ID   B5FE31_ALIFM            Unreviewed;       476 AA.
AC   B5FE31;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN   Name=ccoN {ECO:0000313|EMBL:ACH66632.1};
GN   OrderedLocusNames=VFMJ11_1377 {ECO:0000313|EMBL:ACH66632.1};
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396 {ECO:0000313|EMBL:ACH66632.1, ECO:0000313|Proteomes:UP000001857};
RN   [1] {ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|Proteomes:UP000001857};
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACH66632.1, ECO:0000313|Proteomes:UP000001857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11 {ECO:0000313|EMBL:ACH66632.1,
RC   ECO:0000313|Proteomes:UP000001857};
RX   PubMed=19182778; DOI=10.1038/nature07660;
RA   Mandel M.J., Wollenberg M.S., Stabb E.V., Visick K.L., Ruby E.G.;
RT   "A single regulatory gene is sufficient to alter bacterial host range.";
RL   Nature 458:215-218(2009).
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}.
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DR   EMBL; CP001139; ACH66632.1; -; Genomic_DNA.
DR   RefSeq; WP_012533873.1; NC_011184.1.
DR   AlphaFoldDB; B5FE31; -.
DR   GeneID; 77252531; -.
DR   KEGG; vfm:VFMJ11_1377; -.
DR   HOGENOM; CLU_017702_3_4_6; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001857; Chromosome I.
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   Oxidoreductase {ECO:0000313|EMBL:ACH66632.1};
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        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        164..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        206..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        351..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        433..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..476
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
FT   BINDING         62
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         209
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         260
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604677-50"
FT   BINDING         347
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         349
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   476 AA;  53632 MW;  88228D616A583E46 CRC64;
     MSQVQQHEQN YNYTVVRQFS LVTILWGIVG MGVGVLIAAQ LVWPQLNFDT PWLTYSRLRP
     LHTNAVIFAF GTSALFATSY YVVQRTCQTR LFGGPLVAFT FWGWQAIILA AAITLPLGIT
     SGKEYAELEW PIDIAITLVW VAYAIVFFGT LFKRKTSHIY VANWFFGAFI LTVAVLHIVN
     SLAVPVSLTK SYSMYSGAVD AMVQWWYGHN AVGFLLTAGF LGMMYYFVPK QAERPVYSYR
     LSIVHFWALV SLYIWAGPHH LHYTALPDWT QSLGMVMSLV LFAPSWGGMI NGIMTLSGAW
     HKLRYDPILR FLIVSLSFYG MSTFEGPMMA IKSVNALSHY TDWTIGHVHS GALGWVAMVS
     IGSLYHLIPK LFGQERMYSV SLINVHFWLA TIGTVFYIVA MWISGVMQGL MWRAVNADGT
     LTYSFVESLE ASYPFYFVRF IGGLIFLSGM FLLAYNTYKT ITAPKNSLKA IQQPAQ
//