ID A0A343AXG7_HEMSA Unreviewed; 311 AA. AC A0A343AXG7; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 16-JAN-2019, entry version 3. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1 {ECO:0000256|RuleBase:RU000473}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU000473}; GN Name=nad1 {ECO:0000313|EMBL:APT69309.1}; OS Hemigrapsus sanguineus (Asian shore crab). OG Mitochondrion {ECO:0000313|EMBL:APT69309.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; OC Brachyura; Eubrachyura; Grapsoidea; Varunidae; Hemigrapsus. OX NCBI_TaxID=40176 {ECO:0000313|EMBL:APT69309.1}; RN [1] {ECO:0000313|EMBL:APT69309.1} RP NUCLEOTIDE SEQUENCE. RA Liu Q.-N., Tang B.-P.; RT "The complete mitochondrial genome of Hemigrapsus sanguineus."; RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, CC Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; CC EC=7.1.1.2; Evidence={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; KX456205; APT69309.1; -; Genomic_DNA. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR HAMAP; MF_01350; NDH1_NuoH; 1. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS. DR InterPro; IPR000731; SSD. DR PANTHER; PTHR11432; PTHR11432; 1. DR Pfam; PF00146; NADHdh; 1. DR PROSITE; PS00667; COMPLEX1_ND1_1; 1. DR PROSITE; PS00668; COMPLEX1_ND1_2; 1. DR PROSITE; PS50156; SSD; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000473, KW ECO:0000313|EMBL:APT69309.1}; NAD {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 30 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 71 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 124 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 166 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 190 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 216 245 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 272 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 292 310 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 113 SSD. {ECO:0000259|PROSITE:PS50156}. SQ SEQUENCE 311 AA; 35563 MW; C7B229C19E875CA2 CRC64; MIVEVINFLV LMVCVLIGVA FVTLLERKIL GYIQIRKGPN KVGYMGILQP FSDAVKLFTK EQIVPTMSNF LVYYLCPVFS LFVSLVVWCV LPYETGLMSF NLSILFFLCC LSVGVYSTMV AGWSSNCKYS LLGSLRAVAQ TISYEVSLAL ILLSFVMLIG GFSLELFNKY QNYFWFVMIS FPLSMVWFSS CLTETNRTPF DFAEGESDLV SGFNTYYGAG GFALIFMAEY PSILFMIVLF TIFFLGSKPF KLMFYFKPIM EAFAFVWVRG TLPRLRYDKL MYLAWKSSLP VSINYLIFFV SLKMFCFCLL S //