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Database: UniProt
Entry: A0A3M8SVN1_9GAMM
LinkDB: A0A3M8SVN1_9GAMM
Original site: A0A3M8SVN1_9GAMM 
ID   A0A3M8SVN1_9GAMM        Unreviewed;       538 AA.
AC   A0A3M8SVN1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE            EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN   Name=ctaD {ECO:0000313|EMBL:RNF82910.1};
GN   ORFNames=EER27_13490 {ECO:0000313|EMBL:RNF82910.1};
OS   Lysobacter psychrotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1327343 {ECO:0000313|EMBL:RNF82910.1, ECO:0000313|Proteomes:UP000267049};
RN   [1] {ECO:0000313|EMBL:RNF82910.1, ECO:0000313|Proteomes:UP000267049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZS60 {ECO:0000313|EMBL:RNF82910.1,
RC   ECO:0000313|Proteomes:UP000267049};
RA   Luo Y., Sheng H.;
RT   "Lysobacter cryohumiis sp. nov., isolated from soil in the Tianshan
RT   Mountains, Xinjiang, China.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-3
CC       form the functional core of the enzyme complex. CO I is the catalytic
CC       subunit of the enzyme. Electrons originating in cytochrome c are
CC       transferred via the copper A center of subunit 2 and heme A of subunit
CC       1 to the bimetallic center formed by heme A3 and copper B.
CC       {ECO:0000256|RuleBase:RU363061}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC         [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC         Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=7.1.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00029368,
CC         ECO:0000256|RuleBase:RU363061};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU363061}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363061};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU363061}. Membrane
CC       {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:RNF82910.1}.
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DR   EMBL; RIBS01000006; RNF82910.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8SVN1; -.
DR   OrthoDB; 9803294at2; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000267049; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01663; Cyt_c_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; IPR033944; Cyt_c_oxase_su1_dom.
DR   InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR   NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF18; 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|RuleBase:RU363061};
KW   Copper {ECO:0000256|RuleBase:RU363061};
KW   Electron transport {ECO:0000256|RuleBase:RU000370};
KW   Heme {ECO:0000256|RuleBase:RU000370}; Iron {ECO:0000256|RuleBase:RU363061};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363061};
KW   Metal-binding {ECO:0000256|RuleBase:RU363061};
KW   Oxidoreductase {ECO:0000313|EMBL:RNF82910.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267049};
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:RU363061}; Transport {ECO:0000256|RuleBase:RU000370}.
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        75..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        117..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        158..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        198..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        245..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        281..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        317..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        351..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        387..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        423..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   TRANSMEM        464..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU363061"
FT   DOMAIN          24..527
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   538 AA;  60266 MW;  094F0663A8791954 CRC64;
     MAVSPAADHY HDDHAHKQGF IERWFFSTNH KDIGTLYLIF SFVMFVIGAG MSVIIRTELA
     HPGLQHVSPE FFNQMTSMHA LVMIFGGVMP AFVGLANWMI PLQIGAPDMA LPRMNNWSFW
     ILPFAFSLLL VTLFLPGGGP AGGWTLYPPL SLQGGSNVAF TIFAIHMMGI SSIMGAINVI
     ATILNMRAPG IDLLKMPIFC WTWLITAFLL IAVMPVLAGA VTMLLTDKFF ATSFFNAAGG
     GDPVMYQHIF WFFGHPEVYI MILPAFGIVS EIIPTFSRKP LFGYQAMVYA TAAIAFLSFI
     VWAHHMFTVG MPLGGEIYFM FATMLISIPT GVKVFNWVTT MWRGSITFES PMLWAIAFVI
     LFTIGGFSGL MLAIVPADFQ YHDTYFVVAH FHYVLVTGAL FGIIASVYYW WPKWTGRMYN
     ETWAKFHFWW TMLFVNLLFF PQHFLGLAGM PRRIPDYNVV FADWNLVSSI GAFGMFLTPF
     MMAAILIHSK KYGAKAEARA WEGAKGLEWT LPSPAPHHTF TTPPVIRDGD LAHGDISH
//
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