ID U3LTB8_9STRA Unreviewed; 195 AA. AC U3LTB8; DT 11-DEC-2013, integrated into UniProtKB/TrEMBL. DT 11-DEC-2013, sequence version 1. DT 29-MAY-2024, entry version 40. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457}; DE Flags: Fragment; GN Name=COX2 {ECO:0000313|EMBL:AGK25033.1}; OS Globisporangium nagaii. OG Mitochondrion {ECO:0000313|EMBL:AGK25033.1}. OC Eukaryota; Sar; Stramenopiles; Oomycota; Pythiales; Pythiaceae; OC Globisporangium. OX NCBI_TaxID=289625 {ECO:0000313|EMBL:AGK25033.1}; RN [1] {ECO:0000313|EMBL:AGK25033.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=P16712 {ECO:0000313|EMBL:AGK25033.1}; RX PubMed=23709523; DOI=10.3852/12-322; RA Bahramisharif A., Lamprecht S.C., Spies C.F., Botha W.J., McLeod A.; RT "Pythium cederbergense sp. nov. and related taxa from Pythium clade G RT associated with the South African indigenous plant Aspalathus linearis RT (rooibos)."; RL Mycologia 105:1174-1189(2013). 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:RU000457}. 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:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000457}; CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU000457}; Multi-pass membrane CC protein {ECO:0000256|RuleBase:RU000457}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007866, ECO:0000256|RuleBase:RU000457}. 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; JX397984; AGK25033.1; -; Genomic_DNA. DR AlphaFoldDB; U3LTB8; -. 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 GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:TreeGrafter. 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; IPR008972; Cupredoxin. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. 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; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000457}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000457}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000457}; KW Metal-binding {ECO:0000256|RuleBase:RU000457}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, ECO:0000313|EMBL:AGK25033.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000457}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000457}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000457}. FT TRANSMEM 16..36 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 57..79 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..85 FT /note="Cytochrome oxidase subunit II transmembrane region FT profile" FT /evidence="ECO:0000259|PROSITE:PS50999" FT DOMAIN 86..195 FT /note="Cytochrome oxidase subunit II copper A binding" FT /evidence="ECO:0000259|PROSITE:PS50857" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGK25033.1" FT NON_TER 195 FT /evidence="ECO:0000313|EMBL:AGK25033.1" SQ SEQUENCE 195 AA; 22258 MW; B9E9F027B274F643 CRC64; PATPVMEGII NFHHDLMFFL IVVTIFVCWM LFRVITLFDE KKNKIPSTVV HGATIEIIWT SVPALILLTV AVPSFALLYS MDEVIDPIIT LKVIGSQWYW SYEYSDNLEF SDEPLIFDSY MVQENDLEIG QFRLLEVDNR VVVPTNSHIR VLITASDVLH SWAIPSLGIK LDACPGRLNQ TSMFIKREGV FYGQC //