COX1_THET8
ID COX1_THET8 Reviewed; 562 AA.
AC Q5SJ79;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c ba(3) subunit I;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
DE AltName: Full=Cytochrome cba3 subunit 1;
GN Name=cbaA; OrderedLocusNames=TTHA1135;
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=7657607; DOI=10.1074/jbc.270.35.20345;
RA Keightley J.A., Zimmermann B.H., Mather M.W., Springer P., Pastuszyn A.,
RA Lawrence D.M., Fee J.A.;
RT "Molecular genetic and protein chemical characterization of the cytochrome
RT ba3 from Thermus thermophilus HB8.";
RL J. Biol. Chem. 270:20345-20358(1995).
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=10775261; DOI=10.1093/emboj/19.8.1766;
RA Soulimane T., Buse G., Bourenkov G.P., Bartunik H.D., Huber R., Than M.E.;
RT "Structure and mechanism of the aberrant ba3-cytochrome c oxidase from
RT Thermus thermophilus.";
RL EMBO J. 19:1766-1776(2000).
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=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=Binds 2 heme groups. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds a copper B center. {ECO:0000250};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; L09121; AAB00370.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70958.1; -; Genomic_DNA.
DR RefSeq; WP_011173204.1; NC_006461.1.
DR RefSeq; YP_144401.1; NC_006461.1.
DR PDB; 1EHK; X-ray; 2.40 A; A=1-562.
DR PDB; 2QPD; X-ray; 3.25 A; A=2-562.
DR PDB; 2QPE; X-ray; 2.90 A; A=2-562.
DR PDB; 3BVD; X-ray; 3.37 A; A=2-562.
DR PDB; 3EH3; X-ray; 3.10 A; A=2-562.
DR PDB; 3EH4; X-ray; 2.90 A; A=2-562.
DR PDB; 3EH5; X-ray; 2.80 A; A=2-562.
DR PDB; 3QJQ; X-ray; 2.90 A; A=2-562.
DR PDB; 3QJR; X-ray; 3.20 A; A=2-562.
DR PDB; 3QJS; X-ray; 2.80 A; A=2-562.
DR PDB; 3QJT; X-ray; 2.95 A; A=2-562.
DR PDB; 3QJU; X-ray; 2.90 A; A=2-562.
DR PDB; 3QJV; X-ray; 2.80 A; A=2-562.
DR PDB; 3S33; X-ray; 4.45 A; A=2-562.
DR PDB; 3S38; X-ray; 4.20 A; A=2-562.
DR PDB; 3S39; X-ray; 4.80 A; A=2-562.
DR PDB; 3S3A; X-ray; 4.25 A; A=2-562.
DR PDB; 3S3B; X-ray; 3.30 A; A=2-562.
DR PDB; 3S3C; X-ray; 4.00 A; A=2-562.
DR PDB; 3S3D; X-ray; 3.75 A; A=2-562.
DR PDB; 3S8F; X-ray; 1.80 A; A=2-562.
DR PDB; 3S8G; X-ray; 1.80 A; A=2-562.
DR PDB; 4FA7; X-ray; 2.50 A; A=2-562.
DR PDB; 4FAA; X-ray; 2.80 A; A=2-562.
DR PDB; 4G70; X-ray; 2.60 A; A=2-562.
DR PDB; 4G71; X-ray; 2.90 A; A=2-562.
DR PDB; 4G72; X-ray; 3.19 A; A=2-562.
DR PDB; 4G7Q; X-ray; 2.60 A; A=2-562.
DR PDB; 4G7R; X-ray; 3.05 A; A=2-562.
DR PDB; 4G7S; X-ray; 2.00 A; A=2-562.
DR PDB; 4GP4; X-ray; 2.80 A; A=2-562.
DR PDB; 4GP5; X-ray; 2.70 A; A=2-562.
DR PDB; 4GP8; X-ray; 2.80 A; A=2-562.
DR PDB; 4N4Y; X-ray; 2.90 A; A=2-562.
DR PDB; 5NDC; X-ray; 2.30 A; A=2-562.
DR PDBsum; 1EHK; -.
DR PDBsum; 2QPD; -.
DR PDBsum; 2QPE; -.
DR PDBsum; 3BVD; -.
DR PDBsum; 3EH3; -.
DR PDBsum; 3EH4; -.
DR PDBsum; 3EH5; -.
DR PDBsum; 3QJQ; -.
