ID M9LH18_PAEPP Unreviewed; 647 AA.
AC M9LH18;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Quinol oxidase subunit 1 {ECO:0000256|RuleBase:RU367144};
DE EC=1.10.3.- {ECO:0000256|RuleBase:RU367144};
GN ORFNames=PPOP_1362 {ECO:0000313|EMBL:GAC42005.1};
OS Paenibacillus popilliae ATCC 14706.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1212764 {ECO:0000313|EMBL:GAC42005.1, ECO:0000313|Proteomes:UP000029453};
RN [1] {ECO:0000313|EMBL:GAC42005.1, ECO:0000313|Proteomes:UP000029453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14706 {ECO:0000313|EMBL:GAC42005.1,
RC ECO:0000313|Proteomes:UP000029453};
RA Iiyama K., Mori K., Mon H., Chieda Y., Lee J.M., Kusakabe T., Tashiro K.,
RA Asano S., Yasunaga-Aoki C., Shimizu S.;
RT "Draft Genome Sequence of Paenibacillus popilliae ATCC 14706T.";
RL Submitted (OCT-2012) 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:GAC42005.1}.
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DR EMBL; BALG01000064; GAC42005.1; -; Genomic_DNA.
DR RefSeq; WP_006285391.1; NZ_BALG01000064.1.
DR AlphaFoldDB; M9LH18; -.
DR OrthoDB; 9759913at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000029453; 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:UP000029453};
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..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 224..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..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 446..469
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367144"
FT TRANSMEM 489..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; 73282 MW; F36436CDA9BDC482 CRC64;
MKWDEFFVTG EPMIYGAMAS IVIASLAIVI GLTYFKKWGY LWREWLTTVD HKRIGVMYII
AAHVMLFRGG VDALLMRTQL AAPGMKFLDA QHYNEIFTTH GVIMILFMAM PFIIGLINVV
IPLQIGARDV AFPRLNAVSF WLFFSGAMLF NISFVIGGSP DAGWTAYFPL ASVEFSPTVG
MNYYSIALQI AGIGTLMTGV NFIVTILKMR APGMTLMRMP MFTWSVLITC IIILFAFPVL
TVALALMMFD RMFGSQFFTM ANGGMDMLWA NLFWVWGHPE VYIVILPAFG IYSEIISTFS
RKNLYGYKSM VVSMVAISLL SFIVWAHHFY TMGHGAMVNG FFSVTTMAIA VPTGVKIFNW
LFTLQKGKIQ FTTPMLYTLA FIPIFTIGGV TGVMLAMASA DYQYHNTMFL VAHFHYVLIP
GTVFAVIAGM YYWFPKLFGF RLNERLGKIS FWFIAICFNI TFLPLFFLGL NGMTRRMYTY
SAETGFGPLN LIATIGAFGL AFGFAILVYN IYWSARYAPR DKTGDPWDAR TLEWSTHSPV
PEYNFAVIPN VKSLDAFWFW KKDKQPLYEG KIEEIHMPNN SGQPFILGVI FFFLGFFLVF
GWWIPAIIAG LGVLIMLAVR SFERDHGHHI PVKTIQDTEQ RLRGEQA
//