ID Q85AE9_ECHMA Unreviewed; 361 AA. AC Q85AE9; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|ARBA:ARBA00015947, ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; OS Echinometra mathaei (Rock boring urchin) (Echinus mathaei). OG Mitochondrion {ECO:0000313|EMBL:AAP31634.1}. OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea; OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinometridae; OC Echinometra. OX NCBI_TaxID=31178 {ECO:0000313|EMBL:AAP31634.1}; RN [1] {ECO:0000313|EMBL:AAP31634.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MDm2 {ECO:0000313|EMBL:AAP31634.1}, MDm3 RC {ECO:0000313|EMBL:AAP31635.1}, MDm7 {ECO:0000313|EMBL:AAP31637.1}, and RC MDm8 {ECO:0000313|EMBL:AAP31638.1}; RX PubMed=12964987; DOI=10.1098/rspb.2003.2395; RA Landry C., Geyer L.B., Arakaki Y., Uehara T., Palumbi S.R.; RT "Recent speciation in the Indo-West Pacific: rapid evolution of gamete RT recognition and sperm morphology in cryptic species of sea urchin."; RL Proc. R. Soc. B 270:1839-1847(2003). 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] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|RuleBase:RU000369}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000256|ARBA:ARBA00001971}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, 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|ARBA:ARBA00009578, 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; AY262912; AAP31634.1; -; Genomic_DNA. DR EMBL; AY262913; AAP31635.1; -; Genomic_DNA. DR EMBL; AY262915; AAP31637.1; -; Genomic_DNA. DR EMBL; AY262916; AAP31638.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. 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:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 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; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 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|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, ECO:0000313|EMBL:AAP31634.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 30..55 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 76..100 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 120..143 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 155..182 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 215..233 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 240..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 275..298 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 310..331 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 343..360 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..361 FT /note="Cytochrome oxidase subunit I profile" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAP31634.1" FT NON_TER 361 FT /evidence="ECO:0000313|EMBL:AAP31634.1" SQ SEQUENCE 361 AA; 39192 MW; D1082528B56F0693 CRC64; VGTAMSVIIR AELAQPGSLL NDDQIYNXVV TAHALVMIFF MVMPIMIGGF GNWLIPLMIG APDMAFPRMN NMSFWLVPPS FILLLASAGV ESGAGTGWTI YPPLSSNIAH AGGSVDLAIF SLHLAGASSI LASINFITTI INMRTPGMSF DRLPLFVWSV FVTAFLLLLS LPVLAGAITM LLTDRNINTT FFDPAGGGDP ILFQHLFXXX XHPEVYILIL PGFGMISHVI AHYSGKREPF GYLGMVYAMI AIGVLGFLVW AHHMFTVGMD VDTRAYFTAA TMIIAVPTGI KVFSWMATLQ GSNLQWETPL FWALGFVFLF TLGGLTGIVL ANSSIDVVLH DTYYVVAHFH YVLSMGAVFA I //