ID Q6SZW2_9HYME Unreviewed; 440 AA. AC Q6SZW2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 06-FEB-2007, sequence version 2. DT 11-DEC-2019, entry version 73. 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:AAR17000.2}; OS Crematogaster sp. K SPQ-2003. OG Mitochondrion {ECO:0000313|EMBL:AAR17000.2}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; Formicoidea; OC Formicidae; Myrmicinae; Crematogaster; Decacrema. OX NCBI_TaxID=254728 {ECO:0000313|EMBL:AAR17000.2}; RN [1] {ECO:0000313|EMBL:AAR17000.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPQ.Z {ECO:0000313|EMBL:AAR17000.2}; RX PubMed=15119439; RA Quek S.P., Davies S.J., Itino T., Pierce N.E.; RT "Codiversification in an ant-plant mutualism: stem texture and the RT evolution of host use in Crematogaster (Formicidae: Myrmicinae) inhabitants RT of Macaranga (Euphorbiaceae)."; RL Evolution 58:554-570(2004). RN [2] {ECO:0000313|EMBL:AAR17000.2} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SPQ.Z {ECO:0000313|EMBL:AAR17000.2}; RA Quek S.-P., Davies S.J., Itino T., Pierce N.E.; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1-3 CC form the functional core of the enzyme complex. CO I is the catalytic CC subunit of the enzyme. Electrons originating in cytochrome c are CC transferred via the copper A center of subunit 2 and heme A of subunit CC 1 to the bimetallic center formed by heme A3 and copper B. CC {ECO:0000256|RuleBase:RU000369}. 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=1.9.3.1; CC Evidence={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; AY444008; AAR17000.2; -; Genomic_DNA. DR UniPathway; UPA00705; -. 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:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAAS:SAAS00711163, KW ECO:0000256|SAM:Phobius}; Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AAR17000.2}; 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 ECO:0000256|SAAS:SAAS00711093, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00711122, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 73..99 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 111..138 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 171..187 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 231..253 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 265..285 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 305..324 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 336..355 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 375..401 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..440 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAR17000.2" SQ SEQUENCE 440 AA; 49146 MW; B1F198BB93355FB2 CRC64; FMIGGFGNFL IPLMLGSPDM AYPRMNNMSF WLLPPSILLL LLSSFLSSGV GTGWTIYPPL ASNMFHSGPS IDLTIFSLHI AGMSSILGAI NFIATILNMH HSSISLDKIS LLSWSILITA ILLLLSLPVL AGAITMLLTD RNLNTSFFDP SGGGDPILYQ HLFWFFGHPE VYILILPGFG LISHIIMSES GKKETFGSLG MIYAMIAIGF LGFIVWAHHM FTIGLDVDTR AYFTSATMII AIPTGIKIFS WISTLHGMKI TYNPTLWWAM GFIFLFTMGG LTGIMLSNSS IDIILHDTYY VVAHFHYVLS MGAVFAIIAS FIHWFPLISG FTLNKFYLNI QFISMFIGVN LTFFPQHFLG LSGMPRRYSD YPDNFLSWNI ISSIGSLISI LSLSILIYSI WEALSSKRKI INMFFMAPSL EWLSSYPPQN HCFNEIPSIF //