ID A0A096ZJ20_MASST Unreviewed; 210 AA. AC A0A096ZJ20; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 22-FEB-2023, entry version 25. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AIS20493.1}; OS Mastocarpus stellatus (Carrageen moss) (Gigartina stellata). OG Mitochondrion {ECO:0000313|EMBL:AIS20493.1}. OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales; OC Phyllophoraceae; Mastocarpus. OX NCBI_TaxID=29227 {ECO:0000313|EMBL:AIS20493.1}; RN [1] {ECO:0000313|EMBL:AIS20493.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MAR2 {ECO:0000313|EMBL:AIS20493.1}; RA Robuchon M., Valero M., Gey D., Le Gall L.; RT "How molecular-assisted identification affects our vision of alpha, beta RT and gamma biodiversity? Insights from a study coupling morphological and RT molecular characters to identify understory red seaweeds (Rhodophyta) of RT Laminaria kelp forests in Brittany, France."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000369}. 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|RuleBase:RU000369}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KJ960835; AIS20493.1; -; Genomic_DNA. DR AlphaFoldDB; A0A096ZJ20; -. DR UniPathway; UPA00705; -. DR GO; GO:0005743; C:mitochondrial inner 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: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 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. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AIS20493.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 37..64 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 85..107 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 127..152 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 164..191 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..210 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AIS20493.1" FT NON_TER 210 FT /evidence="ECO:0000313|EMBL:AIS20493.1" SQ SEQUENCE 210 AA; 22506 MW; 4139FFC647E7961C CRC64; FGAFSGVLGG CMSMLIRMEL AQPSNHLLLG NHQVYNVLIT AHAFLMIFFM VMPVMIGGFG NWLVPIMIGS PDMAFPRLNN ISFWLLPPSL CLLLISAIVE VGAGTGWTVY PPLSSIQSHS GAAVDLAIFS LHLSGASSIL GAVNFISTIL NMRSPGQSMY RIPLFVWSIF VTAFLLLLAV PVLAGAITML LTDRNFNTSF FDPAGGGDPV //