ID A0A0M9UCL0_9CHLR Unreviewed; 609 AA.
AC A0A0M9UCL0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN Name=coxA {ECO:0000313|EMBL:GAP63060.1};
GN ORFNames=ARMA_1483 {ECO:0000313|EMBL:GAP63060.1}, SE16_04430
GN {ECO:0000313|EMBL:KPL89655.1};
OS Ardenticatena maritima.
OC Bacteria; Chloroflexota; Ardenticatenia; Ardenticatenales;
OC Ardenticatenaceae; Ardenticatena.
OX NCBI_TaxID=872965 {ECO:0000313|EMBL:GAP63060.1, ECO:0000313|Proteomes:UP000037784};
RN [1] {ECO:0000313|EMBL:GAP63060.1, ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:GAP63060.1,
RC ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic
RT Thermophilic Bacterium, Ardenticatena maritima Strain 110ST.";
RL Genome Announc. 3:e01145-15(2015).
RN [2] {ECO:0000313|EMBL:KPL89655.1, ECO:0000313|Proteomes:UP000050502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|EMBL:KPL89655.1,
RC ECO:0000313|Proteomes:UP000050502};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Whole genome sequence of Ardenticatena maritima DSM 23922.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000037784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=110S {ECO:0000313|Proteomes:UP000037784};
RA Kawaichi S., Yoshida T., Sako Y., Nakamura R.;
RT "Draft Genome Sequence of a Heterotrophic Facultative Anaerobic Bacterium
RT Ardenticatena maritima Strain 110S.";
RL Submitted (AUG-2015) 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:GAP63060.1}.
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DR EMBL; BBZA01000108; GAP63060.1; -; Genomic_DNA.
DR EMBL; LGKN01000003; KPL89655.1; -; Genomic_DNA.
DR RefSeq; WP_054492930.1; NZ_LGKN01000003.1.
DR AlphaFoldDB; A0A0M9UCL0; -.
DR STRING; 872965.SE16_04430; -.
DR PATRIC; fig|872965.6.peg.860; -.
DR InParanoid; A0A0M9UCL0; -.
DR OrthoDB; 9759913at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000037784; Unassembled WGS sequence.
DR Proteomes; UP000050502; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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; cd01662; Ubiquinol_Oxidase_I; 1.
DR Gene3D; 1.10.287.70; -; 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; 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:GAP63060.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037784};
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 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 75..102
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 114..133
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 162..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 200..228
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 248..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 316..334
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 467..491
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 561..580
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 586..604
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT DOMAIN 24..530
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 609 AA; 67962 MW; 6E0A38F58E8F167A CRC64;
MATRTEPIAR PSTLATWWDT IVEWATTVDH KKIGILYILA SMGFFLFGGI EALMIRTQLA
GPELRFIHPQ LYNEVLTMHG TTMVFLVVMP ILTGFGNYFI PLMIGARDMA FPRLNMLGFW
LFVFGGILLY LSFLSGGAPD GGWFAYAPLT DDTFSPTHGM DFWILGLTVT GIASITGSIN
FVVTILNMRA PGMTLNRMPL FVWTTLVTAF LILFAFPSLT VATIFLFFDR NFGTGFYSPE
MGGTPLLWQH LFWFFGHPEV YIMILPAFGL ISEMIPVFSR KPIFGYAAVV YASVAIGFIG
FTVWAHHMFA VGMPPVVTAS FGAASMIIAV PTAIKIFNWV GTMWGGSLRL RTPMLFAISF
VAMFLIGGLT GIFLATVPVD WQLTDSYFVV AHFHYVLFGG AFMSILGAAY YWFPKMTGRM
MDERLGFWNW LLIFVGFNLT FFPMHILGLD GMPRRIATYG AGLGWDFWNF VSTVGAFMIG
VGMIIFFINF FHSLRNGPEA GDNPWEGWTL EWATASPPPA HNFDGLPPIT SRRPLWDVKL
NRVLTPEEVK ARLVKDEHIH LPPPSVWPLV VGLGVVLIAA GMIYTYVITV LGVVTWVIGV
LGWIQQKGY
//
