ID A0A2P1CMX7_9HEMI Unreviewed; 323 AA. AC A0A2P1CMX7; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 05-DEC-2018, entry version 4. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 1 {ECO:0000256|RuleBase:RU000473}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU000473}; GN Name=ND1 {ECO:0000313|EMBL:AVJ52647.1}; OS Agonosoma flavolineatum. OG Mitochondrion {ECO:0000313|EMBL:AVJ52647.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Paraneoptera; Hemiptera; Heteroptera; OC Panheteroptera; Pentatomomorpha; Pentatomoidea; Scutelleridae; OC Pachycorinae; Agonosoma. OX NCBI_TaxID=2080385 {ECO:0000313|EMBL:AVJ52647.1}; RN [1] {ECO:0000313|EMBL:AVJ52647.1} RP NUCLEOTIDE SEQUENCE. RA Wu Y., Redei D., Eger J., Wang Y., Wu H., Carapezza A., Kment P., RA Cai B., Sun X., Guo P., Luo J., Xie Q.; RT "Phylogeny and the colourful history of jewel bugs (Insecta: RT Hemiptera: Scutelleridae)."; RL Cladistics 0:0-0(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57945, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566; 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; MF174005; AVJ52647.1; -; Genomic_DNA. 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. 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:AVJ52647.1}; 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 25 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 70 91 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 103 123 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 144 162 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 168 188 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 222 243 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 267 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 287 308 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 323 AA; 37514 MW; 7BF987A54C090988 CRC64; MVVFIITYLV IIICVLVSVG FVTLLERKIL GYIQLRKGPN KVGFMGLLQP FSDGLKLFFK EQMFPYKSNF IIYYFSPVFM LVLSFSLWLL YPMVTNLYNF NYGILFFMCC TGLGVYGVLL SGWSSNSNYA LLGSLRCVAQ TISYEVSMSL IIICLLIFVF SFNLVDFMYY QCYVWFILFS FPLFFCWLSS CLAETNRAPF DFAEGESELV SGFNVEYSGS GFAFIFLSEY MNIIFMSMLT VVMFLGCDLY SFMFYISVVL IVFWFIWVRG TLPRFRYDKL MYLTWKLFLP LTLNYLLFYT GIICLMMLGD YSIELGGMSQ CSV //