ID M1JMV8_9TELE Unreviewed; 607 AA. AC M1JMV8; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 20-JAN-2016, entry version 17. 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: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: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, RT Chagunius, and Hypselobarbus in the subfamily Cyprininae (Teleostei: RT Cypriniformes) and their relationships with other barbins."; RL Zootaxa 3586:26-40(2012). 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 (By similarity). {ECO:0000256|SAAS:SAAS00370084}. 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; JX066795; AGE83220.1; -; Genomic_DNA. 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:SAAS00061110}; KW Membrane {ECO:0000256|SAAS:SAAS00093326, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00061115, ECO:0000313|EMBL:AGE83220.1}; KW Mitochondrion inner membrane {ECO:0000256|SAAS:SAAS00061114}; KW NAD {ECO:0000256|RuleBase:RU000317, ECO:0000256|SAAS:SAAS00061109}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000317, KW ECO:0000256|SAAS:SAAS00093267}; KW Respiratory chain {ECO:0000256|SAAS:SAAS00061105}; KW Transmembrane {ECO:0000256|RuleBase:RU003404, KW ECO:0000256|SAAS:SAAS00093342, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00093282, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00061102}; KW Ubiquinone {ECO:0000256|RuleBase:RU000318, KW ECO:0000256|SAAS:SAAS00061120}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 44 65 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 106 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 118 135 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 161 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 173 192 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 231 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 243 263 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 275 296 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 303 321 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 327 352 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 364 388 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 408 433 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 459 475 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 487 507 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 587 606 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 66 122 Proton_antipo_N. {ECO:0000259|Pfam: FT PF00662}. FT DOMAIN 135 419 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 424 603 NADH5_C. {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 //