ID Q2YG56_LIPVE Unreviewed; 606 AA.
AC Q2YG56;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=nadh5 {ECO:0000313|EMBL:AAV49121.1};
GN Synonyms=ND5 {ECO:0000313|RefSeq:YP_423959.1};
GN ORFNames=KEG26_p03 {ECO:0000313|RefSeq:YP_423959.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OG Mitochondrion {ECO:0000313|EMBL:AAV49121.1,
OG ECO:0000313|RefSeq:YP_423959.1}.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|EMBL:AAV49121.1};
RN [1] {ECO:0000313|EMBL:AAV49121.1, ECO:0000313|RefSeq:YP_423959.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16046150; DOI=10.1016/j.ympev.2005.06.009;
RA Yan J., Zhou K., Yang G.;
RT "Molecular phylogenetics of 'river dolphins' and the baiji mitochondrial
RT genome.";
RL Mol. Phylogenet. Evol. 37:743-750(2005).
RN [2] {ECO:0000313|RefSeq:YP_423959.1}
RP NUCLEOTIDE SEQUENCE.
RG NCBI Genome Project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:YP_423959.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00024313, 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}.
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DR EMBL; AY789529; AAV49121.1; -; Genomic_DNA.
DR RefSeq; YP_423959.1; NC_007629.1.
DR STRING; 118797.Q2YG56; -.
DR GeneID; 3802090; -.
DR KEGG; lve:3802090; -.
DR CTD; 4540; -.
DR OrthoDB; 1463698at2759; -.
DR Proteomes; UP000265300; Mitochondrion MT.
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 InterPro; IPR003945; NU5C-like.
DR InterPro; IPR001516; Proton_antipo_N.
DR NCBIfam; TIGR01974; NDH_I_L; 1.
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.
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 NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003404};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 172..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 301..319
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 325..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 362..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 406..432
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 453..472
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 484..502
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT TRANSMEM 587..605
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003404"
FT DOMAIN 68..118
FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00662"
FT DOMAIN 134..416
FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT subunit"
FT /evidence="ECO:0000259|Pfam:PF00361"
FT DOMAIN 422..602
FT /note="NADH dehydrogenase subunit 5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06455"
SQ SEQUENCE 606 AA; 68582 MW; 5307C43721090DE4 CRC64;
MNPFISSILL TLLMLTTPIM MSFTNLYKTD KYQHYVKNMT LYAFIASLTP TMMFIHTNQE
ALISNWHWMT IQTLKLSLSF KMDYFSLMFM PVALFITWSI MEFSTWYMHS DPYINQFFKY
LLIFLITMLI LITANNIFQL FIGWEGVGIM SFLLINWWSA RTDANTAALQ AILYNRIGDI
GLLVSMAWFL SNMNTWDLQQ IFMLNQNPSN TPLMGLVLAA TGKSAQFGLH PWLPSAMEGP
TPVSALLHSS TMVVAGIFLL IRFHPLMENN EPILTMILSL GAITTLFAAI CALTQNDIKK
IIAFSTSSQL GLMMMTVGLN QPHLAFLHIC THAFFKAMLF MCSGSIIHNL NNEQDIRKMG
GLYKMLPFTT TALTIGCLAL TGTPFLTGFY SKDLIIEAAT SSYTNAWALL LMLTSTSFTA
IYSARIIFYT MLGQPRFPPF MNINELNTTS INPIKRLLIG SIFAGFILSQ NIPPMTTPLM
TMPLYLKLTA LTMTALGFIL ALEINTYTQN LKYPCPSNFT KFSTLLGYFP TIMHRLPTHL
NLTTNQKLMT SLLDLAWTEI IMPKTMTSMQ LKASILTSNQ KGLIKSYFLS FLISLTLSMI
LFNYFE
//
