ID M4YDE5_9HYME Unreviewed; 396 AA. AC M4YDE5; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 12-APR-2017, entry version 22. 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:AGI42619.1}; OS Hylaeus sp. 17 PK-2011. OG Mitochondrion {ECO:0000313|EMBL:AGI42619.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; OC Apoidea; Colletidae; Hylaeinae; Hylaeus. OX NCBI_TaxID=1084789 {ECO:0000313|EMBL:AGI42619.1}; RN [1] {ECO:0000313|EMBL:AGI42619.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PK0101 {ECO:0000313|EMBL:AGI42619.1}; RX PubMed=23138101; DOI=10.1016/j.ympev.2012.10.018; RA Kayaalp P., Schwarz M.P., Stevens m.I.; RT "Rapid diversification in Australia and two dispersals out of RT Australia in the globally distributed bee genus, Hylaeus (Colletidae: RT Hylaeinae)."; RL Mol. Phylogenet. Evol. 66:668-678(2013). 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; JN578908; AGI42619.1; -; 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:0005506; F:iron ion binding; IEA:InterPro. 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; 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}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAAS:SAAS00711163, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AGI42619.1}; 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 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 57 81 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 93 120 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 153 169 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 181 201 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 235 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 247 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 307 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 319 340 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 360 383 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 396 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGI42619.1}. FT NON_TER 396 396 {ECO:0000313|EMBL:AGI42619.1}. SQ SEQUENCE 396 AA; 44857 MW; 2B5DF01DBA0B5C4D CRC64; DMAFPRMNNM SFWLLPPSLM LLLLSSMLYT GSGTGWTVYP PLSSILYHSS LSVDLTIFSL HIAGISSIMG AINFIVTILN MKNFNLNYDQ MTLFSWSVLI TAILLLLSLP VLAGAITMLL TDRNLNTSFF DPSGGGDPIL YQHLFWFFGH PEVYILILPG FGLISHIIFN ESGKKETFGN LGMIYAMLGI GFLGFIVWAH HMFTVGLDVD TRAYFTSATM IIAVPTGIKV FSWMATYYGS KIKFNPTILW SLGFIFLFTM GGLTGIMLSN SSIDIMLHDT YYVVAHFHYV LSMGAVFAIM NSLIYWFPIF TGFTLNSNWL YIQFIFMFLG VNLTFFPQHF LGLMGMPRRY SDYPDSYYCW NLLSSIGAIL SLNSLILFIF IIMESLISKR NIIFKY //