ID F6CZ11_MARPP Unreviewed; 659 AA.
AC F6CZ11;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=Mar181_0069 {ECO:0000313|EMBL:AEF53138.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF53138.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF53138.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(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; CP002771; AEF53138.1; -; Genomic_DNA.
DR RefSeq; WP_013794615.1; NC_015559.1.
DR AlphaFoldDB; F6CZ11; -.
DR STRING; 491952.Mar181_0069; -.
DR KEGG; mpc:Mar181_0069; -.
DR eggNOG; COG0843; Bacteria.
DR HOGENOM; CLU_011899_7_1_6; -.
DR OrthoDB; 9803294at2; -.
DR Proteomes; UP000009230; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 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 18..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 59..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 417..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 587..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..561
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 659 AA; 73311 MW; 908AF08D2C7388B5 CRC64;
MSGFLGKLSM EAIPHDPIVI TTLCVVAVVA CVVAFLVLKN NLLGVLWRDW LTSVDHKKLG
IMYIVLALIM LLRGFADAIM MRLQLALATS GDPGYLPPHH YDQIFTAHGV IMIIFMAMPF
MIGLMNIVVP LQIGARDVAF PFLNNLSFWL AASGAILVNI SLGLGEFAKT GWVAYPPLAG
LEYSPGVGVD YYIWALQISG IGTTLTAVNF LATVFKMRTP GMKLMDMPIF TWTCTWANIL
IAASFPILTA VLAMLTLDRY LDFHFFTNDG GGNSMMYINL FWAWGHPEVY ILVLPAFGIF
SEVVSTFTGK RLFGYKSMVW ATASISILGF IVWLHHFFTM GSSANVNAFF GVMTMIIAVP
TGVKLFNWLF TMYRGRLRMT VPVLWTLGFM VTFTIGGMTG VLLAVPGADY VLHNSLFLIA
HFHNTIIGGA VFGYLAGFAF WFPKAMGFHL NVKLGKAAFW CWLVGFFLAF MPLYVLGFLG
MTRRLNHTDN PDWNIWLYIA LVGAVVIFAG IGCQLLQLFV SFRDRKQNLD TTGDPWDGHT
LEWSTSSPPQ YYNFAELPVV SDIDAFTDMK EKGTAYQRKA SYAPIHMPKN TSAGIIIGGL
ITAFGFAMIW HIWWLAILGF AGSIVTFIIR AYTKDVDYYV QPDEIAQIEN EHLDNVAKG
//