ID A9MM29_SALAR Unreviewed; 663 AA.
AC A9MM29;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=SARI_02492 {ECO:0000313|EMBL:ABX22351.1};
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX22351.1, ECO:0000313|Proteomes:UP000002084};
RN [1] {ECO:0000313|EMBL:ABX22351.1, ECO:0000313|Proteomes:UP000002084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC {ECO:0000313|Proteomes:UP000002084};
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000880; ABX22351.1; -; Genomic_DNA.
DR AlphaFoldDB; A9MM29; -.
DR STRING; 41514.SARI_02492; -.
DR KEGG; ses:SARI_02492; -.
DR HOGENOM; CLU_011899_7_1_6; -.
DR Proteomes; UP000002084; 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:UP000002084};
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..79
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..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..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 593..626
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 663 AA; 74350 MW; 07C87FD732059E94 CRC64;
MFGKLSLDAV PFHEPIVMVT IAAIIVGGLA ILAAITYFGK WTYLWKEWLT SVDHKRLGIM
YIIVAIVMLL RGFADAIMMR SQQALASAGE AGFLPPHHYD QIFTAHGVIM IFFVAMPFVI
GLMNLVVPLQ IGARDVAFPF LNNLSFWFTV VGVILVNLSL GVGEFAQTGW LAYPPLSGIE
YSPSVGVDYW IWALQLSGIG TTLTGINFFV TILKMRAPGM TMFKMPVFTW ASLCANVLII
ASFPILTVTV ALLTLDRYLG THFFTNDMGG NMMMYINLIW AWGHPEVYIL ILPVFGVFSE
IAATFSRKRL FGYTSLVWAT VCITVLSFIV WLHHFFTMGA GANVNAFFGI TTMIIAIPTG
VKIFNWLFTM YQGRIVFHSA MMWTIGFIVT FSVGGMTGVL LAVPGADFVL HNSLFLIAHF
HNVIIGGVVF GCFAGMTYWW PKAFGFKLNE TWGKRAFWFW IIGFFVAFMP LYVLGFMGMT
RRLSQQIDPQ FHTMLMVAAA GAALIALGIL CQLIQIFVSI RDREQNRDLT GDPWGGRTLE
WSTSSPPPFY NFAVVPHVHE RDAFWEMKEK GEAYQQPGHY EEIHMPKNSG AGIVIAAFAT
VFGFAMIWHI WWLAIVGFAG MIISWIVKSF DEDVDYYVPV RDVEKLENQH FDEITKAGLK
NGN
//
