ID   A0A143FT14_9LILI        Unreviewed;       393 AA.
AC   A0A143FT14;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-NOV-2024, entry version 25.
DE   RecName: Full=NADH-quinone oxidoreductase subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NADH dehydrogenase I subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
DE   AltName: Full=NDH-1 subunit D {ECO:0000256|HAMAP-Rule:MF_01358};
GN   Name=ndhH {ECO:0000313|EMBL:AMW65512.1};
GN   Synonyms=nuoD {ECO:0000256|HAMAP-Rule:MF_01358};
OS   Tahina spectabilis.
OG   Plastid {ECO:0000313|EMBL:AMW65512.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Coryphoideae;
OC   Chuniophoeniceae; Tahina.
OX   NCBI_TaxID=462332 {ECO:0000313|EMBL:AMW65512.1};
RN   [1] {ECO:0000313|EMBL:AMW65512.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26350789; DOI=10.1111/nph.13617;
RA   Barrett C.F., Baker W.J., Comer J.R., Conran J.G., Lahmeyer S.C.,
RA   Leebens-Mack J.H., Li J., Lim G.S., Mayfield-Jones D.R., Perez L.,
RA   Medina J., Pires J.C., Santos C., Wm Stevenson D., Zomlefer W.B.,
RA   Davis J.I.;
RT   "Plastid genomes reveal support for deep phylogenetic relationships and
RT   extensive rate variation among palms and other commelinid monocots.";
RL   New Phytol. 209:855-870(2016).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC         H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000256|HAMAP-Rule:MF_01358};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoB, C,
CC       D, E, F, and G constitute the peripheral sector of the complex.
CC       {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01358};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01358}.
CC   -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005769, ECO:0000256|HAMAP-Rule:MF_01358,
CC       ECO:0000256|RuleBase:RU003685}.
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DR   EMBL; KT312919; AMW65512.1; -; Genomic_DNA.
DR   RefSeq; YP_009247545.1; NC_029952.1.
DR   AlphaFoldDB; A0A143FT14; -.
DR   GeneID; 27248217; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:TreeGrafter.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050136; F:NADH:ubiquinone reductase (non-electrogenic) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   FunFam; 1.10.645.10:FF:000003; NAD(P)H-quinone oxidoreductase subunit H, chloroplastic; 1.
DR   Gene3D; 1.10.645.10; Cytochrome-c3 Hydrogenase, chain B; 1.
DR   HAMAP; MF_01358; NDH1_NuoD; 1.
DR   InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR   InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR   InterPro; IPR022885; NDH1_su_D/H.
DR   InterPro; IPR029014; NiFe-Hase_large.
DR   PANTHER; PTHR11993:SF10; NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11993; NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA SUBUNIT; 1.
DR   Pfam; PF00346; Complex1_49kDa; 1.
DR   SUPFAM; SSF56762; HydB/Nqo4-like; 1.
DR   PROSITE; PS00535; COMPLEX1_49K; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01358};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01358};
KW   Plastid {ECO:0000313|EMBL:AMW65512.1};
KW   Plastoquinone {ECO:0000256|ARBA:ARBA00022957};
KW   Quinone {ECO:0000256|HAMAP-Rule:MF_01358};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01358};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01358};
KW   Ubiquinone {ECO:0000256|HAMAP-Rule:MF_01358}.
FT   DOMAIN          124..393
FT                   /note="NADH-quinone oxidoreductase subunit D"
FT                   /evidence="ECO:0000259|Pfam:PF00346"
SQ   SEQUENCE   393 AA;  45602 MW;  FE660EB93394CE1F CRC64;
     MTISATKKDL MIVNMGPHHP SMHGVLRLIV TLDGEDVIDC EPILGYLHRG MEKIAENRTI
     IQYLPYVTRW DYLATMFTEA ITVNAPEQLE NVQVPQRASY IRVIMLELSR IASHLLWLGP
     FMADIGAQTP FFYIFREREL LYDLFEAATG MRMMHNYFRI GGVAADLPHG WIDKCLDFCD
     YSLTGVVEYQ KLITRNPIFL ERVERVGIIG GEEAINWGLS GPMLRASGIQ WDLRKVDHYE
     CYNEFDWEVQ WQKEGDSLAR YLVRIGEMRE SIKIIQQALE GIPGGPYENL EVRRFDRAKN
     SEWNDFEYRF ISKKPSPNFE LSKQELYVRV EAPKGELGIY LIGDNSIFPW RWKIRPPGFI
     NLQILPQLVK RMKLADIMTI LGSIDIIMGE VDR
//