ID D8TE51_SELML Unreviewed; 190 AA.
AC D8TE51;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 6 {ECO:0000256|RuleBase:RU004430};
DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU004430};
GN Name=ndhG {ECO:0000313|EMBL:ADH10450.1};
GN ORFNames=SELMODRAFT_137798 {ECO:0000313|EMBL:EFJ05039.1};
OS Selaginella moellendorffii (Spikemoss).
OG Mitochondrion {ECO:0000313|EMBL:EFJ05039.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|EMBL:EFJ05039.1, ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ05039.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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:RU004430}.
CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN
CC and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain
CC and possibly in a chloroplast respiratory chain. The immediate electron
CC acceptor for the enzyme in this species is believed to be
CC plastoquinone. Couples the redox reaction to proton translocation, and
CC thus conserves the redox energy in a proton gradient.
CC {ECO:0000256|ARBA:ARBA00004059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n
CC H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n
CC H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561,
CC Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
CC Evidence={ECO:0000256|ARBA:ARBA00001558};
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|RuleBase:RU004430};
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000256|ARBA:ARBA00011199}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC membrane {ECO:0000256|RuleBase:RU004430}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU004430}. Plastid, chloroplast thylakoid
CC membrane {ECO:0000256|ARBA:ARBA00004454}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004454}.
CC -!- SIMILARITY: Belongs to the complex I subunit 6 family.
CC {ECO:0000256|ARBA:ARBA00005698, ECO:0000256|RuleBase:RU004430}.
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DR EMBL; HM173080; ADH10450.1; -; Genomic_DNA.
DR EMBL; GL377739; EFJ05039.1; -; Genomic_DNA.
DR RefSeq; XP_002993898.1; XM_002993852.1.
DR AlphaFoldDB; D8TE51; -.
DR STRING; 88036.D8TE51; -.
DR EnsemblPlants; ADH10450; ADH10450; ADH10450.
DR EnsemblPlants; EFJ05039; EFJ05039; SELMODRAFT_137798.
DR Gramene; ADH10450; ADH10450; ADH10450.
DR Gramene; EFJ05039; EFJ05039; SELMODRAFT_137798.
DR eggNOG; ENOG502QQHR; Eukaryota.
DR HOGENOM; CLU_085957_3_0_1; -.
DR InParanoid; D8TE51; -.
DR OMA; IEWASIG; -.
DR Proteomes; UP000001514; Mitochondrion.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.1200; NADH-ubiquinone/plastoquinone oxidoreductase chain 6, subunit NuoJ; 1.
DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR PANTHER; PTHR48391; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48391:SF1; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 6, CHLOROPLASTIC; 1.
DR Pfam; PF00499; Oxidored_q3; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:ADH10450.1};
KW Electron transport {ECO:0000256|RuleBase:RU004430};
KW Mitochondrion {ECO:0000256|RuleBase:RU004430, ECO:0000313|EMBL:EFJ05039.1};
KW NAD {ECO:0000256|RuleBase:RU004430}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:ADH10450.1};
KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW Quinone {ECO:0000256|ARBA:ARBA00022719};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Respiratory chain {ECO:0000256|RuleBase:RU004430};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW Translocase {ECO:0000256|RuleBase:RU004430};
KW Transport {ECO:0000256|RuleBase:RU004430};
KW Ubiquinone {ECO:0000256|RuleBase:RU004430}.
SQ SEQUENCE 190 AA; 19848 MW; 43034C5A7CFD143B CRC64;
MSSPESVHDA VLVSSASGPA LGSLGVVSLV NIVHPAPSSG SVSACISLPH PSMNADFAAA
VQILIHAGAV NVPIPFAAMP VSQPQYPHPA KPWTVGDGIT SALRTSAFPP LINMILYTSW
YRIFPIVLRN AGSSPTHSVQ RIGSYSSTES LPPFEPPSIV LLVALVGAIT VARREQVIGQ
ETEPALRIDD
//
