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Database: UniProt
Entry: A0A081N5S7_9GAMM
LinkDB: A0A081N5S7_9GAMM
Original site: A0A081N5S7_9GAMM 
ID   A0A081N5S7_9GAMM        Unreviewed;       478 AA.
AC   A0A081N5S7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN   ORFNames=GZ77_16105 {ECO:0000313|EMBL:KEQ13800.1};
OS   Endozoicomonas montiporae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Endozoicomonadaceae; Endozoicomonas.
OX   NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ13800.1, ECO:0000313|Proteomes:UP000028006};
RN   [1] {ECO:0000313|EMBL:KEQ13800.1, ECO:0000313|Proteomes:UP000028006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ13800.1,
RC   ECO:0000313|Proteomes:UP000028006};
RA   Neave M.J., Apprill A., Voolstra C.R.;
RT   "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC       Note=Binds 1 copper ion per subunit, denoted as copper B.
CC       {ECO:0000256|PIRSR:PIRSR604677-50};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|ARBA:ARBA00001970};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604677-50};
CC       Note=Binds 2 heme groups per subunit, denoted as high- and low-spin.
CC       {ECO:0000256|PIRSR:PIRSR604677-50};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000256|ARBA:ARBA00004673}.
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|ARBA:ARBA00009578, 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:KEQ13800.1}.
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DR   EMBL; JOKG01000003; KEQ13800.1; -; Genomic_DNA.
DR   RefSeq; WP_034877002.1; NZ_JOKG01000003.1.
DR   AlphaFoldDB; A0A081N5S7; -.
DR   eggNOG; COG3278; Bacteria.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000028006; Unassembled WGS sequence.
DR   GO; GO:0045278; C:plasma membrane 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd01661; cbb3_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; IPR004677; Cyt_c_oxidase_cbb3_su1.
DR   NCBIfam; TIGR00780; ccoN; 1.
DR   PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR   PANTHER; PTHR10422:SF29; CYTOCHROME C OXIDASE SUBUNIT 1 HOMOLOG, BACTEROID; 1.
DR   Pfam; PF00115; COX1; 1.
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|PIRSR:PIRSR604677-50, ECO:0000256|RuleBase:RU000370};
KW   Iron {ECO:0000256|PIRSR:PIRSR604677-50};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR604677-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028006};
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        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        129..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        238..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        350..367
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        435..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..459
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   BINDING         61
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1; low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         208
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         258
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         259
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         346
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="2; high-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         348
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_label="1; low-spin"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
SQ   SEQUENCE   478 AA;  53436 MW;  CE0B09F5C2BE4E01 CRC64;
     MSTVMLQPAY NYKVVRQFAL MAVVWAIVGM GVGLFIATQM VFPELNLNLP WTSFGRLRPL
     HTNAVIFAFG GCVLFSTSYY VVQRTCQTTL ALPKLAAFTF WGWQLVIVLA AITLPMGMTS
     SKEYAELEWP IDILITIVWV SYALVFFATI MKRKARHIYV ANWFFGAFII TVAVLHVVNS
     AAIPVTLTKS YSAYAGAMDA MIQWWYGHNA VGFFLTAGFL GMMYYFVPKQ AERPVYSYRL
     SIVHFWALIA IYIWAGPHHL HYTALPDWAQ SLGMVMSLIL LAPSWGGMIN GIMTLSGAWH
     KLRTDPILRF LVVSLSFYGM STFEGPMMAI KTVNALSHYT DWTIGHVHSG ALGWVAMVSF
     GSLYHLIPRV YGREQMYSVP LINAHFWLAT IGTVLYVVAM WVNGITQGLM WRAVNNDGTL
     TYSFIESVVA SEFGYIVRAI GGAFFVSGVL IMAYNVYRTS QLPAQDTEAD ASTEPQAV
//
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