ID A0A7T6ZR05_9SAUR Unreviewed; 536 AA. AC A0A7T6ZR05; 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}; GN Name=COX1 {ECO:0000313|EMBL:QQK90409.1}; OS Pseudagkistrodon rudis (Red keelback). OG Mitochondrion {ECO:0000313|EMBL:QQK90409.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera; OC Serpentes; Colubroidea; Colubridae; Natricinae; Pseudagkistrodon. OX NCBI_TaxID=2759634 {ECO:0000313|EMBL:QQK90409.1}; RN [1] {ECO:0000313|EMBL:QQK90409.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Muscle {ECO:0000313|EMBL:QQK90409.1}; RA Zhou Y.-N., Zhong J.-J., Zhang Z.-H., Ma L., Ding G.-H.; RT "The Complete mitochondrial genome of Pseudagkistrodon rudis."; RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases. 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 -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|ARBA:ARBA00001935}; 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane CC protein {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; MW327508; QQK90409.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. 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 Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Copper {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000369}; Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000369}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU000369}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792, KW ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000369}; Sodium {ECO:0000256|ARBA:ARBA00023053}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000369}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 21..40 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 60..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 107..129 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 149..174 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 186..213 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 246..264 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 276..294 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 306..329 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 341..362 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 374..396 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 417..436 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 456..479 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 3..514 FT /note="COX1" FT /evidence="ECO:0000259|PROSITE:PS50855" SQ SEQUENCE 536 AA; 59857 MW; 9B045786268DDB65 CRC64; MLPVFMTRWL FSTNHKDIGT LYLLFGAWSG LIGACLSILM RMELTQPGTL FGSDQIFNVL VTAHAFIMIF FMVMPIMIGG FGNWLIPLMI GAPDMAFPRM NNMSFWLLPP ALLLLLSSSY VEAGAGTGWT VYPPLSGNLA HSGPSVDLAI FSLHLAGASS ILGAINFITT CINMKPKSMP MFNIPLFVWS VLITAIMLLT ALPVLAAAIT MLLTDRNLNT SFFDPSGGGD PVLFQHLFWF FGHPEVYILI LPGFGIISSI ITFYTGKKNT FGYTSMIWAM MSIAILGFVV WAHHMFTVGL DIDSRAYFTA ATMIIAIPTG IKVFGWLATL TGGQIKWQTP VYWALGFIFL FTVGGMTGII LANSSLDIVL HDTYYVVAHF HYVLSMGAVF AIMGGLTHWF PLFTGYSLNQ TMTKTQFWVM FIGVNLTFFP QHFLGLSGMP RRYSDFPDAF TLWNTISSIG STISLMAVLM SLFIVWEALS YKRELAQSMG KKTHIEWFFG TPPPHHTHTE PTFMLNNVFA PIRNFITYME WPWPEK //