ID D7F022_ACOCL Unreviewed; 640 AA. AC D7F022; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 05-DEC-2018, entry version 26. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|RuleBase:RU364062}; DE EC=1.6.5.- {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:ACF19260.1}; OS Acorus calamus (Sweet flag). OG Plastid; Chloroplast {ECO:0000313|EMBL:ACF19260.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Acoraceae; Acorus. OX NCBI_TaxID=4465 {ECO:0000313|EMBL:ACF19260.1}; RN [1] {ECO:0000313|EMBL:ACF19260.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=56.16 {ECO:0000313|EMBL:ACF19260.1}; RA Zhang W., Saarela J.M., Graham S.W.; RT "Molecular Systematics of Acorus Based On Plastid and Nuclear RT Ribosomal DNA Sequence Data."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via CC FMN and iron-sulfur (Fe-S) centers, to quinones in the CC photosynthetic chain and possibly in a chloroplast respiratory CC chain. The immediate electron acceptor for the enzyme in this CC species is believed to be plastoquinone. Couples the redox CC reaction to proton translocation, and thus conserves the redox CC energy in a proton gradient. {ECO:0000256|RuleBase:RU364062}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + H(+) + NADPH = a plastoquinol + CC NADP(+); Xref=Rhea:RHEA:42612, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:62192, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562; CC Evidence={ECO:0000256|RuleBase:RU364062, CC ECO:0000256|SAAS:SAAS00029624}; CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of CC which are encoded in the nucleus. {ECO:0000256|RuleBase:RU364062}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|RuleBase:RU364062}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU364062}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|RuleBase:RU364062, ECO:0000256|SAAS:SAAS00573047}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of 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; EU814663; ACF19260.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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; IPR003945; NADHpl_OxRdtase_5. DR InterPro; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR InterPro; IPR001516; Proton_antipo_N. DR Pfam; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01435; NPOXDRDTASE5. DR TIGRFAMs; TIGR01974; NDH_I_L; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU364062, KW ECO:0000313|EMBL:ACF19260.1}; KW Membrane {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00093326}; KW NAD {ECO:0000256|RuleBase:RU364062, ECO:0000256|SAAS:SAAS00093277}; KW NADP {ECO:0000256|RuleBase:RU364062, ECO:0000256|SAAS:SAAS00029647}; KW Oxidoreductase {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00106999}; KW Plastid {ECO:0000256|RuleBase:RU364062, ECO:0000313|EMBL:ACF19260.1}; KW Plastoquinone {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00029663}; KW Quinone {ECO:0000256|RuleBase:RU364062}; KW Thylakoid {ECO:0000256|RuleBase:RU364062}; KW Transmembrane {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00093342}; KW Transmembrane helix {ECO:0000256|RuleBase:RU364062, KW ECO:0000256|SAAS:SAAS00093282}; KW Transport {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 17 38 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 63 87 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 99 117 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 123 144 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 165 183 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 240 259 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 265 289 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 305 326 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 371 390 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 402 425 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 521 542 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 580 598 Helical. {ECO:0000256|RuleBase:RU364062}. FT DOMAIN 51 107 Proton_antipo_N. {ECO:0000259|Pfam: FT PF00662}. FT DOMAIN 119 420 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 426 640 Proton_antipo_C. {ECO:0000259|Pfam: FT PF01010}. FT NON_TER 1 1 {ECO:0000313|EMBL:ACF19260.1}. FT NON_TER 640 640 {ECO:0000313|EMBL:ACF19260.1}. SQ SEQUENCE 640 AA; 72430 MW; BBE055FF65892EA4 CRC64; GLGLLLVPTA TKNLRRIWAF FSVLLLSIAM VFSADLAIQQ INGSFIYQYS WSWTINNTFS LEFGYLIDPL TSIMLILITT VGIMVLIYSD NYMSHDQGYL RFFAYMSFFN TSMLGLVTSS NLIQIYIFWE LVGMCSYLLI GFWFTRPTAA NACQKAFVTN RXXDFGLLLG ILXLYWITGS FEFRDLFEIL KNLIHNNEVN SLXAALCASL LFVGAVAKSA QFPLHVWLPD AMEGPTPISA LIHAATMVAA GIFLVARLLP LFTVIPYIMN FISLIGIITV LLGATLALAQ RDIKRSLAYS TMSQLGYIML APGIGSYRAA LFHLITHAYS KALLFLGSGS IIHSMEPIVG YSPEKSQNMI LMGGLRRYVP ITKTTFFLGT LSLCGMPPLA CFWSKDEILN DTWLYSPIFA IIAWSTAGLT AFYMFRVYLL TFDGHLQVHF QNFSSTKNSS FYSISIWGKE VPKPLNVNLF LSTMNTNEKM SFFSKNTYQI DRNGKNRIRY FSTQFGNKYT SMYPHESDNT MLFPMLVLVL FTLFIGFIGI PFDQGVIDLD ILSKWLTPSI NLLHSNSGDS FDWYEFVTNA IYSVTISFLG IFLAYIFYGS VYSSFQNLDL INSFVRIDSK RILSDRIING IYNWSYNRGY //