ID G7UPJ2_PSEUP Unreviewed; 666 AA.
AC G7UPJ2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Cytochrome bo(3) ubiquinol oxidase subunit 1 {ECO:0000256|ARBA:ARBA00014691};
DE EC=7.1.1.3 {ECO:0000256|ARBA:ARBA00012941};
DE AltName: Full=Cytochrome o ubiquinol oxidase subunit 1 {ECO:0000256|ARBA:ARBA00032190};
DE AltName: Full=Oxidase bo(3) subunit 1 {ECO:0000256|ARBA:ARBA00030075};
DE AltName: Full=Ubiquinol oxidase polypeptide I {ECO:0000256|ARBA:ARBA00032435};
DE AltName: Full=Ubiquinol oxidase subunit 1 {ECO:0000256|ARBA:ARBA00031883};
GN OrderedLocusNames=DSC_10805 {ECO:0000313|EMBL:AER56805.1};
OS Pseudoxanthomonas spadix (strain BD-a59).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1045855 {ECO:0000313|EMBL:AER56805.1, ECO:0000313|Proteomes:UP000005870};
RN [1] {ECO:0000313|EMBL:AER56805.1, ECO:0000313|Proteomes:UP000005870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BD-a59 {ECO:0000313|EMBL:AER56805.1,
RC ECO:0000313|Proteomes:UP000005870};
RX PubMed=22207748; DOI=10.1128/JB.06436-11;
RA Lee S.H., Jin H.M., Lee H.J., Kim J.M., Jeon C.O.;
RT "Complete Genome Sequence of the BTEX-Degrading Bacterium Pseudoxanthomonas
RT spadix BD-a59.";
RL J. Bacteriol. 194:544-544(2012).
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:0000256|ARBA:ARBA00001193};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- COFACTOR:
CC Name=Fe(II)-heme o; Xref=ChEBI:CHEBI:60530;
CC Evidence={ECO:0000256|ARBA:ARBA00034455};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
CC -!- SUBUNIT: The cytochrome bo(3) ubiquinol oxidase complex is a
CC heterooctamer of two A chains, two B chains, two C chains and two D
CC chains. {ECO:0000256|ARBA:ARBA00034513}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family.
CC {ECO:0000256|RuleBase:RU000370}.
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DR EMBL; CP003093; AER56805.1; -; Genomic_DNA.
DR RefSeq; WP_014160979.1; NC_016147.2.
DR AlphaFoldDB; G7UPJ2; -.
DR STRING; 1045855.DSC_10805; -.
DR KEGG; psd:DSC_10805; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_1_6; -.
DR OrthoDB; 9803294at2; -.
DR Proteomes; UP000005870; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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: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 CDD; cd01662; Ubiquinol_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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 NCBIfam; TIGR02843; CyoB; 1.
DR PANTHER; PTHR10422:SF35; CYTOCHROME BO(3) UBIQUINOL OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS00077; COX1_CUB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|RuleBase:RU000370};
KW Heme {ECO:0000256|RuleBase:RU000370}; Iron {ECO:0000256|RuleBase:RU000370};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000370};
KW Reference proteome {ECO:0000313|Proteomes:UP000005870};
KW Respiratory chain {ECO:0000256|RuleBase:RU000370};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000370};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000370}.
FT TRANSMEM 16..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 415..440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 452..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 37..559
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 666 AA; 74841 MW; 11831C48A036BB5F CRC64;
MLGKLTLESI PYHEPILIAT AAGVGLAGVL VVALMTYYKK WGWLWREWLT TVDHKKIGVM
YIFVALVMLL RGFADAIMMR MQLAMGHGGN EGFLPPHHYD QIFTAHGVIM IFFMAMPFIT
GLMNLIVPLQ IGARDVAFPF LNSLSFWLFV AGVVLMMLSL FVGEFAQTGW LAFPPLSELQ
YSPGVGVDYY IWALQISGLG TTLTGVNFVA TIFKMRAPGM TLMRMPIFTW TALITNILMI
AAFPFLTISL ALLTADRYLG THFFTNDGGG NAMMYINMIW IWGHPEVYIL ILPCFGVFSE
VVSTFSRKPL FGYTSMVWAT SAIGVLSFIV WLHHFFTMGS GANVNAFFGI TTMIIAVPTG
VKIFNWLFTM FRGRIEMTSM MYWTVGFIVT FTIGGMTGVM MAIPAVSFVL HNSLFLIAHF
HNVIIGGVVF GCLCGLTYWW PKAFGFKLVD KLGKASFWCW IVGFFIAFMP LYVLGFLGMT
RRLNTYNNPE WVPWLYVAAC GAVIIACGIA LNIIQIGWSI WKRNDNRDLT GDPWDGRTLE
WASSSPAPFY NFAHLPKVTG RDQHWADKQA GTAYQRPTHY EDIHMPRNTS IGVFMGAFGV
LLGFGMVWHI WWMAIVGLVG MIGSYIVRTF DEDTDYYVPA AEVARIENAR YDQLDRLRAA
KPQEAV
//
