ID A0A345UP12_9BACT Unreviewed; 575 AA.
AC A0A345UP12;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU363061};
DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU363061};
GN ORFNames=CYPRO_2977 {ECO:0000313|EMBL:AXJ02214.1};
OS Cyclonatronum proteinivorum.
OC Bacteria; Balneolota; Balneolia; Balneolales; Cyclonatronaceae;
OC Cyclonatronum.
OX NCBI_TaxID=1457365 {ECO:0000313|EMBL:AXJ02214.1, ECO:0000313|Proteomes:UP000254808};
RN [1] {ECO:0000313|EMBL:AXJ02214.1, ECO:0000313|Proteomes:UP000254808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Omega {ECO:0000313|EMBL:AXJ02214.1,
RC ECO:0000313|Proteomes:UP000254808};
RA Toshchakov S.V., Korzhenkov A., Samarov N.I., Kublanov I.V., Muntyan M.S.,
RA Sorokin D.Y.;
RT "Phenotypic and genomic properties of Cyclonatronum proteinivorum gen.
RT nov., sp. nov., a haloalkaliphilic bacteroidete from soda lakes possessing
RT Na+-translocating rhodopsin.";
RL Submitted (MAR-2018) 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}.
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DR EMBL; CP027806; AXJ02214.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345UP12; -.
DR KEGG; cprv:CYPRO_2977; -.
DR OrthoDB; 9759913at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000254808; Chromosome.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000254808};
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 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 87..115
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 168..192
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 212..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 256..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 292..313
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 325..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 362..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 398..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 433..455
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT TRANSMEM 475..498
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363061"
FT DOMAIN 36..537
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
SQ SEQUENCE 575 AA; 63988 MW; 9824B7871AD9FFB4 CRC64;
MSATASNGNT LKVRYFDIDE NPSKNYLNAE SGLKSWLFTV DHKRIGLMYL ASIALFFFVG
GVLALVLRTE LFTPAENLMN AETYNRIFTL HGAIMVFLFI IPSIPAALGN FLLPIMLGAK
DVAFPRLNLA SFWIYSIGAL FTLASLAVNP IDTGWTFYTP YSVQTGSAVI LMTFGVFIMG
FSSILTGMNF IVTIHKMRAP GLTWGRLPLF IWAMYATSVI QVLATPVLAI TLALLIMERV
LGVGIFDPAL GGDPVLYQHF FWFYSHPAVY IMIVPAFGVI SELIGTFSRK TVFGYWAIAM
SSLAIAFIGS LVWGHHMFVS GQSELSTVVF SFLTFFVGIP TGIKIFNWLA TMHKGSIDMK
TPMLYACIFL FLFTIGGVTG IMLGAISVNV HLHDTYYVVA HFHYVMMGGT VMAFLGGLHF
WWPKMTGKMY NEFWGKISAV IIFIGFNLTF LPQFIMGSQG MPRRYYSYID QFQAMHQLST
IGSYVLGIGF VIIAIYLAHS LLKGEKAPAN PWGARTLDWM TSSPPVQHNF DYQPVVTNGA
YDYHKPVSEF TLGISDDVYH QEHAGEKKSE SAQTV
//
