ID G3CUR9_SPITA Unreviewed; 580 AA. AC G3CUR9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 13-FEB-2019, entry version 30. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|SAAS:SAAS00061106}; DE EC=7.1.1.2 {ECO:0000256|SAAS:SAAS01106874}; GN Name=ND5 {ECO:0000313|EMBL:ADN43213.1}; OS Spindasis takanonis (Butterfly) (Cigaritis takanonis). OG Mitochondrion {ECO:0000313|EMBL:ADN43213.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; OC Papilionoidea; Lycaenidae; Aphnaeinae; Spindasis. OX NCBI_TaxID=885001 {ECO:0000313|EMBL:ADN43213.1}; RN [1] {ECO:0000313|EMBL:ADN43213.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21816227; DOI=10.1016/j.ympev.2011.07.013; RA Kim M.J., Kang A.R., Jeong H.C., Kim K.G., Kim I.; RT "Reconstructing intraordinal relationships in Lepidoptera using RT mitochondrial genome data with the description of two newly sequenced RT lycaenids, Spindasis takanonis and Protantigius superans (Lepidoptera: RT Lycaenidae)."; RL Mol. Phylogenet. Evol. 61:436-445(2011). CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory CC chain NADH dehydrogenase (Complex I) that is believed to belong to CC the minimal assembly required for catalysis. Complex I functions CC in the transfer of electrons from NADH to the respiratory chain. CC The immediate electron acceptor for the enzyme is believed to be CC ubiquinone. {ECO:0000256|SAAS:SAAS00061107}. 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|SAAS:SAAS01122516}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|SAAS:SAAS00061113}; Multi-pass membrane protein CC {ECO:0000256|SAAS:SAAS00061113}. 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; HQ184266; ADN43213.1; -; Genomic_DNA. DR RefSeq; YP_004857895.1; NC_016018.1. DR GeneID; 11162849; -. DR CTD; 4540; -. 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:0070469; C:respirasome; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR010934; NADH_DH_su5_C. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01435; NPOXDRDTASE5. PE 4: Predicted; KW Electron transport {ECO:0000256|SAAS:SAAS00061110}; KW Membrane {ECO:0000256|SAAS:SAAS00448218, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|SAAS:SAAS00448066, KW ECO:0000313|EMBL:ADN43213.1}; KW Mitochondrion inner membrane {ECO:0000256|SAAS:SAAS00061114}; KW NAD {ECO:0000256|SAAS:SAAS00061109}; KW Respiratory chain {ECO:0000256|SAAS:SAAS00061105}; KW Translocase {ECO:0000256|SAAS:SAAS01106877}; KW Transmembrane {ECO:0000256|SAAS:SAAS00061112, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00061103, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00061102}; KW Ubiquinone {ECO:0000256|SAAS:SAAS00061120}. FT TRANSMEM 7 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 77 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 89 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 113 133 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 174 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 186 208 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 220 240 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 246 268 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 275 295 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 307 324 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 336 364 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 384 406 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 427 447 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 453 476 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 497 516 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 536 554 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 561 579 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 109 384 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 396 577 NADH5_C. {ECO:0000259|Pfam:PF06455}. SQ SEQUENCE 580 AA; 68157 MW; 2C7508B970B7DE5D CRC64; MLLKKYNICF ISFFFLFFFM IMNFFMFIYF MMNNIILFLE WEIISFNSMN IVMSILLDWM SLLFLMFVCL ISSCVIYYSK SYMSSELNLN RFIILILLFV LSMMLLIVSP NMISIFLGWD GLGLISYCLV IYYQNMKSYN SGMLTALSNR IGDVMILMVV CWMMNYGSWN YIFYLEFMIN DYSMNYISVF VIIAAMTKSA QIPFSSWLPA AMAAPTPVSA LVHSSTLVTA GVYLLIRFNL LLINMFFTKI LLLLSGLTML MSGISANYEF DLKKIIALST LSQLGLMMSI LMMGYFDLAF YHLLTHAMFK ALLFMCSGMI IHMMNNNQNI RFMGGLSFYI PLTSLCMNIS NLALCGIPFL SGFYSKDLIL EMIMMDNLNL MVFYMYYLSV GMTVFYSMRL LMYLMINDYN LISVYNLFDE DYIMLNGMLL LLFMSVISGS MLNWMIYNYP YMIYMSLNMK LMVFYVSLIG LILGVLMSKM SLYSKNKFLM SYMLSNFLSL MWFMPSLSTY SLNYLILSYG ENLNKNIDLG WIEYFSGYSI YNILKNYSFI YYFYQMNNFK IYLFSFMLWM MLIFMMVLFK //