ID A0A5B9GB21_9LAMI Unreviewed; 689 AA. AC A0A5B9GB21; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 27-MAR-2024, entry version 16. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|ARBA:ARBA00018648, ECO:0000256|RuleBase:RU364062}; DE EC=7.1.1.- {ECO:0000256|RuleBase:RU364062}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 {ECO:0000256|RuleBase:RU364062}; DE Flags: Fragment; GN Name=ndhF {ECO:0000256|RuleBase:RU364062, GN ECO:0000313|EMBL:QEE82441.1}; OS Fridericia fanshawei. OG Plastid; Chloroplast {ECO:0000313|EMBL:QEE82441.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Bignoniaceae; Bignonieae; Fridericia. OX NCBI_TaxID=2604117 {ECO:0000313|EMBL:QEE82441.1}; RN [1] {ECO:0000313|EMBL:QEE82441.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=FfanAV741 {ECO:0000313|EMBL:QEE82441.1}; RA Kaehler M., Michelangeli F.A., Lohmann L.G.; RT "Fine tuning the circumscription of Fridericia (Bignonieae, RT Bignoniaceae)."; RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases. 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, ECO:0000256|RuleBase:RU364062}. 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 ECO:0000256|RuleBase:RU364062}; 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 ECO:0000256|RuleBase:RU364062}; 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 ECO:0000256|RuleBase:RU364062}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|ARBA:ARBA00004454, CC ECO:0000256|RuleBase:RU364062}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004454, ECO:0000256|RuleBase:RU364062}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|ARBA:ARBA00008200, ECO:0000256|RuleBase:RU364062}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|RuleBase:RU364062}. 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; MK436082; QEE82441.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5B9GB21; -. 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 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 {ECO:0000256|ARBA:ARBA00022528, ECO:0000256|RuleBase:RU364062}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU364062}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364062}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU364062}; KW Plastid {ECO:0000256|RuleBase:RU364062, ECO:0000313|EMBL:QEE82441.1}; KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957, KW ECO:0000256|RuleBase:RU364062}; KW Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|RuleBase:RU364062}; KW Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|RuleBase:RU364062}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU364062}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU364062}; Transport {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 6..24 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 36..56 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 76..100 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 112..130 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 136..157 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 178..196 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 253..278 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 284..302 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 309..330 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 384..403 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 415..438 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 539..559 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 597..615 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT DOMAIN 69..116 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 132..432 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 439..681 FT /note="NADH:ubiquinone/plastoquinone oxidoreductase FT chloroplast chain 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF01010" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:QEE82441.1" FT NON_TER 689 FT /evidence="ECO:0000313|EMBL:QEE82441.1" SQ SEQUENCE 689 AA; 77763 MW; 220B0AF90690E6C4 CRC64; IIPFLPLLVP MLIGVGLLLF PTATKNLRRM WTFPSILLLS IVMIFATNLS IQQINTSSIY QYVWSWTLDN GFSLEFGYLI DPLTSIMLML ITTVGIMVLI YSDNYMAHDE GYLRFFAYMS FFSTSMLGLV TSSNLLQIYI FWELVGMCSY LLIGFWSTRP PAANACQKAF VTNRVGDFGL LLGILGFYWI TGSFEFRDLF EIFNNLISNN EVNCPFVTLC AALLFAGAVA KSAQFPLHVW LPDAMEGPTP ISALIHAATM VAAGIFLVAR LLPLFIVIPY IMNLISLIGL ITVLLGATLA LAQKDIKRGL AYSTMSQLGY MMLALGMGSY RSALFHLITH AYSKALLFLG SGSVIHSMET IVGYSPDKSQ NMVLMGGLRK HVPITKASFL LGTLSLCGIP PLACFWSKDE ILNDSWLYSP IFAIIAWATA GLTAFYMFRI YLLTFEGHLN VHFQNYSGSQ NTPFYSISLW GKGCSQKINK NFRLLRMNNN ESSSFFSKKT YRNDETVRKT NRGQPFINIV HFDTKKPFSY PYESDNTMLF PLLVLVLFTL FVGSLGIPFN QEGTDLDILA KWLAPSINLL HQKSKDSTNW YEFLKDAIFS VSIAYFGIFL ASFLYKPIYS SFKNFDLINL FVKTGSKRSR WDKILNVLYD WSYNRAYIDA FYTTSLTGAI RGLAQLTHFF DRRVIDGIT //