ID A0A0H3V7J4_9ORYZ Unreviewed; 734 AA. AC A0A0H3V7J4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 28-JUN-2023, entry version 28. 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}; GN Name=ndhF {ECO:0000256|RuleBase:RU364062, GN ECO:0000313|EMBL:AJP34157.1}; OS Oryza glumipatula. OG Plastid; Chloroplast {ECO:0000313|EMBL:AJP34157.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza. OX NCBI_TaxID=40148 {ECO:0000313|EMBL:AJP34157.1}; RN [1] {ECO:0000313|EMBL:AJC09894.1} RP NUCLEOTIDE SEQUENCE. RA Chen X.-L., Norrbom A., Zhu C.-D.; RT "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein, RT Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae)."; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AJP34157.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26355750; DOI=10.1038/srep13957; RA Wambugu P.W., Brozynska M., Furtado A., Waters D.L., Henry R.J.; RT "Relationships of wild and domesticated rices (Oryza AA genome species) RT based upon whole chloroplast genome sequences."; RL Sci. Rep. 5:13957-13957(2015). RN [3] {ECO:0000313|EMBL:ALK00741.1} RP NUCLEOTIDE SEQUENCE. RA Kim K.-H., Yu Y.-S., Wing R.-A., Yang T.-J.; RT "High throughput and simultaneous assembly of complete chloroplast and RT nuclear ribosomal DNA sequences from plant genomes."; RL Submitted (APR-2015) 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 --------------------------------------------------------------------------- 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; KM103374; AJC09894.1; -; Genomic_DNA. DR EMBL; KM881640; AJP34157.1; -; Genomic_DNA. DR EMBL; KR364802; ALK00741.1; -; Genomic_DNA. DR EMBL; KR364803; ALK00845.1; -; Genomic_DNA. DR RefSeq; YP_009155669.1; NC_027461.1. DR AlphaFoldDB; A0A0H3V7J4; -. DR SMR; A0A0H3V7J4; -. DR GeneID; 25015933; -. 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 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. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. 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:AJP34157.1}; 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|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}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 6..28 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 40..60 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 85..109 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 121..139 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 145..167 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 179..201 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 221..239 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 260..278 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 284..306 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 327..348 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 393..412 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 424..447 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 542..562 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 596..618 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 714..733 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT DOMAIN 75..125 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 141..442 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 448..684 FT /note="NADH:ubiquinone/plastoquinone oxidoreductase FT chloroplast chain 5 C-terminal" FT /evidence="ECO:0000259|Pfam:PF01010" SQ SEQUENCE 734 AA; 82527 MW; 4B308BD933E9608C CRC64; MEHTYQYAWV IPLLPLPVIM SMGFGLFLVP TATKNLRRIW AFPSVLLLSI AMVFSVHLSI QQINGSSIYQ YLWSWTVNND FSLEFGYLID PLTSIMLILI TTVGILVLIY SDDYMSHDEG YLRFFVYISF FNTSMLGLVT SSNLIQIYFF WELVGMCSYL LIGFWFTRPI AASACQKAFV TNRVGDFGLL LGILGFFWIT GSLEFRDLFK IANNWIPNNE INSLLTILCA FLLFLGAVAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLIARL LPLFISLPLI MSFISLIGTL TLFLGATLAL AQRDIKRSLA YSTMSQLGYM MLALGIGSYQ AALFHLITHA YSKALLFLGS GSVIHSMEPL VGYSPDKSQN MVLMGGLRKY IPITRTCFLW GTLSLCGIPP LACFWSKDEI LSNSWLYSPF FGIIASFTAG LTAFYMFRIY LLTFDGYLRV HFQNYSSTKE DSLYSISLWG KRISKGVNRD FVLSTAKSGV SFFSQNLSKI HVNTGNRIGS FSTSLGTKNT FVYPHEPGNT MLFPLLILLL CTLFIGSIGI HFDNEIGELT ILSKWLTPSI NFFQESSNSS INSYEFITNA ISSVSLAIFG LFIAYMFYGS AYSFFQNLDL INSFVKGGPK KYFFHQLKKK IYSWSYNRGY IDIFYTRTFT LGIRGLTELT QFFDKGVIDG ITNGVGLASF CIGEEIKYVG GGRISSYLFF FLCYVSVFLF FFLS //