COX13_THET8
ID COX13_THET8 Reviewed; 791 AA.
AC P98005; Q5SLI1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cytochrome c oxidase polypeptide I+III;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c aa(3) subunit 1;
DE Short=A-protein;
DE Short=Cytochrome caa3;
GN Name=caaA; Synonyms=ctaD; OrderedLocusNames=TTHA0312;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383670; DOI=10.1016/s0021-9258(18)53335-4;
RA Mather M.W., Springer P., Hensel S., Buse G., Fee J.A.;
RT "Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence of
RT the fused gene and analysis of the deduced primary structures for subunits
RT I and III of cytochrome caa3.";
RL J. Biol. Chem. 268:5395-5408(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP COVALENT BOND.
RX PubMed=10338009; DOI=10.1110/ps.8.5.985;
RA Buse G., Soulimane T., Dewor M., Meyer H.E., Blueggel M.;
RT "Evidence for a copper-coordinated histidine-tyrosine cross-link in the
RT active site of cytochrome oxidase.";
RL Protein Sci. 8:985-990(1999).
CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC form the functional core of the enzyme complex. Co I is the catalytic
CC subunit of the enzyme. Electrons originating in cytochrome c are
CC transferred via the copper A center of subunit 2 and heme a of subunit
CC 1 to the bimetallic center formed by heme a3 and copper B. This
CC cytochrome c oxidase shows proton pump activity across the membrane in
CC addition to the electron transfer.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Note=Binds 1 copper B ion per subunit.;
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 2 heme groups per subunit.;
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBUNIT: Possibly a heterodimer of A-protein (contains: cytochrome c
CC oxidase subunits I and III) and subunit II. The A-protein could also
CC present a precursor form of subunits I and III.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: In the N-terminal section; belongs to the heme-copper
CC respiratory oxidase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the cytochrome c
CC oxidase subunit 3 family. {ECO:0000305}.
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DR EMBL; M84341; AAA27485.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70135.1; -; Genomic_DNA.
DR PIR; A46616; A46616.
DR RefSeq; WP_011227851.1; NC_006461.1.
DR RefSeq; YP_143578.1; NC_006461.1.
DR PDB; 2YEV; X-ray; 2.36 A; A/D=1-791.
DR PDBsum; 2YEV; -.
DR AlphaFoldDB; P98005; -.
DR SMR; P98005; -.
DR DIP; DIP-59901N; -.
DR IntAct; P98005; 2.
DR STRING; 300852.55771694; -.
DR TCDB; 3.D.4.4.3; the proton-translocating cytochrome oxidase (cox) superfamily.
DR EnsemblBacteria; BAD70135; BAD70135; BAD70135.
DR GeneID; 3168081; -.
DR KEGG; ttj:TTHA0312; -.
DR PATRIC; fig|300852.9.peg.312; -.
DR eggNOG; COG0843; Bacteria.
DR eggNOG; COG1845; Bacteria.
DR HOGENOM; CLU_011899_4_0_0; -.
DR OMA; WAMMSIG; -.
DR PhylomeDB; P98005; -.
DR BRENDA; 7.1.1.9; 2305.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.120.80; -; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR Pfam; PF00510; COX3; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR SUPFAM; SSF81452; SSF81452; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
DR PROSITE; PS50253; COX3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Electron transport; Heme;
KW Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..791
FT /note="Cytochrome c oxidase polypeptide I+III"
FT /id="PRO_0000183464"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 729..749
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 771..791
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..473
FT /note="COX1"
FT REGION 545..791
FT /note="COX3"
FT BINDING 73
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 250
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 254
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 299
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 300
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 385
FT /ligand="heme a3"
FT /ligand_id="ChEBI:CHEBI:83282"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 387
FT /ligand="Fe(II)-heme a"
FT /ligand_id="ChEBI:CHEBI:61715"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT CROSSLNK 250..254
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 24..52
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 63..80
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2YEV"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 89..99
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 107..126
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2YEV"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 153..180
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 193..208
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 210..225
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 251..272
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 308..320
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 322..336
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 345..368
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 370..376
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:2YEV"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 394..410
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 416..442
FT /evidence="ECO:0007829|PDB:2YEV"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:2YEV"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 459..490
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:2YEV"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 546..548
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 557..574
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 580..597
FT /evidence="ECO:0007829|PDB:2YEV"
FT STRAND 611..614
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 616..644
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 657..683
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 686..715
FT /evidence="ECO:0007829|PDB:2YEV"
FT TURN 720..722
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 724..756
FT /evidence="ECO:0007829|PDB:2YEV"
FT HELIX 765..788
FT /evidence="ECO:0007829|PDB:2YEV"
SQ SEQUENCE 791 AA; 89214 MW; F4DCF3E8AFF07606 CRC64;
MAITAKPKAG VWAVLWDLLT TVDHKKIGLM YTATAFFAFA LAGVFSLLIR TQLAVPNNQF
LTGEQYNQIL TLHGATMLFF FIIQAGLTGF GNFVVPLMLG ARDVALPRVN AFSYWAFLGA
IVLALMSYFF PGGAPSVGWT FYYPFSAQSE SGVDFYLAAI LLLGFSSLLG NANFVATIYN
LRAQGMSLWK MPIYVWSVFA ASVLNLFSLA GLTAATLLVL LERKIGLSWF NPAVGGDPVL
FQQFFWFYSH PTVYVMLLPY LGILAEVAST FARKPLFGYR QMVWAQMGIV VLGTMVWAHH
MFTVGESTLF QIAFAFFTAL IAVPTGVKLF NIIGTLWGGK LQMKTPLYWV LGFIFNFLLG
GITGVMLSMT PLDYQFHDSY FVVAHFHNVL MAGSGFGAFA GLYYWWPKMT GRMYDERLGR
LHFWLFLVGY LLTFLPQYAL GYLGMPRRYY TYNADIAGWP ELNLLSTIGA YILGLGGLVW
IYTMWKSLRS GPKAPDNPWG GYTLEWLTAS PPKAHNFDVK LPTEFPSERP LYDWKKKGVE
LKPEDPAHIH LPNSSFWPFY SAATLFAFFV AVAALPVPNV WMWVFLALFA YGLVRWALED
EYSHPVEHHT VTGKSNAWMG MAWFIVSEVG LFAILIAGYL YLRLSGAATP PEERPALWLA
LLNTFLLVSS SFTVHFAHHD LRRGRFNPFR FGLLVTIILG VLFFLVQSWE FYQFYHHSSW
QENLWTAAFF TIVGLHGLHV VIGGFGLILA YLQALRGKIT LHNHGTLEAA SMYWHLVDAV
WLVIVTIFYV W