DR PDBsum; 3QJR; -.
DR PDBsum; 3QJS; -.
DR PDBsum; 3QJT; -.
DR PDBsum; 3QJU; -.
DR PDBsum; 3QJV; -.
DR PDBsum; 3S33; -.
DR PDBsum; 3S38; -.
DR PDBsum; 3S39; -.
DR PDBsum; 3S3A; -.
DR PDBsum; 3S3B; -.
DR PDBsum; 3S3C; -.
DR PDBsum; 3S3D; -.
DR PDBsum; 3S8F; -.
DR PDBsum; 3S8G; -.
DR PDBsum; 4FA7; -.
DR PDBsum; 4FAA; -.
DR PDBsum; 4G70; -.
DR PDBsum; 4G71; -.
DR PDBsum; 4G72; -.
DR PDBsum; 4G7Q; -.
DR PDBsum; 4G7R; -.
DR PDBsum; 4G7S; -.
DR PDBsum; 4GP4; -.
DR PDBsum; 4GP5; -.
DR PDBsum; 4GP8; -.
DR PDBsum; 4N4Y; -.
DR PDBsum; 5NDC; -.
DR AlphaFoldDB; Q5SJ79; -.
DR SMR; Q5SJ79; -.
DR STRING; 300852.55772517; -.
DR DrugBank; DB02451; B-nonylglucoside.
DR TCDB; 3.D.4.2.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR EnsemblBacteria; BAD70958; BAD70958; BAD70958.
DR GeneID; 3168993; -.
DR KEGG; ttj:TTHA1135; -.
DR PATRIC; fig|300852.9.peg.1114; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_033807_1_0_0; -.
DR OMA; VVYFWLM; -.
DR PhylomeDB; Q5SJ79; -.
DR BioCyc; MetaCyc:MON-21000; -.
DR BRENDA; 7.1.1.9; 2305.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; Q5SJ79; -.
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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR CDD; cd01660; ba3-like_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 1.
DR InterPro; IPR033943; Ba3-like_Oxidase_I.
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 Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 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..562
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183462"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 72
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 233
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 237
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT BINDING 282
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 283
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 384
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 386
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 233..237
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 16..36
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 38..45
FT /evidence="ECO:0007829|PDB:3S8F"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 79..97
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 103..125
FT /evidence="ECO:0007829|PDB:3S8F"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:3EH3"
FT HELIX 143..173
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 181..206
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 234..249
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 251..254
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:3S8F"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4G70"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5NDC"
FT HELIX 292..326
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 344..366
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 372..375
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3EH3"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:3S8F"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 392..399
FT /evidence="ECO:0007829|PDB:3S8F"
FT TURN 400..403
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 404..409
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 415..444
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:3QJU"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 464..492
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:3EH5"
FT HELIX 499..503
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 520..524
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 527..550
FT /evidence="ECO:0007829|PDB:3S8F"
SQ SEQUENCE 562 AA; 62528 MW; 769B9E2F2033617B CRC64;
MAVRASEISR VYEAYPEKKA TLYFLVLGFL ALIVGSLFGP FQALNYGNVD AYPLLKRLLP
FVQSYYQGLT LHGVLNAIVF TQLFAQAIMV YLPARELNMR PNMGLMWLSW WMAFIGLVVA
ALPLLANEAT VLYTFYPPLK GHWAFYLGAS VFVLSTWVSI YIVLDLWRRW KAANPGKVTP
LVTYMAVVFW LMWFLASLGL VLEAVLFLLP WSFGLVEGVD PLVARTLFWW TGHPIVYFWL
LPAYAIIYTI LPKQAGGKLV SDPMARLAFL LFLLLSTPVG FHHQFADPGI DPTWKMIHSV
LTLFVAVPSL MTAFTVAASL EFAGRLRGGR GLFGWIRALP WDNPAFVAPV LGLLGFIPGG
AGGIVNASFT LDYVVHNTAW VPGHFHLQVA SLVTLTAMGS LYWLLPNLTG KPISDAQRRL
GLAVVWLWFL GMMIMAVGLH WAGLLNVPRR AYIAQVPDAY PHAAVPMVFN VLAGIVLLVA
LLLFIYGLFS VLLSRERKPE LAEAPLPFAE VISGPEDRRL VLAMDRIGFW FAVAAILVVL
AYGPTLVQLF GHLNPVPGWR LW
