ID A0A7U3SCX4_9CRUS Unreviewed; 206 AA. AC A0A7U3SCX4; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=7.1.1.9 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:QPF20796.1}; OS Abyssorchomene gerulicorbis. OG Mitochondrion {ECO:0000313|EMBL:QPF20796.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Peracarida; Amphipoda; Amphilochidea; OC Lysianassida; Lysianassidira; Lysianassoidea; Lysianassidae; OC Abyssorchomene. OX NCBI_TaxID=2584831 {ECO:0000313|EMBL:QPF20796.1}; RN [1] {ECO:0000313|EMBL:QPF20796.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2 {ECO:0000313|EMBL:QPF20796.1}; RA Weston J.N.; RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QPF20796.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2 {ECO:0000313|EMBL:QPF20796.1}; RA Weston J.N.J., Peart R.A., Stewart H.A., Ritchie H., Piertney S.B., RA Linley T.D., Jamieson A.J.; RT "Scavenging amphipods from the Wallaby-Zenith Fracture Zone: Extending the RT hadal paradigm beyond subduction trenches."; RL Mar. Biol. 168:0-0(2021). 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 CC [Fe(III)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 -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|ARBA:ARBA00004673, ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000369}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004448, 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; MN262164; QPF20796.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. 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 PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 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:QPF20796.1}; 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 29..52 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 73..95 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 115..138 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 150..179 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..206 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QPF20796.1" FT NON_TER 206 FT /evidence="ECO:0000313|EMBL:QPF20796.1" SQ SEQUENCE 206 AA; 22275 MW; 19CC23BF8A96F0B5 CRC64; ALSVIIRSEL SGPGNLIGSD QIYNVMVTAH AFVMIFFMVM PIMIGGFGNW LVPLMLGSPD MAFPRMNNMS FWLLPPSLIL LLMSGMVETG VGTGWTVYPP LASSVAHSGG SVDMAIFSLH LAGASSILGA INFISSVINM RSYGMSFDRL SLFVWSVFIT AILLLLSLPV LAGAITMLLT DRNLNTSFFD PSGGGDPILY QHLFWF //