPRO_0000183464Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki250 ↔ 2541'-histidyl-3'-tyrosine (His-Tyr)By similarity

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

DIPiDIP-59901N.
STRINGi300852.TTHA0312.

Structurei

Secondary structure

1
791
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 208Combined sources
Helixi24 – 5229Combined sources
Helixi63 – 8018Combined sources
Helixi82 – 854Combined sources
Turni86 – 883Combined sources
Helixi89 – 9911Combined sources
Helixi107 – 12620Combined sources
Helixi127 – 1293Combined sources
Turni138 – 1414Combined sources
Helixi145 – 1484Combined sources
Helixi153 – 18028Combined sources
Helixi188 – 1903Combined sources
Helixi193 – 20816Combined sources
Helixi210 – 22516Combined sources
Helixi232 – 2343Combined sources
Helixi238 – 24912Combined sources
Helixi251 – 27222Combined sources
Helixi279 – 29214Combined sources
Helixi297 – 3004Combined sources
Helixi308 – 32013Combined sources
Helixi322 – 33615Combined sources
Helixi345 – 36824Combined sources
Helixi370 – 3767Combined sources
Helixi380 – 39011Combined sources
Turni391 – 3933Combined sources
Helixi394 – 41017Combined sources
Helixi416 – 44227Combined sources
Beta strandi446 – 4483Combined sources
Beta strandi454 – 4563Combined sources
Helixi459 – 49032Combined sources
Helixi504 – 5074Combined sources
Beta strandi526 – 5283Combined sources
Helixi530 – 5367Combined sources
Helixi546 – 5483Combined sources
Helixi557 – 57418Combined sources
Helixi580 – 59718Combined sources
Beta strandi611 – 6144Combined sources
Helixi616 – 64429Combined sources
Helixi657 – 68327Combined sources
Helixi686 – 71530Combined sources
Turni720 – 7223Combined sources
Helixi724 – 75633Combined sources
Helixi765 – 78824Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YEVX-ray2.36A/D1-791[»]
ProteinModelPortaliP98005.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 473473COX1Add
BLAST
Regioni545 – 791247COX3Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the heme-copper respiratory oxidase family.Curated
In the C-terminal section; belongs to the cytochrome c oxidase subunit 3 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0843.
HOGENOMiHOG000085274.
KOiK15408.
OMAiMGMTRRV.
OrthoDBiEOG6B35XR.
PhylomeDBiP98005.

