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Database: UniProt
Entry: A0A0M0I1G3_9VIBR
LinkDB: A0A0M0I1G3_9VIBR
Original site: A0A0M0I1G3_9VIBR 
ID   A0A0M0I1G3_9VIBR        Unreviewed;       475 AA.
AC   A0A0M0I1G3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=cytochrome-c oxidase {ECO:0000256|ARBA:ARBA00012949};
DE            EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949};
GN   ORFNames=AKJ31_08220 {ECO:0000313|EMBL:KOO08155.1};
OS   Vibrio hepatarius.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=171383 {ECO:0000313|EMBL:KOO08155.1, ECO:0000313|Proteomes:UP000037530};
RN   [1] {ECO:0000313|Proteomes:UP000037530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19134 {ECO:0000313|Proteomes:UP000037530};
RA   Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT   "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT   isolated from the Solomon Islands.";
RL   Submitted (AUG-2015) 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:KOO08155.1}.
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DR   EMBL; LHPI01000005; KOO08155.1; -; Genomic_DNA.
DR   RefSeq; WP_053408630.1; NZ_VTYD01000002.1.
DR   AlphaFoldDB; A0A0M0I1G3; -.
DR   STRING; 171383.AKJ31_08220; -.
DR   PATRIC; fig|171383.3.peg.1687; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000037530; 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   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..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        348..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..475
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   475 AA;  53463 MW;  609DABDA7CB12811 CRC64;
     MSQEKQLEQN YNYTVVRQFT LVTILWGIVG MAVGVLIAAQ LVWPQLNFDT PWLTYSRLRP
     LHTNAVIFAF GTSALFATSY YVVQRTCQTR LFGGPLVAFT FWGWQAIILA AAITLPLGYT
     SGKEYAELEW PIDIAIAVVW VSYAIVFFGT LVKRKTSHIY VANWFFGAFI ITVAVLHIVN
     SMAIPVSMGK SYSIYAGAVD AMVQWWYGHN AVGFLLTAGF LGMMYYFVPK QAERPVYSYR
     LSIVHFWALI SLYIWAGPHH LHYTALPDWT QSLGMVMSLV LFAPSWGGMI NGIMTLSGAW
     HKLRYDPILR FLIVSLSFYG MSTFEGPMMS IKTVNALSHY TDWTVGHVHS GALGWVAMVS
     IGSVYHLIPR LFGQERMYSV SLINAHFWLA TIGTVLYIVA MWISGVMQGL MWRAVNSDGT
     LTYSFVESVE ASYPFYFVRF LGGFIFLSGM FLMAYNTYKT LSAPKASLKA IQQPA
//
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