ID S2KL81_HALAF Unreviewed; 675 AA.
AC S2KL81;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=L861_10140 {ECO:0000313|EMBL:EPC02695.1};
OS Halomonas anticariensis (strain DSM 16096 / CECT 5854 / LMG 22089 / FP35).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1121939 {ECO:0000313|EMBL:EPC02695.1, ECO:0000313|Proteomes:UP000014463};
RN [1] {ECO:0000313|EMBL:EPC02695.1, ECO:0000313|Proteomes:UP000014463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16096 / CECT 5854 / LMG 22089 / FP35
RC {ECO:0000313|Proteomes:UP000014463};
RX PubMed=23868129; DOI=10.1128/genomeA.00497-13;
RA Tahrioui A., Quesada E., Llamas I.;
RT "Draft genome sequence of the moderately halophilic gammaproteobacterium
RT Halomonas anticariensis FP35.";
RL Genome Announc. 1:31-31(2013).
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:EPC02695.1}.
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DR EMBL; ASTJ01000024; EPC02695.1; -; Genomic_DNA.
DR RefSeq; WP_016416631.1; NZ_KE332388.1.
DR AlphaFoldDB; S2KL81; -.
DR STRING; 1121939.L861_10140; -.
DR PATRIC; fig|1121939.11.peg.2126; -.
DR eggNOG; COG0843; Bacteria.
DR OrthoDB; 9803294at2; -.
DR Proteomes; UP000014463; 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 Reference proteome {ECO:0000313|Proteomes:UP000014463};
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 233..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..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..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 491..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..627
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 675 AA; 76141 MW; 899ACD30B93DC0CA CRC64;
MFGKLSLEAI PYHEPILVAV GIVAAIGGLA LFGALTYFRK WNWLWSEWFT SVDHKKLGIM
YFIVALVMLL RGFADAIMMR TQLAMASAGS AGYLPPEHYD QIFTAHGVIM IFFVAMPMVI
GLMNLVVPLQ IGARDVAFPF LNNLSFWLFV AGALLVNISL FVGEFAKTGW LAYAPLSGIE
YSPGVGVDYW IWALQISGIG TTLTGINFFV TILKMRTKGM TLFRMPIFTW TSLCANVLII
ASFPILTVTI ALLTLDRYLG MHFFTNDFGG NMMMYVNLIW AWGHPEVYIL ILPAFGVFSE
VIATFARKRL FGYNTMVWAT VCITLLSFIV WLHHFFTMGA GANVNAFFGI MTMIIAIPTG
VKVFNWLFTM YRGSLELSSP VLWTLGFIIT FTLGGMTGVM LAVPAANFVL HNSLFVIAHF
HNVIIGGVVF GMLAGLTYWF PKAFGFKLDE KWGKRSFWCW LVGFYLAFMP LYVLSFFGAV
RRMQSYENPE WQSWMILAWV GAVIIMLGIA CTVIQFYVSI RDRRKYADVT GDPWDGRTLE
WATSSPAPFY NFAHLPQVES VDCFWEQKQQ GIATVSKGPY QDIHMPKNTV AGPIISLFAL
IMGFALVWHI WWLAIVGAAG TFISFLARIF NEDVDYYVPA AEVERIELEH QQRLKLHEQQ
PEDESVLNTR FGVQV
//
