ID A0A059SIT6_ANOST Unreviewed; 189 AA. AC A0A059SIT6; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 29-OCT-2014, entry version 3. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AGX30036.1}; OS Anopheles stephensi (Indo-Pakistan malaria mosquito). OG Mitochondrion {ECO:0000313|EMBL:AGX30036.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; OC Culicidae; Anophelinae; Anopheles. OX NCBI_TaxID=30069 {ECO:0000313|EMBL:AGX30036.1}; RN [1] {ECO:0000313|EMBL:AGX30036.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24827460; RA Ashfaq M., Hebert P.D., Mirza J.H., Khan A.M., Zafar Y., Mirza M.S.; RT "Analyzing mosquito (Diptera: culicidae) diversity in pakistan by DNA RT barcoding."; RL PLoS ONE 9:E97268-E97268(2014). CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {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|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; KF406704; AGX30036.1; -; Genomic_DNA. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AGX30036.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGX30036.1}. FT NON_TER 189 189 {ECO:0000313|EMBL:AGX30036.1}. SQ SEQUENCE 189 AA; 20270 MW; 9F1A087734B0724B CRC64; FIRAELGHPG AFIGDDQIYN VIVTAHAFIM IFFMVMPIMI GGFGNWLVPL MLGAPDMAFP RMNNMSFWML PPSLTLLISS SMVENGAGTG WTVYPPLSSG IAHAGASVDL AIFSLHLAGI SSILGAVNFI TTVINMRSPG ITLDRMPLFV WSVVITAILL LLSLPVLAGA ITMLLTDRNL NTSFFDPAG //