COX1A_PARDE
ID COX1A_PARDE Reviewed; 554 AA.
AC P08305;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Cytochrome c oxidase subunit 1-alpha;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 1-alpha;
DE AltName: Full=Cytochrome c oxidase polypeptide I-alpha;
GN Name=ctaDI; Synonyms=coi;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S1657;
RX PubMed=16453796; DOI=10.1002/j.1460-2075.1987.tb02579.x;
RA Raitio M., Jalli T., Saraste M.;
RT "Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus
RT denitrificans.";
RL EMBO J. 6:2825-2833(1987).
CC -!- FUNCTION: Subunit I and II form the functional core of the enzyme
CC complex. Electrons originating in cytochrome c are transferred via heme
CC a and Cu(A) to the binuclear center formed by heme a3 and Cu(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 -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; X05829; CAA29274.1; -; Genomic_DNA.
DR PIR; S03809; S03809.
DR AlphaFoldDB; P08305; -.
DR SMR; P08305; -.
DR UniPathway; UPA00705; -.
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: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 PANTHER; PTHR10422; PTHR10422; 1.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Copper; Disulfide bond;
KW Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron;
KW Membrane; Metal-binding; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Cytochrome c oxidase subunit 1-alpha"
FT /id="PRO_0000183455"
FT TRANSMEM 26..56
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 81..118
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 175..203
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 215..248
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 260..295
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 301..319
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 331..359
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 367..390
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 399..425
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 436..463
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 478..508
FT /note="Helical"
FT /evidence="ECO:0000250"
FT BINDING 91
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:0000250"
FT BINDING 273
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 322
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 323
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 406
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:0000250"
FT BINDING 408
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:0000250"
FT DISULFID 63..77
FT /evidence="ECO:0000250"
FT CROSSLNK 273..277
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 554 AA; 62013 MW; 58AD591FBBDCE794 CRC64;
MSAQISDSIE EKRGFFTRWF MSTNHKDIGV LYLFTAGLAG LISVTLTVYM RMELQHPGVQ
YMCLEGMRLV ADAAAECTPN AHLWNVVVTY HGILMMFFVV IPALFGGFGN YFMPLHIGAP
DMAFPRLNNL SYWLYVCGVS LAIASLLSPG GSDQPGAGVG WVLYPPLSTT EAGYAMDLAI
FAVHVSGATS ILGAINIITT FLNMRAPGMT LFKVPLFAWA VFITAWMILL SLPVLAGGIT
MLLMDRNFGT QFFDPAGGGD PVLYQHILWF FGHPEVYMLI LPGFGIISHV ISTFARKPIF
GYLPMVLAMA AIAFLGFIVW AHHMYTAGMS LTQQTYFQMA TMTIAVPTGI KVFSWIATMW
GGSIEFKTPM LWALAFLFTV GGVTGVVIAQ GSLDRVYHDT YYIVAHFHYV MSLGALFAIF
AGTYYWIGKM SGRQYPEWAG QLHFWMMFIG SNLIFFPQHF LGRQGMPRRY IDYPVEFSYW
NNISSIGAYI SFASFLFFIG IVFYTLFAGK PVNVPNYWNE HADTLEWTLP SPPPEHTFET
LPKPEDWDRA QAHR
