ID A0A2N7QP27_9GAMM Unreviewed; 674 AA.
AC A0A2N7QP27;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Name=cyoB_2 {ECO:0000313|EMBL:PMQ03397.1};
GN ORFNames=DyAD56_19205 {ECO:0000313|EMBL:PMQ03397.1};
OS Dyella sp. AD56.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1528744 {ECO:0000313|EMBL:PMQ03397.1, ECO:0000313|Proteomes:UP000235676};
RN [1] {ECO:0000313|EMBL:PMQ03397.1, ECO:0000313|Proteomes:UP000235676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD56 {ECO:0000313|EMBL:PMQ03397.1,
RC ECO:0000313|Proteomes:UP000235676};
RA Schulz-Bohm K., Janssens T.K., De Jager V., Gawehns F., De Boer W.,
RA Garbeva P.;
RT "Bacterial performance in fungal presence.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PMQ03397.1}.
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DR EMBL; NRDP01000030; PMQ03397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7QP27; -.
DR OrthoDB; 9803294at2; -.
DR Proteomes; UP000235676; Unassembled WGS sequence.
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 Oxidoreductase {ECO:0000313|EMBL:PMQ03397.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235676};
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..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 57..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..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..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..474
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 589..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..630
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 39..559
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 674 AA; 75272 MW; E342822F118C665B CRC64;
MFGKLTLDAV PYHEPIVMGT LVAVILGGLA MLAIITKFRL WGYLWKEWFT SVDHKKIGIM
YIIVALVMLL RGFSDAIMMR MQQAMAAGES AGYLPPHHFD QVFTAHGVIM IFFVAMPFIT
GLMNMVVPLQ IGARDVAYPF LNSLSFWLFM SGVVLVMVSL FVGDFAATGW LAYPPLSGIK
YSPTVGVDYY IWSLQLSGLG TTLSGINFIV TIMKMRAPGM TLMKMPVFTW TALVTNILIV
AAFPILTVTL ALLTADRYLD MHFFTNELGG NAMMYVNMIW IWGHPEVYIL ILPCFGAYSE
IVATFSKKPL FGYKSMVYAT SCIGVLSFVV WLHHFFTMGS GASVNAFFGI TTMIISVPTG
AKLFNWLFTM YRGRVEYNVP MLWTVGFMVT FVIGGVTGVL MAVPGADFVL HNSVFLIAHF
HNVIIGGVVF GVFAAINYWF PKAFGFRLNE FWGKASFWCW LVGFWMAFAP LYVLGLKGMT
RRMNHYANPD WQPFLIVAAL GAAVIAVGIL CTLVQFYVSI RDRKSLTDPS GDPWGGRTLE
WAISSPAPFY NFAIVPQVKE LDQFWEDKQN GVAYVQPAKY EDIHMPRNTG VGVVMGAFGT
VLGFALVWHI WWLAAVGLLG MIGAFIVRAY DRDIDYWVPA AEVEKIERSR HAQLKQFQTT
QVAPVAAPQR QKVA
//
