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Database: UniProt
Entry: A0A1W6CU50_9RHOB
LinkDB: A0A1W6CU50_9RHOB
Original site: A0A1W6CU50_9RHOB 
ID   A0A1W6CU50_9RHOB        Unreviewed;       558 AA.
AC   A0A1W6CU50;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Cytochrome c oxidase subunit I {ECO:0000313|EMBL:ARJ68356.1};
GN   ORFNames=B0A89_00480 {ECO:0000313|EMBL:ARJ68356.1};
OS   Paracoccus contaminans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ68356.1, ECO:0000313|Proteomes:UP000193017};
RN   [1] {ECO:0000313|EMBL:ARJ68356.1, ECO:0000313|Proteomes:UP000193017}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC   {ECO:0000313|Proteomes:UP000193017};
RA   Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT   "Genome sequence of Paracoccus contaminans isolated from a water
RT   microcosm.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- 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|RuleBase:RU000370}.
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DR   EMBL; CP020612; ARJ68356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6CU50; -.
DR   STRING; 1945662.B0A89_00480; -.
DR   KEGG; pcon:B0A89_00480; -.
DR   OrthoDB; 9803294at2; -.
DR   Proteomes; UP000193017; Chromosome.
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:0009060; P:aerobic respiration; IEA:InterPro.
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   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   Electron transport {ECO:0000256|RuleBase:RU000370};
KW   Heme {ECO:0000256|RuleBase:RU000370}; Iron {ECO:0000256|RuleBase:RU000370};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000370};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193017};
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        31..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        279..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        373..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        491..512
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          22..550
FT                   /note="Cytochrome oxidase subunit I profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50855"
SQ   SEQUENCE   558 AA;  62412 MW;  2EC7D8023E49C266 CRC64;
     MADAALHGHG GHHDTRGFFT RWFMSTNHKD IGVLYLFTAG IVGLISVCFT VYMRMELQHP
     GVQYMCLEGA RLIADASQPC TPNGHLWNVM ITYHGVLMMF FVVIPALFGG FGNYFMPLHI
     GAPDMAFPRL NNLSYWLYVS GVALGIASLL APGGNDQMGS GVGWVLYPPL STTEGGYSMD
     LAIFAVHVSG ASSIVGAINI ITTFLNMRAP GMTLFKVPLF AWSVFITAWM ILLSLPVLAG
     AITMLLMDRN FGTHFFDPAG GGDPVLYQHI LWFFGHPEVY MIILPGFGII SHVIATFARK
     PIFGYLPMVL AMAAIAVLGF VVWAHHMYTA GMSLTQQSYF MLATMTIAVP TGIKVFSWIA
     TMWGGSIEFK TPMLWAFGFL FLFTVGGVTG VVLSQAPLDR VYHDTYYVVA HFHYVMSLGA
     VYAIFAGVYY WIGKMSGRQY PEWAGRLHFF MMFIGSNLLF FPQHFLGREG MPRRYIDYPE
     AFAYWNNISS LGAYLSFASF LFFIGVVFYT LFAGRRVTEN NYWNEYADTL EWTLPSPPPE
     HTFETLPKRE DWDHAAAH
//
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