CYOB_PSEPU
ID CYOB_PSEPU Reviewed; 672 AA.
AC Q9WWR2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IH-2000;
RX PubMed=9868765; DOI=10.1111/j.1574-6968.1998.tb13321.x;
RA Hirayama H., Takami H., Inoue A., Horikoshi K.;
RT "Isolation and characterization of toluene-sensitive mutants from
RT Pseudomonas putida IH-2000.";
RL FEMS Microbiol. Lett. 169:219-225(1998).
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 inner membrane {ECO:0000250}; Multi-pass
CC membrane 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; AB016787; BAA76357.1; -; Genomic_DNA.
DR RefSeq; WP_013970980.1; NZ_RJAI01000064.1.
DR AlphaFoldDB; Q9WWR2; -.
DR SMR; Q9WWR2; -.
DR STRING; 1240350.AMZE01000009_gene4205; -.
DR GeneID; 58529242; -.
DR eggNOG; COG0843; Bacteria.
DR OrthoDB; 316745at2; -.
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 inner membrane; 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..672
FT /note="Cytochrome bo(3) ubiquinol oxidase subunit 1"
FT /id="PRO_0000183482"
FT TOPO_DOM 1..14
FT /note="Periplasmic"
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..101
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..189
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..277
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..346
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..413
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..493
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..672
FT /note="Periplasmic"
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 98
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 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:0000250"
FT BINDING 284
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 288
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 333
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 419
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 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:0000250"
FT CROSSLNK 284..288
FT /note="1'-histidyl-3'-tyrosine (His-Tyr)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 672 AA; 74394 MW; D9DEC872AD3CADF8 CRC64;
MFGKLSLEAI PYHEPIVMVT LAMIALGGIA VVGAITYFRK WTYLWSEWLT TVDHKKIGVM
YIIVAMVMLL RGFADAIMMR TQLAAATGGS EGYLPPEHYD QIFTAHGVIM IIFMAMPFFT
GLMNLAVPLQ IGARDVAFPF LNSLSFYLLL AGVLLVNISL GVGEFAKTGW VAYPPLAGIQ
YSPGVGVDYY IWALQLSGLG TTLTGVNFLV TVMKMRAPGM KLMDMPIFTW TCTWANVLIV
ASFPILTAAL ALLTVDRYLD FHIFTNELGG NPMMYVNLFW AWGHPEVYIL ILPAFGVFSE
VTSTFAGKRL FGHHSMIYAS GAIAVLGFAV WLHHFFTMGA GASVNTFFGL ATMLISIPTG
VKLFNWLFTI YQGRLRFTAP IMWTLGFMIT FSIGGMTGVL LAVPGADFVL HNSLFVIAHF
HNVIIGGAVF GYIAGFAYWF PKAFGFTLNE KWGKAAFWFW ISGFYVAFMP LYALGFMGMT
RRLNHSDNPL WEPYLYVAVV GAVLILFGIA CQLIQLYVSV RDRNQNLDVT GDPWGGRTLE
WSTSSPPPFY NFAHMPEKVG LDAWHEAKEA GVAYKPAAKY EAIHMPSNTS TGLFMGLFLT
VFGFAFIWHI WWLVGASLVA TIAVFVRHAA RDDQGYMVPA EEVARIEGER MKALAKAGAL
PAGARVESFE RV
