ID A0A0U1XGD6_9PETR Unreviewed; 598 AA. AC A0A0U1XGD6; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 08-JUN-2016, entry version 4. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404, ECO:0000256|SAAS:SAAS00370141}; DE EC=1.6.5.3 {ECO:0000256|RuleBase:RU003404}; GN Name=ND5 {ECO:0000313|EMBL:AIT96672.1}; OS Ichthyomyzon fossor. OG Mitochondrion {ECO:0000313|EMBL:AIT96672.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Ichthyomyzon. OX NCBI_TaxID=245073 {ECO:0000313|EMBL:AIT96672.1}; RN [1] {ECO:0000313|EMBL:AIT96672.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Muscle {ECO:0000313|EMBL:AIT96672.1}; RX PubMed=25319286; RA Ren J., Buchinger T., Pu J., Jia L., Li W.; RT "Complete mitochondrial genomes of paired species northern brook RT lamprey (Ichthyomyzon fossor) and silver lamprey (I. unicuspis)."; RL Mitochondrial DNA 1-2:0-0(2014). 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: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). {ECO:0000256|RuleBase:RU003404, CC ECO:0000256|SAAS:SAAS00370008}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU003404, ECO:0000256|SAAS:SAAS00370072}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU003404, CC ECO:0000256|SAAS:SAAS00370072}. 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; KM267716; AIT96672.1; -; Genomic_DNA. DR RefSeq; YP_009106937.1; NC_025552.1. DR GeneID; 22161475; -. 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:respiratory chain; 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; IPR003945; NADHpl_OxRdtase_5. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR001516; Proton_antipo_N. DR Pfam; PF06455; NADH5_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. PE 3: Inferred from homology; KW Electron transport {ECO:0000256|SAAS:SAAS00448190}; KW Membrane {ECO:0000256|SAAS:SAAS00464283, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00448066, ECO:0000313|EMBL:AIT96672.1}; KW Mitochondrion inner membrane {ECO:0000256|SAAS:SAAS00448105}; KW NAD {ECO:0000256|RuleBase:RU000317, ECO:0000256|SAAS:SAAS00448053}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000317, KW ECO:0000256|SAAS:SAAS00464177}; KW Respiratory chain {ECO:0000256|SAAS:SAAS00448195}; KW Transmembrane {ECO:0000256|RuleBase:RU003404, KW ECO:0000256|SAAS:SAAS00464191, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00464492, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00448204}; KW Ubiquinone {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00448240}. FT TRANSMEM 6 26 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 75 95 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 116 133 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 139 158 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 241 261 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 273 294 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 301 319 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 325 347 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 368 387 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 407 428 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 456 472 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 478 499 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 511 530 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 579 597 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 66 120 Proton_antipo_N. {ECO:0000259|Pfam: FT PF00662}. FT DOMAIN 133 415 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 422 596 NADH5_C. {ECO:0000259|Pfam:PF06455}. SQ SEQUENCE 598 AA; 67382 MW; 8D318B8D9B54715C CRC64; MNSHYLTLIM NSGALLTIII LLPPIIMPKP SMLFTTKLVK TSTFISLIPL TIYLNENMET TLTLKPWMDW TMFNIALSFK IDKYTTIFTP ITLMITWNIM EFSQWYMAKE RHMDKFFKYL ILFLITMITF ISANNLLQLF IGWEGVGIMS FLLISWWSGR TKANISALQA VAYNRIGDIG LMMSMAWMCS NTNSWDLQQI TMLLSDQQYL IPTLGFLIAT TGKSAQFGLH PWLPAAMEGP TPVSALLHSS TMVVAGVFLL IRLHPLFKNY QSMLEMTLCL GAMTTIFAAL CATTQNDIKK IIAFSTSSQL GLMMVAIGLN HPHIAFLHMC THAFFKAMLF LCSGSIIHNM NNEQDIRKFS CLNNNLPFTT TCMMIGSMAL MGLPFLAGFF TKDLILEALN TSYTNAWALM MTLLAVTLTT AYSSRLIIMS TSGTPRYLPL SQTSENYFIK NPLKRLAWGS LISGLILTTT IPPMKPQIFT MPIHIKTAAL IMFMVSLIIS IELTNKKINQ TVFSFFTQLA FYPHILHRLM SHLSFISSQK LMTQIMDLSW LEKIGPKGLT NNQLKPSTML TEAHHSNSAT LPLMAFALTL IMLSLTAR //