ID M1JMV8_9TELE Unreviewed; 607 AA. AC M1JMV8; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 12-AUG-2020, entry version 34. DE RecName: Full=NADH-ubiquinone oxidoreductase chain 5 {ECO:0000256|RuleBase:RU003404}; DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU003404}; GN Name=ND5 {ECO:0000313|EMBL:AGE83220.1}; OS Amblyrhynchichthys truncatus. OG Mitochondrion {ECO:0000313|EMBL:AGE83220.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Amblyrhynchichthys. OX NCBI_TaxID=643417 {ECO:0000313|EMBL:AGE83220.1}; RN [1] {ECO:0000313|EMBL:BAV69466.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CBM ZF 11208 {ECO:0000313|EMBL:BAV69466.1}; RA Miya M.; RT "Whole mitochondrial genome sequences in Cypriniformes."; RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AGE83220.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CTOL01545 {ECO:0000313|EMBL:AGE83220.1}; RA Yang L., Hirt M.V., Sado T., Arunachalam M., Manickam R., Tang K.L., RA Simons A.M., Wu H.-H., Mayden R.L., Miya M.; RT "Phylogenetic placements of the barbin genera Discherodontus, Chagunius, RT and Hypselobarbus in the subfamily Cyprininae (Teleostei: Cypriniformes) RT and their relationships with other barbins."; RL Zootaxa 3586:26-40(2012). 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:ARBA00002539, 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; JX066795; AGE83220.1; -; Genomic_DNA. DR EMBL; AP011179; BAV69466.1; -; Genomic_DNA. DR RefSeq; YP_009310914.1; NC_031519.1. DR GeneID; 29992106; -. 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; 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|ARBA:ARBA00022982}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003404}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, KW ECO:0000256|RuleBase:RU003404, ECO:0000313|EMBL:AGE83220.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW NAD {ECO:0000256|RuleBase:RU003404}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660}; 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|ARBA:ARBA00023075, ECO:0000256|RuleBase:RU003404}. FT TRANSMEM 6..24 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 44..65 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 85..106 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 118..135 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 141..161 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 173..192 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 212..231 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 243..263 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 275..296 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 303..321 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 327..352 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 364..388 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 408..433 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 459..475 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 487..507 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT TRANSMEM 587..606 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003404" FT DOMAIN 66..122 FT /note="Proton_antipo_N" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 135..419 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 424..603 FT /note="NADH5_C" FT /evidence="ECO:0000259|Pfam:PF06455" SQ SEQUENCE 607 AA; 67494 MW; 346AE8F405D7F9C0 CRC64; MTLIMHSSLL LIFFVLMYPL LTTLNPNQQE AKMAKMTKTA VSSAFFISLL PLMIFLNLNT EGIITNWQWM NTQTFDVNMS FKFDHYSLIF VPIALYVTWS ILEFALWYMH SDPNIDRFFK YLLTFLVAMI ILVTANNMFQ LFIGWEGVGI MSFLLIGWWH GRADANTAAL QAVIYNRVGD IGLIMAMAWF AMNLNSWEIQ QIFTLSKNFD MTIPLMGLAL AATGKSAQFG LHPWLPSAME GPTPVSALLH SSTMVVAGIF LLIRLHPLME NNQLALTTCL CLGALTSLFT ATCALTQNDI KKIVAFSTSS QLGLMMVTIG LNQPQLAFLH ICTHAFFKAM LFLCSGSIIH SLNDEQDIRK MGGLLNIMPA TSTYFTIGSL ALTGTPFLAG FFSKDAIIEA LNTSYLNAWA LTLTLIATSF TAVYSFRLVY FVIMGNPRFL PLSPINENNP LVINPIKRLA WGSIIAGLII TQNFLPMKTP IMTMPTTLKM AALMVTILGL ITAMELANMT SKQVKITPII PTHHFSNMLG FFPQIIHRLL PKLKLTLGQS AATQLDKTWL ETLGPKGLAQ VQTTMAKISN DTARGMIKTY LTIFLLTLTL ATIPILL //