ID COX2_ZANCU Reviewed; 254 AA. AC Q3T4C0; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 13-SEP-2023, entry version 83. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000250|UniProtKB:Q0H8Y7}; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide II {ECO:0000250|UniProtKB:Q0H8Y7}; GN Name=cox2 {ECO:0000312|EMBL:AAW49494.1}; OS Zancudomyces culisetae (Gut fungus) (Smittium culisetae). OG Mitochondrion {ECO:0000312|EMBL:AAW49494.1}. OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina; OC Harpellomycetes; Harpellales; Legeriomycetaceae; Zancudomyces. OX NCBI_TaxID=1213189; RN [1] {ECO:0000312|EMBL:AAW49494.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=18-3 {ECO:0000312|EMBL:AAW49494.1}; RX PubMed=15689432; DOI=10.1093/nar/gki199; RA Seif E., Leigh J., Liu Y., Roewer I., Forget L., Lang B.F.; RT "Comparative mitochondrial genomics in zygomycetes: bacteria-like RNase P RT RNAs, mobile elements, and a close source of the group I intron invasion in RT angiosperms."; RL Nucleic Acids Res. 33:734-744(2005). 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:0000250|UniProtKB:P00410}. 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:0000250|UniProtKB:P00410}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC Note=Binds a dinuclear copper A center per subunit. CC {ECO:0000250|UniProtKB:P00410}; CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of a catalytic core of 3 subunits and CC several supernumerary subunits. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00410}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00410}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000305}. 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; AY863213; AAW49494.1; -; Genomic_DNA. DR RefSeq; YP_203327.1; NC_006837.1. DR AlphaFoldDB; Q3T4C0; -. DR SMR; Q3T4C0; -. DR GeneID; 3260112; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 1. DR InterPro; IPR045187; CcO_II. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR034210; CcO_II_C. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR014222; Cyt_c_oxidase_su2. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. DR NCBIfam; TIGR02866; CoxB; 1. DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1. DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 1. DR PROSITE; PS00078; COX2; 1. DR PROSITE; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 3: Inferred from homology; KW Copper; Electron transport; Magnesium; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..254 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000393948" FT TOPO_DOM 12..38 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 60..73 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT TRANSMEM 74..94 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 95..248 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT BINDING 182 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 217 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 217 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 219 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 219 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 221 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 221 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 225 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 228 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" SQ SEQUENCE 254 AA; 29146 MW; 49F6B1CABBD940C0 CRC64; MNIFSFYIIN NDAPEPWQIC YQDSATKIMS GIDKLTGEIF YYETLLLIIV GWVLISAIIK YTKTELSYKY FNHGTLIEIL WTCSPAFILI AISFPSFKLL YLMDSIIDSQ ITIKVLGHQW YWSYEYSDYL DNSGDSISFD SIMIPTDDLE PGQFRLLEVD NRIVLPIHTH IRFICTSSDV IHSFAVPSLG LKIDALPGRL NGISTYVERE GTFYGQCSEL CGVYHFGMPI VIEAVRIEKY LEWLNIHLDN TPSS //