ID A0A347ZJS0_9TELE Unreviewed; 232 AA. AC A0A347ZJS0; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 17-JUN-2020, entry version 10. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709560}; GN Name=COII {ECO:0000313|EMBL:BBA85485.1}; OS Notacanthus chemnitzii (spiny eel). OG Mitochondrion {ECO:0000313|EMBL:BBA85485.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Notacanthiformes; Notacanthidae; OC Notacanthus. OX NCBI_TaxID=143895 {ECO:0000313|EMBL:BBA85485.1}; RN [1] {ECO:0000313|EMBL:BBA85485.1} RP NUCLEOTIDE SEQUENCE. RA Poulsen JY.; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BBA85485.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30044814; DOI=10.1371/journal.pone.0199982; RA Poulsen J.Y., Miller M.J., Sado T., Hanel R., Tsukamoto T., Miya M.; RT "Resolving deep-sea pelagic saccopharyngiform eel mysteries: Identification RT of Neocyema and Monognathidae leptocephali and establishment of a new fish RT family "Neocyematidae" based on larvae, adults and mitogenomic gene RT orders."; RL PLoS ONE 13:e0199982-e0199982(2018). 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 ECO:0000256|SAAS:SAAS01246537}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 [Fe(III)cytochrome c] CC + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA- CC COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|SAAS:SAAS01254289}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|SAAS:SAAS01254289}; 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: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709542}; Multi- CC pass membrane protein {ECO:0000256|RuleBase:RU000457, CC ECO:0000256|SAAS:SAAS00709542}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00709553}. 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; AP018344; BBA85485.1; -; Genomic_DNA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:InterPro. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. 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 Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR SUPFAM; SSF49503; SSF49503; 1. DR SUPFAM; SSF81464; SSF81464; 1. DR TIGRFAMs; TIGR02866; CoxB; 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 {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00477878}; KW Electron transport {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS01155864}; Magnesium {ECO:0000256|SAAS:SAAS01246526}; KW Membrane {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS00883094, KW ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00119299}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709499, ECO:0000313|EMBL:BBA85485.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00709564}; KW Respiratory chain {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS01154861}; KW Translocase {ECO:0000256|SAAS:SAAS01254292}; KW Transmembrane {ECO:0000256|RuleBase:RU000457, KW ECO:0000256|SAAS:SAAS00882981, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00883111, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000457, ECO:0000256|SAAS:SAAS01155879}. FT TRANSMEM 27..51 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 63..85 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..91 FT /note="COX2_TM" FT /evidence="ECO:0000259|PROSITE:PS50999" FT DOMAIN 92..225 FT /note="COX2_CUA" FT /evidence="ECO:0000259|PROSITE:PS50857" SQ SEQUENCE 232 AA; 26296 MW; ADB009D8010EA0A2 CRC64; MAHPSQLGFQ DAASPVMEEL LHFHDHALMI VFLISTLVVY IIVAMVTTKL TNKYILDSQE IEIIWTVLPA VILILIALPS LRILYLMDEI NDPHLTIKAM GHQWYWSYEY TDYEDLGFDS YMIPTQDLTP GQFRLLETDH RMVVPMEAPV RMLISAEDVL HSWAVPALGV KMDAVPGRLN QSAFIASRPG VYYGQCSEIC GANHSFMPIV VEAVPLQHFE NWSSLMMEDA SL //