Family and domain databases

Gene3Di1.20.120.80. 1 hit.
1.20.210.10. 1 hit.
InterProiIPR000883. COX1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
IPR013833. Cyt_c_oxidase_su3_a-hlx.
IPR000298. Cyt_c_oxidase_su3_dom.
[Graphical view]
PANTHERiPTHR10422. PTHR10422. 1 hit.
PfamiPF00115. COX1. 1 hit.
PF00510. COX3. 1 hit.
[Graphical view]
PRINTSiPR01165. CYCOXIDASEI.
SUPFAMiSSF81442. SSF81442. 1 hit.
SSF81452. SSF81452. 1 hit.
TIGRFAMsiTIGR02891. CtaD_CoxA. 1 hit.
PROSITEiPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
PS50253. COX3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P98005-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAITAKPKAG VWAVLWDLLT TVDHKKIGLM YTATAFFAFA LAGVFSLLIR
60 70 80 90 100
TQLAVPNNQF LTGEQYNQIL TLHGATMLFF FIIQAGLTGF GNFVVPLMLG
110 120 130 140 150
ARDVALPRVN AFSYWAFLGA IVLALMSYFF PGGAPSVGWT FYYPFSAQSE
160 170 180 190 200
SGVDFYLAAI LLLGFSSLLG NANFVATIYN LRAQGMSLWK MPIYVWSVFA
210 220 230 240 250
ASVLNLFSLA GLTAATLLVL LERKIGLSWF NPAVGGDPVL FQQFFWFYSH
260 270 280 290 300
PTVYVMLLPY LGILAEVAST FARKPLFGYR QMVWAQMGIV VLGTMVWAHH
310 320 330 340 350
MFTVGESTLF QIAFAFFTAL IAVPTGVKLF NIIGTLWGGK LQMKTPLYWV
360 370 380 390 400
LGFIFNFLLG GITGVMLSMT PLDYQFHDSY FVVAHFHNVL MAGSGFGAFA
410 420 430 440 450
GLYYWWPKMT GRMYDERLGR LHFWLFLVGY LLTFLPQYAL GYLGMPRRYY
460 470 480 490 500
TYNADIAGWP ELNLLSTIGA YILGLGGLVW IYTMWKSLRS GPKAPDNPWG
510 520 530 540 550
GYTLEWLTAS PPKAHNFDVK LPTEFPSERP LYDWKKKGVE LKPEDPAHIH
560 570 580 590 600
LPNSSFWPFY SAATLFAFFV AVAALPVPNV WMWVFLALFA YGLVRWALED
610 620 630 640 650
EYSHPVEHHT VTGKSNAWMG MAWFIVSEVG LFAILIAGYL YLRLSGAATP
660 670 680 690 700
PEERPALWLA LLNTFLLVSS SFTVHFAHHD LRRGRFNPFR FGLLVTIILG
710 720 730 740 750
VLFFLVQSWE FYQFYHHSSW QENLWTAAFF TIVGLHGLHV VIGGFGLILA
760 770 780 790
YLQALRGKIT LHNHGTLEAA SMYWHLVDAV WLVIVTIFYV W
Length:791
Mass (Da):89,214
Last modified:February 1, 1996 - v1
Checksum:iF4DCF3E8AFF07606
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84341 Genomic DNA. Translation: AAA27485.1.
AP008226 Genomic DNA. Translation: BAD70135.1.
PIRiA46616.
RefSeqiWP_011227851.1. NC_006461.1.
YP_143578.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70135; BAD70135; BAD70135.
GeneIDi3168081.
KEGGittj:TTHA0312.
PATRICi23955580. VBITheThe93045_0312.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84341 Genomic DNA. Translation: AAA27485.1 .
AP008226 Genomic DNA. Translation: BAD70135.1 .
PIRi A46616.
RefSeqi WP_011227851.1. NC_006461.1.
YP_143578.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YEV X-ray 2.36 A/D 1-791 [» ]
ProteinModelPortali P98005.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59901N.
STRINGi 300852.TTHA0312.

Protein family/group databases

TCDBi 3.D.4.4.3. the proton-translocating cytochrome oxidase (cox) superfamily.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAD70135 ; BAD70135 ; BAD70135 .
GeneIDi 3168081.
KEGGi ttj:TTHA0312.
PATRICi 23955580. VBITheThe93045_0312.

Phylogenomic databases

eggNOGi COG0843.
HOGENOMi HOG000085274.
KOi K15408.
OMAi MGMTRRV.
OrthoDBi EOG6B35XR.
PhylomeDBi P98005.

Enzyme and pathway databases

UniPathwayi UPA00705 .
BioCyci TTHE300852:GH8R-326-MONOMER.

Family and domain databases

Gene3Di 1.20.120.80. 1 hit.
1.20.210.10. 1 hit.
InterProi IPR000883. COX1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
IPR014241. Cyt_c_oxidase_su1_bac.
IPR013833. Cyt_c_oxidase_su3_a-hlx.
IPR000298. Cyt_c_oxidase_su3_dom.
[Graphical view ]
PANTHERi PTHR10422. PTHR10422. 1 hit.
Pfami PF00115. COX1. 1 hit.
PF00510. COX3. 1 hit.
[Graphical view ]
PRINTSi PR01165. CYCOXIDASEI.
SUPFAMi SSF81442. SSF81442. 1 hit.
SSF81452. SSF81452. 1 hit.
TIGRFAMsi TIGR02891. CtaD_CoxA. 1 hit.
PROSITEi PS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
PS50253. COX3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCOX13_THET8
AccessioniPrimary (citable) accession number: P98005
Secondary accession number(s): Q5SLI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3