COX1_CERSP
ID COX1_CERSP Reviewed; 566 AA.
AC P33517;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Cytochrome c oxidase subunit 1;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 1;
DE AltName: Full=Cytochrome c oxidase polypeptide I;
GN Name=ctaD;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Ga;
RX PubMed=1313140; DOI=10.1111/j.1365-2958.1992.tb01511.x;
RA Shapleigh J.P., Gennis R.B.;
RT "Cloning, sequencing and deletion from the chromosome of the gene encoding
RT subunit I of the aa3-type cytochrome c oxidase of Rhodobacter
RT sphaeroides.";
RL Mol. Microbiol. 6:635-642(1992).
RN [2]
RP SEQUENCE REVISION TO 436-439 AND 518-521.
RA Shapleigh J.P., Gennis R.B.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- INTERACTION:
CC P33517; Q03736: ctaC; NbExp=3; IntAct=EBI-1034008, EBI-1033998;
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; X62645; CAA44514.2; -; Genomic_DNA.
DR PIR; S20534; S20534.
DR RefSeq; WP_011337048.1; NZ_WSNV01000001.1.
DR PDB; 1M56; X-ray; 2.30 A; A/G=1-566.
DR PDB; 1M57; X-ray; 3.00 A; A/G=1-566.
DR PDB; 2GSM; X-ray; 2.00 A; A/C=1-566.
DR PDB; 3DTU; X-ray; 2.15 A; A/C=1-566.
DR PDB; 3FYE; X-ray; 2.15 A; A/C=1-566.
DR PDB; 3FYI; X-ray; 2.20 A; A/C=1-566.
DR PDB; 5WEH; X-ray; 3.45 A; A/G=1-566.
DR PDB; 6CI0; X-ray; 2.40 A; A/C=17-551.
DR PDBsum; 1M56; -.
DR PDBsum; 1M57; -.
DR PDBsum; 2GSM; -.
DR PDBsum; 3DTU; -.
DR PDBsum; 3FYE; -.
DR PDBsum; 3FYI; -.
DR PDBsum; 5WEH; -.
DR PDBsum; 6CI0; -.
DR AlphaFoldDB; P33517; -.
DR SMR; P33517; -.
DR DIP; DIP-38013N; -.
DR IntAct; P33517; 3.
DR DrugBank; DB03619; Deoxycholic acid.
DR TCDB; 3.D.4.6.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR GeneID; 67445668; -.
DR OMA; WAMMSIG; -.
DR OrthoDB; 316745at2; -.
DR BRENDA; 7.1.1.9; 5383.
DR UniPathway; UPA00705; -.
DR EvolutionaryTrace; P33517; -.
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:0045277; C:respiratory chain complex IV; IEA:InterPro.
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 CDD; cd01663; Cyt_c_Oxidase_I; 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; IPR033944; Cyt_c_oxase_su1_dom.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02891; CtaD_CoxA; 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 Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..566
FT /note="Cytochrome c oxidase subunit 1"
FT /id="PRO_0000183459"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 543..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 102
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 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 288
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 333
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 334
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000305"
FT BINDING 419
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 421
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 284..288
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
FT HELIX 16..20
FT /evidence="ECO:0007829|PDB:3DTU"
FT HELIX 26..55
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 136..156
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1M56"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3DTU"
FT HELIX 186..214
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 227..258
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 272..306
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 327..330
FT /evidence="ECO:0007829|PDB:5WEH"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 342..354
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 379..402
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 414..424
FT /evidence="ECO:0007829|PDB:2GSM"
FT TURN 425..427
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 428..444
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 450..476
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 491..521
FT /evidence="ECO:0007829|PDB:2GSM"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:6CI0"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:2GSM"
FT HELIX 557..559
FT /evidence="ECO:0007829|PDB:1M56"
SQ SEQUENCE 566 AA; 63147 MW; 65A74DBCC5C550B0 CRC64;
MADAAIHGHE HDRRGFFTRW FMSTNHKDIG VLYLFTGGLV GLISVAFTVY MRMELMAPGV
QFMCAEHLES GLVKGFFQSL WPSAVENCTP NGHLWNVMIT GHGILMMFFV VIPALFGGFG
NYFMPLHIGA PDMAFPRMNN LSYWLYVAGT SLAVASLFAP GGNGQLGSGI GWVLYPPLST
SESGYSTDLA IFAVHLSGAS SILGAINMIT TFLNMRAPGM TMHKVPLFAW SIFVTAWLIL
LALPVLAGAI TMLLTDRNFG TTFFQPSGGG DPVLYQHILW FFGHPEVYII VLPAFGIVSH
VIATFAKKPI FGYLPMVYAM VAIGVLGFVV WAHHMYTAGL SLTQQSYFMM ATMVIAVPTG
IKIFSWIATM WGGSIELKTP MLWALGFLFL FTVGGVTGIV LSQASVDRYY HDTYYVVAHF
HYVMSLGAVF GIFAGIYFWI GKMSGRQYPE WAGKLHFWMM FVGANLTFFP QHFLGRQGMP
RRYIDYPEAF ATWNFVSSLG AFLSFASFLF FLGVIFYTLT RGARVTANNY WNEHADTLEW
TLTSPPPEHT FEQLPKREDW ERAPAH
