ID COX2_PODAN Reviewed; 250 AA. AC P20682; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 13-SEP-2023, entry version 135. DE RecName: Full=Cytochrome c oxidase subunit 2; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide II; GN Name=COII; OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) OS (Pleurage anserina). OG Mitochondrion. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora; OC Podospora anserina. OX NCBI_TaxID=515849; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=A, and s; RX PubMed=2157023; DOI=10.1016/0022-2836(90)90125-6; RA Cummings D.J., Michel F., Domenico J.M., McNally K.L.; RT "Mitochondrial DNA sequence analysis of the cytochrome oxidase subunit II RT gene from Podospora anserina. A group IA intron with a putative alternative RT splice site."; RL J. Mol. Biol. 212:287-294(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=s; RX PubMed=2357736; DOI=10.1007/bf00334517; RA Cummings D.J., McNally K.L., Domenico J.M., Matsuura E.T.; RT "The complete DNA sequence of the mitochondrial genome of Podospora RT anserina."; RL Curr. Genet. 17:375-402(1990). 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; X55026; CAA38803.1; -; Genomic_DNA. DR PIR; S09135; OBJJMP. DR RefSeq; NP_074950.1; NC_001329.3. DR AlphaFoldDB; P20682; -. DR SMR; P20682; -. DR STRING; 515849.P20682; -. DR GeneID; 802467; -. DR KEGG; pan:PoanfMp43; -. DR InParanoid; P20682; -. DR Proteomes; UP000001197; Mitochondrion. 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; Reference proteome; KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..250 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000183665" FT TOPO_DOM 1..39 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 61..81 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT TRANSMEM 82..104 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 105..250 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT BINDING 185 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 220 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 220 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 222 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 222 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 224 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 224 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="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 231 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" SQ SEQUENCE 250 AA; 28541 MW; 4A3E094E9C682997 CRC64; MFFLINKLVM NFDAPSPWGI YFQDSATPQM EGLNELHDNI MYYLVVILFA VGWILLSIVI NYVSTKSPIS HKYLNHGTLI ELIWTITPAV ILILIAFPSF KLLYLMDEVS DPSMSVLAEG HQWYWSYQYP DFLDSNDQFI EFDSYIVPES DLDEGGLRML EVDNRVVLPE LTHVRFIITA GDVIHSFAAP ALGIKCDAYP GRLNQVSVFI NREGVFYGQC SEICGILHSS MPIVIESVSL EKFLIWLKEQ //