ID A0A1U6ZEY4_CENAU Unreviewed; 324 AA. AC A0A1U6ZEY4; DT 10-MAY-2017, integrated into UniProtKB/TrEMBL. DT 10-MAY-2017, sequence version 1. DT 07-JUN-2017, entry version 2. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1 {ECO:0000256|RuleBase:RU000473}; DE EC=1.6.5.3 {ECO:0000256|RuleBase:RU000473}; GN Name=ND1 {ECO:0000313|EMBL:AKS03568.1}; OS Centropyge aurantia (Golden angelfish). OG Mitochondrion {ECO:0000313|EMBL:AKS03568.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Pomacanthidae; Centropyge. OX NCBI_TaxID=466111 {ECO:0000313|EMBL:AKS03568.1}; RN [1] {ECO:0000313|EMBL:AKS03568.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Muscle {ECO:0000313|EMBL:AKS03568.1}; RA Shen K.-N., Hsiao C.-D.; RT "Next generation sequencing yields the complete mitochondrial genome RT of the Golden angelfish, Centropyge aurantius (Perciformes: RT Pomacanthidae)."; RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). {ECO:0000256|RuleBase:RU000473}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000471}. CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC {ECO:0000256|RuleBase:RU000471}. 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; KP973959; AKS03568.1; -; Genomic_DNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR HAMAP; MF_01350; NDH1_NuoH; 1. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS. DR PANTHER; PTHR11432; PTHR11432; 1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00667; COMPLEX1_ND1_1; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000473, KW ECO:0000313|EMBL:AKS03568.1}; NAD {ECO:0000256|RuleBase:RU000471}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000471}; KW Transmembrane {ECO:0000256|RuleBase:RU000471, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Ubiquinone {ECO:0000256|RuleBase:RU000473}. FT TRANSMEM 6 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 107 129 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 150 171 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 177 194 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 254 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 260 279 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 320 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 324 AA; 35707 MW; 0EF4218F06749F6E CRC64; MISTLITHIL NPLAFIVPVL LAVAFLTLLE RKVLGYMQAR KGPNIVGPHG ILQPISDGAK LFTKEPIRPL TSSSFLFLIT PIMALTLALT LWAPLPMPHP VIDLNLGILF IIALSSLAVY SILGSGWASN SKYALLGALR AVAQTISYEV SLGLILLNAV ILTGNFTLQT FSTAQESMWL ILPTWPLAAM WYISTLAETN RAPFDLTEGE SELVSGFNVE YAGGPFALFF LAEYSNILFM NTLSAILFMG ATYFPSLPMF TTANLMTKAA LLSLVFLWVR ASYPRFRYDQ LMHLIWKNFL PLTLALIIWH LAMPIALAGL PPQM //