ID M4YDE5_9HYME Unreviewed; 396 AA. AC M4YDE5; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 22-APR-2020, entry version 28. 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; Pterygota; OC Neoptera; Holometabola; Hymenoptera; Apocrita; Aculeata; Apoidea; OC 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 Australia in RT the globally distributed bee genus, Hylaeus (Colletidae: Hylaeinae)."; RL Mol. Phylogenet. Evol. 66:668-678(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: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; 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; 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: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: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 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 93..120 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 153..169 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 181..201 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 213..235 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 247..267 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 287..307 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 319..340 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 360..383 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..396 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AGI42619.1" FT NON_TER 396 FT /evidence="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 //