ID G3CUR9_SPITA Unreviewed; 580 AA. AC G3CUR9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 11-DEC-2019, entry version 33. 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; Pterygota; OC Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia; Papilionoidea; OC 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 chain CC NADH dehydrogenase (Complex I) that is believed to belong to the CC minimal assembly required for catalysis. Complex I functions in the CC transfer of electrons from NADH to the respiratory chain. The immediate CC electron acceptor for the enzyme is believed to be ubiquinone. CC {ECO:0000256|SAAS:SAAS00061107}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; CC 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:UniProtKB-EC. 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:SAAS00448190}; KW Membrane {ECO:0000256|SAAS:SAAS00061101, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|SAAS:SAAS00061115, ECO:0000313|EMBL:ADN43213.1}; KW Mitochondrion inner membrane {ECO:0000256|SAAS:SAAS00448105}; KW NAD {ECO:0000256|SAAS:SAAS00448053}; KW Respiratory chain {ECO:0000256|SAAS:SAAS00448195}; KW Translocase {ECO:0000256|SAAS:SAAS01106877}; KW Transmembrane {ECO:0000256|SAAS:SAAS00448069, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00448120, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00448204}; KW Ubiquinone {ECO:0000256|SAAS:SAAS00448240}. FT TRANSMEM 7..31 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 51..77 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 89..107 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 113..133 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 154..174 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 186..208 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 220..240 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 246..268 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 275..295 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 307..324 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 336..364 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 384..406 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 427..447 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 453..476 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 497..516 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 536..554 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 561..579 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 109..384 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 396..577 FT /note="NADH5_C" FT /evidence="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 //