ID A0A168LT92_9BACL Unreviewed; 647 AA.
AC A0A168LT92;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Quinol oxidase subunit 1 {ECO:0000256|RuleBase:RU367144};
DE EC=1.10.3.- {ECO:0000256|RuleBase:RU367144};
GN ORFNames=PBAT_16365 {ECO:0000313|EMBL:OAB43805.1};
OS Paenibacillus antarcticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=253703 {ECO:0000313|EMBL:OAB43805.1, ECO:0000313|Proteomes:UP000077355};
RN [1] {ECO:0000313|EMBL:OAB43805.1, ECO:0000313|Proteomes:UP000077355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5836 {ECO:0000313|EMBL:OAB43805.1,
RC ECO:0000313|Proteomes:UP000077355};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Paenibacillus antarcticus CECT 5836.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes quinol oxidation with the concomitant reduction of
CC oxygen to water. {ECO:0000256|RuleBase:RU367144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a quinol + O2 = 2 a quinone + 2 H2O; Xref=Rhea:RHEA:55376,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000256|ARBA:ARBA00000725,
CC ECO:0000256|RuleBase:RU367144};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000256|RuleBase:RU367144};
CC Note=Binds a copper B center. {ECO:0000256|RuleBase:RU367144};
CC -!- COFACTOR:
CC Name=ferriheme a; Xref=ChEBI:CHEBI:60532;
CC Evidence={ECO:0000256|RuleBase:RU367144};
CC Note=Heme A3. {ECO:0000256|RuleBase:RU367144};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU367144}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU367144}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU367144}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:OAB43805.1}.
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DR EMBL; LVJI01000024; OAB43805.1; -; Genomic_DNA.
DR RefSeq; WP_068650976.1; NZ_LVJI01000024.1.
DR AlphaFoldDB; A0A168LT92; -.
DR OrthoDB; 9759913at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000077355; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-UniRule.
DR GO; GO:0005507; F:copper ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
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; IPR014233; QoxB.
DR NCBIfam; TIGR02882; QoxB; 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 ECO:0000256|RuleBase:RU367144}; Copper {ECO:0000256|RuleBase:RU367144};
KW Electron transport {ECO:0000256|RuleBase:RU000370};
KW Heme {ECO:0000256|RuleBase:RU000370};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781,
KW ECO:0000256|RuleBase:RU367144};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU367144}; Iron {ECO:0000256|RuleBase:RU367144};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367144};
KW Metal-binding {ECO:0000256|RuleBase:RU367144};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU367144};
KW Reference proteome {ECO:0000313|Proteomes:UP000077355};
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|RuleBase:RU367144}; Transport {ECO:0000256|RuleBase:RU000370}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 96..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 183..207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 227..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 269..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 304..328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 340..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 374..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 450..471
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 491..512
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 585..618
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT DOMAIN 36..552
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 647 AA; 72781 MW; 4E8FAE65A805FC32 CRC64;
MKWDEFFVTG EPMIYGAMAS IVLATIAIIV GLTYFKKWGY LWREWLTTVD HKRIGVMYIL
SALIMLFRGG VDAIMMRFQT AVPENKFLDA QHYNEIFTTH GLIMILFMAM PFIIGIMNVV
VPLQIGARDV AFPRLNAISF WLFFAGAMLL NLSFVIGGSP DAGWSAYFPL ASLEFSPTVG
NNYYSLALQI SGIGTLLTGI NFIVTILKMR APGMKLMRMP MFTWSSLITS VIIAFAFPVL
TVALALMMFD RIFGSQFFTM SNGGMDMLWA NLFWVWGHPE VYIVILPAFG IFSEIIATFS
KKNLYGYTSM VVSMVVISLL SFLVWAHHFY TMGQGAMVNG FFSITTMAIS VPTGVKIFNW
LFTMRKGKIT FTTPMLYSLA FIPIFTIGGV TGVMLAMASA DYQYHNTMFL VAHFHYVLIP
GTVFAVIAGF HYWFPKVFGF KLNERLGKHA FWWIAISFNV TFFPLFFLGL QGMTRRMYTY
SEETGFGPLN LLSFAGALGL AFGFIILVYN IYYSIRYSPR ETNGDPWDAR TLEWATSSPI
PAYNFAITPN VKGRDALWSA KHDNQPIFDG KIEPIHLPSN SGKPVILAGV FFVFGFALVF
SWWIPAIISG IGILIVLATM SFDRDHGITV SVEEIIETEK KLRGETL
//
