ID A0A0F7LG11_9APHY Unreviewed; 284 AA. AC A0A0F7LG11; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 10-MAY-2017, entry version 5. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1 {ECO:0000256|RuleBase:RU000473}; DE EC=1.6.5.3 {ECO:0000256|RuleBase:RU000473}; GN Name=nad1 {ECO:0000313|EMBL:AKH60738.1}; OS Ganoderma applanatum. OG Mitochondrion {ECO:0000313|EMBL:AKH60738.1}. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Polyporales; Ganodermataceae; Ganoderma. OX NCBI_TaxID=29884 {ECO:0000313|EMBL:AKH60738.1}; RN [1] {ECO:0000313|EMBL:AKH60738.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGMCC5.249 {ECO:0000313|EMBL:AKH60738.1}; RA Wang X.-C., Liu C.; RT "The complete mitochondrial genome of the medicinal fungus Ganoderma RT applanatum (Polyporales, Basidiomycota)."; RL Submitted (APR-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; KR109212; AKH60738.1; -; Genomic_DNA. DR RefSeq; YP_009142661.1; NC_027188.1. DR RefSeq; YP_009142661.1; NC_027188.1. DR RefSeq; YP_009142661.1; NC_027188.1. DR GeneID; 24404525; -. 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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. 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. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000473, KW ECO:0000313|EMBL:AKH60738.1}; 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 29 51 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 63 85 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 106 128 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 134 153 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 180 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 220 241 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 253 279 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 284 AA; 31888 MW; D27276EC564F7E8D CRC64; MYYGILQPFA DALKLVVKET IIPSQSNKIL FYLAPVSTLI FSLLGWGIIP FGEGLTLFDF PLGILYTLAL SSLGVYGVLF AGWSANSKYA FLGSLRSTAA MISYELILSS AILIIILLTG SFNFTTIIES QQSVWFIIPL LPIFIIYFIS ILAETSRTPF DLQEAESELV AGFFTEHSSI IFVFFFLAEY TSIVLFSCIT AILFLGGYNM PNLIVNDTFF NIQSIILGLK TCIFCFMFVW FRATLPRLRY DQLIEFCWLN LLPVVVGFII LVPSILVAFD IAPY //