QOX1_ACEAC
ID QOX1_ACEAC Reviewed; 664 AA.
AC P98009;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Ubiquinol oxidase subunit 1;
DE EC=1.10.3.-;
DE AltName: Full=Cytochrome A1 subunit 1;
DE AltName: Full=Oxidase BA(3) subunit 1;
DE AltName: Full=Ubiquinol oxidase polypeptide I;
GN Name=cyaA;
OS Acetobacter aceti.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter; Acetobacter subgen. Acetobacter.
OX NCBI_TaxID=435;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-32.
RC STRAIN=1023;
RX PubMed=8392509; DOI=10.1128/jb.175.14.4307-4314.1993;
RA Fukaya M., Tayama K., Tamaki T., Ebisuya H., Okumura H., Kawamura Y.,
RA Horinouchi S., Beppu T.;
RT "Characterization of a cytochrome a1 that functions as a ubiquinol oxidase
RT in Acetobacter aceti.";
RL J. Bacteriol. 175:4307-4314(1993).
CC -!- FUNCTION: Catalytic subunit of the enzyme. Electrons originating in a
CC quinol are transferred to the bimetallic center formed by heme a and
CC copper B.
CC -!- SUBUNIT: Heterotetramer of the subunits 1, 2, 3 and 4.
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; D13185; BAA02481.1; -; Genomic_DNA.
DR PIR; B36885; B36885.
DR AlphaFoldDB; P98009; -.
DR SMR; P98009; -.
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:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro.
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; IPR014207; Cyt_c_ubiqinol_oxidase_su1.
DR PANTHER; PTHR10422; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 1.
DR TIGRFAMs; TIGR02843; CyoB; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Copper; Direct protein sequencing; Electron transport; Heme;
KW Iron; Membrane; Metal-binding; Oxidoreductase; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..664
FT /note="Ubiquinol oxidase subunit 1"
FT /id="PRO_0000006036"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 106
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
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="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 421
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
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"
SQ SEQUENCE 664 AA; 74364 MW; 454929C42BB9B29B CRC64;
MLGRLSLSAI PLDVPILVGT FIGVVIVGVA VLGLITYYGK WGYLWKEWFT SVDHKRLAAM
YIILALVALF RGFADAIMMR TQLALAYAGN PGYLPPHHYD QIFSAHGTIM IFFLAMAFMT
GLFNFIVPLQ IGARDVAFPF LNNLSFWMTA VAFILVNVSL FIGEFSQCGW LAYPPLSENQ
FSPGVGVDYY IWAVQISGVG TLLTGVNFFV TIVKMRAPGM TWRKMPVFTW TALCASILIM
VAFPVLTVAV GLLGMDRYFG MHFFTNDGGG NQMMYLNLIW AWGHPEVYIL VIPAFGVFSE
VVPAFSGKPL FGYSTMVYAT CSIMVLSFLV WVHHFFTMGA GPDVNAFFGI ATMIISIPTG
IKLFNWLFTM YKGRIQFHAC MYWAVGFMIT FTIGGMTGVM LAIPGADFVL HNSLFLIAHF
HNTIIGGVYF GYICGMNFWF PKVMGFKLDE TWGKRAFWFW FVGFYCAFVP LYIVGFEGMT
RRLNHYDNPA WHPWLLVAEV GAVLVMLGIA CQLTQLYVSI RDRNLPQNRD VTGDPWNGRT
LEWSTSSPPP VYNFAIVPHV HELDTFMLDK ENGIDTRQAG AQYEAIHMPK NTSFGSGLCK
CSALIFGFAA VWYIWWLAAV GLVGVIGTVI ARSADKDIDY YIPAEEVARI ENEHTRKLMA
QAAE
