ID NU5C_GOSBA Reviewed; 745 AA. AC A0ZZ82; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 13-SEP-2023, entry version 50. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic; DE EC=7.1.1.-; DE AltName: Full=NAD(P)H dehydrogenase subunit 5; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5; GN Name=ndhF; OS Gossypium barbadense (Sea-island cotton) (Egyptian cotton). OG Plastid; Chloroplast. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium. OX NCBI_TaxID=3634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17159292; DOI=10.1266/ggs.81.311; RA Ibrahim R.I.H., Azuma J., Sakamoto M.; RT "Complete nucleotide sequence of the cotton (Gossypium barbadense L.) RT chloroplast genome with a comparative analysis of sequences among 9 dicot RT plants."; RL Genes Genet. Syst. 81:311-321(2006). 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 (By similarity). CC {ECO:0000250}. 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 -!- 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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}. 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; AP009123; BAF41294.1; -; Genomic_DNA. DR RefSeq; YP_913233.1; NC_008641.1. DR AlphaFoldDB; A0ZZ82; -. DR SMR; A0ZZ82; -. DR GeneID; 4575199; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR Gene3D; 1.20.5.2700; -; 1. DR InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_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; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. DR PRINTS; PR01435; NPOXDRDTASE5. PE 3: Inferred from homology; KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone; KW Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..745 FT /note="NAD(P)H-quinone oxidoreductase subunit 5, FT chloroplastic" FT /id="PRO_0000360936" FT TRANSMEM 9..29 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 50..70 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 99..119 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 135..155 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 157..177 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 194..214 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 229..249 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 268..288 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 290..310 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 337..357 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 364..384 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 406..426 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 435..455 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 550..570 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 610..630 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 724..744 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 745 AA; 84612 MW; C12B3AD1FC31897B CRC64; MEHADQYSWI IPFVPLPIPI LIGMGLLLFP TATKRLLLFP TATKNLRRMW AFPNILLLSI VMIFSLDLSI QQINGSSIYQ YVWSWTINND FSFEFGYFID SLTSIMSILI TTVGIFVLIY SDNYMSHDEG YLRFFAYMSL FNTSMLGLVT SCNLIQIYIF WELVGMCSYL LIGFWFTRPA AANACQKAFV TNRIGDFGLL LGILGFYWIT GSFEFQDLFE IFNNLIYNNE VHFLFVTLCA SLLFAGAVAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL FPLFIVIPYI MNLISLIGII TVLLGATLAL AQNDIKRGLA YSTMSQLGYM MLALGMGSYR AALFHLITHA YSKALLFLAS GSIIHSMEAI VGYSPEKSQN MVFMGGLRKH VPVTQIAFLV GTLSLCGIPP LACFWSKDEI LSDSWLYSPI FAIIAWSTAG LTAFYMFRIY LLTFEGHLNV HFQKYSGKKS SSFYSIKLWG KEEQKIINRN FRLFPLLTLT MNNNEQPYTI GGKKEARITI TNFGYKKAFS YPHESDNTML FPMLILLLFT LFVGAIAIPF NQEGMHLDIL SKLLTPSINL LHQNSNDFED SYQFFKNATF SVSIACFGIF TAFLLYKPFY SSVQNLNLLN SFVKRGPKRI LLDKMIYLIY DWSYNRGYID MFYSISLTKG IRGLAELTHF FDRRVIDGIT NGVGITSFFV GESVKYLGGS RISFYLLLYL VYVFIFLVIS YFILF //