ID I6TF46_9NEOP Unreviewed; 582 AA. AC I6TF46; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 27-MAR-2024, entry version 47. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|ARBA:ARBA00021096, ECO:0000256|RuleBase:RU003404}; DE EC=7.1.1.2 {ECO:0000256|ARBA:ARBA00012944, ECO:0000256|RuleBase:RU003404}; GN Name=ND5 {ECO:0000313|EMBL:AFM95199.1}; OS Actias selene (Indian moon moth). OG Mitochondrion {ECO:0000313|EMBL:AFM95199.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea; OC Saturniidae; Saturniinae; Saturniini; Actias. OX NCBI_TaxID=37776 {ECO:0000313|EMBL:AFM95199.1}; RN [1] {ECO:0000313|EMBL:AFM95199.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HF {ECO:0000313|EMBL:AFM95199.1}; RX PubMed=22688122; DOI=10.1016/j.gene.2012.06.003; RA Liu Q.N., Zhu B.J., Dai L.S., Wei G.Q., Liu C.L.; RT "The complete mitochondrial genome of the wild silkworm moth, Actias RT selene."; RL Gene 505:291-299(2012). RN [2] {ECO:0000313|EMBL:AFM95199.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=HF {ECO:0000313|EMBL:AFM95199.1}; RA Liu C., Liu Q., Zhu B.; RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00003257}. CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from CC NADH through the respiratory chain, using ubiquinone as an electron CC acceptor. Essential for the catalytic activity and assembly of complex CC I. {ECO:0000256|RuleBase:RU003404}. 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|ARBA:ARBA00000766, CC ECO:0000256|RuleBase:RU003404}; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane CC protein {ECO:0000256|ARBA:ARBA00004448}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|RuleBase:RU003404}. 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; JX186589; AFM95199.1; -; Genomic_DNA. DR RefSeq; YP_006504059.1; NC_018133.1. DR AlphaFoldDB; I6TF46; -. DR GeneID; 13230631; -. DR CTD; 4540; -. 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; IPR001750; ND/Mrp_mem. DR InterPro; IPR003945; NU5C-like. DR InterPro; IPR001516; Proton_antipo_N. DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. DR PRINTS; PR01435; NPOXDRDTASE5. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|ARBA:ARBA00022982}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003404}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU003404}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003404}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003404}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU003404}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003404}; KW Ubiquinone {ECO:0000256|RuleBase:RU003404}. FT TRANSMEM 7..32 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 62..79 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 91..108 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 154..174 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 186..204 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 210..234 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 246..264 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 307..324 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 336..361 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 368..388 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 400..418 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 430..451 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 457..477 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 497..517 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 561..581 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT DOMAIN 44..92 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 109..386 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 396..577 FT /note="NADH dehydrogenase subunit 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF06455" SQ SEQUENCE 582 AA; 67667 MW; 9BA80AF95CC0F731 CRC64; MFYKNYSICY ISFFFLFMYS MFNFMLMIYF IMNDLVYFFE WEIITLNSVS VVMSILLDWM SLLFMMFVCL ISSVVIYYSK SYMQSELNLD RFIILVLLFV FSMILLIISP NMVSILLGWD GLGLVSYCSV IYYQNLKSYN AGMLTALTNR IGDVFILMVI SWMLNYGSWD YISYLEFMKN DFMMEVIGVM IILAAMTKSA QIPFSSWLPA AMAAPTPVSA LVHSSTLVTV GVYLLNRFNM LLIDMFFFKI LLMLSILTMF MAGISANHEF DLKKIIALST LSQLGLMMSI LSMGFPNLAF FHLLTHAMFK ALLFMCAGVI IHMMNDIQDI RYMGGVSIYI PLTSLCLNIS NMALCGIPFL AGFYSKDLVL EMVSLSSLNF LVFFFYYIST GLTMFYTFRL LMYTMVMDFN LMVIYNLYDE DFIMLKSMMV LLFMSVISGS MLSWLIFSYP YMIYLPFNMK MMVIYVSLIG GILGYLVSNM KVYSVNKFLM TYSLSNFFCL MWFMPNLSTY GVTYYFLNLG QNLMKNIDLG WSELYSGQGM VNILKNNSIF YNIFQSNNMK IYLFSFVLWL FIMLMMITMI IY //