CYOB_BUCBP
ID CYOB_BUCBP Reviewed; 659 AA.
AC Q89AA4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1;
DE EC=7.1.1.3 {ECO:0000250|UniProtKB:P0ABI8};
DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 1;
DE Short=Cytochrome o subunit 1;
DE AltName: Full=Oxidase bo(3) subunit 1;
DE AltName: Full=Ubiquinol oxidase polypeptide I;
DE AltName: Full=Ubiquinol oxidase subunit 1;
GN Name=cyoB; OrderedLocusNames=bbp_416;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC -!- FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component
CC of the aerobic respiratory chain of E.coli that predominates when cells
CC are grown at high aeration. Has proton pump activity across the
CC membrane in addition to electron transfer, pumping 2 protons/electron
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a ubiquinol + n H(+)(in) + O2 = 2 a ubiquinone + n H(+)(out)
CC + 2 H2O; Xref=Rhea:RHEA:30251, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=7.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:P0ABI8};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 1 copper B ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 1 low-spin heme b per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme o; Xref=ChEBI:CHEBI:24480; Evidence={ECO:0000250};
CC Note=Binds 1 high-spin heme o per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=a quinone; Xref=ChEBI:CHEBI:132124; Evidence={ECO:0000250};
CC Note=Binds 1 high-affinity quinone that appears to function as a
CC tightly bound cofactor (QH), forming a semiquinone intermediate in the
CC reaction. {ECO:0000250};
CC -!- SUBUNIT: Heterooctamer of two A chains, two B chains, two C chains and
CC two D chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquinol oxidase catalyzes the terminal step in the
CC electron transport chain.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000305}.
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DR EMBL; AE016826; AAO27126.1; -; Genomic_DNA.
DR RefSeq; WP_011091527.1; NC_004545.1.
DR AlphaFoldDB; Q89AA4; -.
DR SMR; Q89AA4; -.
DR STRING; 224915.bbp_416; -.
DR EnsemblBacteria; AAO27126; AAO27126; bbp_416.
DR GeneID; 56470951; -.
DR KEGG; bab:bbp_416; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_1_6; -.
DR OMA; FWGKMSF; -.
DR OrthoDB; 316745at2; -.
DR Proteomes; UP000000601; 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:0009486; F:cytochrome bo3 ubiquinol oxidase activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Hydrogen ion transport;
KW Ion transport; Iron; Membrane; Metal-binding; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..659
FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 1"
FT /id="PRO_0000183481"
FT TOPO_DOM 1..14
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..350
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 372..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..499
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 500..520
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 521..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 71
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
FT BINDING 109
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:0000250"
FT BINDING 287
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 291
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 336
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="Fe(II)-heme o"
FT /ligand_id="ChEBI:CHEBI:60530"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT BINDING 424
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:0000250"
FT CROSSLNK 287..291
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 659 AA; 75583 MW; 13DD8E19D4F5FC15 CRC64;
MFGKLSLNSI PYHDPIIMIT CCVVILVFLV ISIIITIAQK WQYLWNEWCC TVDHKKIAKM
YIFLAFIMLF RGFADAIMMR MQQFLVSSYH GNGTGFLPPH HYDQIFTAHG VIMIFFVAMP
LVIGLMNFVV PLQIGSRDVA FPFLNNLSLW LTIFSALLMN VSLGIGEFAQ TGWLAYPPLS
ELQYSPGVGV DYWIWSLQIS GIGTTLTAIN FLVTIIKMRS SGMNWFKIPV FTWTSFCTNI
LIIASFPVLT VSLLLLTLDR YLGFHFFTND FGGNMMMYVN LIWIWGHPEV YILILPVFGI
FSEVVATFSS KELFGYTSLI WATIVITILS FIVWLHHFFT MGASANVNAF FGITTMIISI
PTGVKIFNWL FTMYRGNVRI NSIMLWTIGF LITFSIGGMA GVLLSLPVID FSLHNSLFLV
AHFHNVIIGG VVFGCFAGIT YWFPKLFGFM LSEKWGKRAF WCWFFGFFCA FMPLYALGLM
GMTRRLSQNI NPQFHSMLTI AALGTILIFI GIVFQIIQIF VSIRDRNLNR DCSGDPWNGR
TLEWSTTSPP PFYNFAVLPI VQFRDSFWES KKSFKSNKLP ILYTSFHMPK NTKFGFLIGF
FAFLLGFSAV WYIFWLFFIS FFVIIYLLVI KSLDTNCDYI ISIEEIKEIE KCINIKKMD
