ID A0A143FT14_9LILI Unreviewed; 393 AA. AC A0A143FT14; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 14-DEC-2022, entry version 20. 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 + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; CC 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}. 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; KT312919; AMW65512.1; -; Genomic_DNA. DR RefSeq; YP_009247545.1; NC_029952.1. DR AlphaFoldDB; A0A143FT14; -. DR GeneID; 27248217; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009536; C:plastid; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.645.10; -; 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; 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 NADP {ECO:0000256|ARBA:ARBA00022857}; 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="Complex1_49kDa" 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 //