ID A0A4P2USK8_CYRTA Unreviewed; 219 AA. AC A0A4P2USK8; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 24-JAN-2024, entry version 19. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|ARBA:ARBA00012949, ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AZI71108.1}; GN Synonyms=cox1 {ECO:0000313|EMBL:QOE31739.1}; OS Cyrtonaias tampicoensis (Tampico pearly mussel). OG Mitochondrion {ECO:0000313|EMBL:AZI71108.1}. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia; OC Autobranchia; Heteroconchia; Palaeoheterodonta; Unionida; Unionoidea; OC Unionidae; Ambleminae; Lampsilini; Cyrtonaias. OX NCBI_TaxID=152249 {ECO:0000313|EMBL:AZI71108.1}; RN [1] {ECO:0000313|EMBL:AZI71108.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=UF441144 {ECO:0000313|EMBL:AZI71108.1}; RA Smith C.H., Johnson N.A., Inoue K., Doyle R.D., Randklev C.R.; RT "Integrative taxonomy reveals a new species of freshwater mussel, Potamilus RT streckersoni sp. nov. (Bivalvia: Unionidae): implications for conservation RT and management."; RL Syst. Biodivers. 17:331-348(2019). RN [2] {ECO:0000313|EMBL:QOE31739.1} RP NUCLEOTIDE SEQUENCE. RA Inoue K., Cummings K.S., Tiemann J.S., Miller T.D., Johnson N.A., RA Smith C.H., Randklev C.R.; RT "A new species of freshwater mussel in the genus Popenaias Frierson, 1927, RT from the Gulf coastal rivers of central Mexico (Bivalvia: Unionida: RT Unionidae) with comments on the genus."; RL Zootaxa 4816:457-490(2020). 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 -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, 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|ARBA:ARBA00009578, 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; MK044906; AZI71108.1; -; Genomic_DNA. DR EMBL; MT553984; QOE31739.1; -; Genomic_DNA. DR EMBL; MT553985; QOE31740.1; -; Genomic_DNA. DR EMBL; MT553986; QOE31741.1; -; Genomic_DNA. DR EMBL; MT553987; QOE31742.1; -; Genomic_DNA. DR EMBL; MT553988; QOE31743.1; -; Genomic_DNA. DR EMBL; MT553989; QOE31744.1; -; Genomic_DNA. DR EMBL; MT553991; QOE31746.1; -; Genomic_DNA. DR EMBL; MT553992; QOE31747.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4P2USK8; -. 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:AZI71108.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..219 FT /note="Cytochrome c oxidase subunit 1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5033829860" FT TRANSMEM 46..72 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 84..102 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 122..146 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 167..194 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..219 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AZI71108.1" FT NON_TER 219 FT /evidence="ECO:0000313|EMBL:AZI71108.1" SQ SEQUENCE 219 AA; 23276 MW; 5A8205BDCE006EDC CRC64; TLYLLFALWS GLIGLALSLL IRAELGQPGS LLGDDQLYNV IVTAHAFMMI FFLVMPMMIG GFGNWLIPLM IGAPDMAFPR LNNLSFWLLV PALFLLLSSS LVESGVGTGW TVYPPLSGNV AHSGASVDLA IFSLHLAGAS SILGAINFIS TVGNMRSPGV VAERIPLFVW AVTVTAVLLV AALPVLAGAI TMLLTDRNIN TSFFDPVGGG DPILYMHLF //