ID A0A1D6ZJT3_9POAL Unreviewed; 368 AA. AC A0A1D6ZJT3; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 13-FEB-2019, entry version 10. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {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:ANR01880.1}; OS Cyperus retrorsus. OG Plastid; Chloroplast {ECO:0000313|EMBL:ANR01880.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Cyperaceae; OC Cyperoideae; Cypereae; Cyperus; C4 Cyperus; Cyperus; OC C4 Cyperus unplaced. OX NCBI_TaxID=1352561 {ECO:0000313|EMBL:ANR01880.1}; RN [1] {ECO:0000313|EMBL:ANR01880.1} RP NUCLEOTIDE SEQUENCE. RA Reid C.S., Doyle V., Carter R., Vargas-Rodriguez Y., Urbatsch L.E.; RT "An exploratory multi-locus phylogenetic analysis of Cyperus RT (Cyperaceae), with emphasis on New World taxa."; RL Submitted (JUN-2016) 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 + (n+1) H(+)(in) + NADH = a plastoquinol CC + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, CC ChEBI:CHEBI:62192; Evidence={ECO:0000256|RuleBase:RU364062}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol CC + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA- CC COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:62192; Evidence={ECO:0000256|RuleBase:RU364062}; 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}. 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; KX405920; ANR01880.1; -; 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; IPR018393; NADHpl_OxRdtase_5_subgr. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR PRINTS; PR01435; NPOXDRDTASE5. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|RuleBase:RU364062, KW ECO:0000313|EMBL:ANR01880.1}; KW Membrane {ECO:0000256|RuleBase:RU364062}; KW NAD {ECO:0000256|RuleBase:RU364062}; KW NADP {ECO:0000256|RuleBase:RU364062}; KW Plastid {ECO:0000256|RuleBase:RU364062, ECO:0000313|EMBL:ANR01880.1}; KW Plastoquinone {ECO:0000256|RuleBase:RU364062}; KW Quinone {ECO:0000256|RuleBase:RU364062}; KW Thylakoid {ECO:0000256|RuleBase:RU364062}; KW Transmembrane {ECO:0000256|RuleBase:RU364062}; KW Transmembrane helix {ECO:0000256|RuleBase:RU364062}; KW Transport {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 19 41 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 57 78 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 159 181 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 270 291 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 325 347 Helical. {ECO:0000256|RuleBase:RU364062}. FT DOMAIN 2 172 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 178 366 Proton_antipo_C. {ECO:0000259|Pfam: FT PF01010}. FT NON_TER 1 1 {ECO:0000313|EMBL:ANR01880.1}. FT NON_TER 368 368 {ECO:0000313|EMBL:ANR01880.1}. SQ SEQUENCE 368 AA; 41344 MW; B83C348DF6ECF381 CRC64; AAGVFLVARL FPLFLITPYI MDIISSIGLI TLFLGATLAL AQKDIKRSLA YSTMSQLGYI IMALGIGSFR AALFHLITHA YSKALLFLGS GSIIHSMEPV VGYSPDKNQN MVFMGGLTNY IPITKTAFLL GTLSLCGIPP LGCFWSKDEI LSNSWLHSPI YGIIAYFTAG LTAFYMFRVY LLTFDGYLRI NFQAYSSTKT NFFYSISLWG KSTCNKSNTN RSLPLSKINK KVSFFSKEKK NSLRNKIYCF NIFEANKYTS LFPHESDNTM LIPLILLIVF TVFIGLIGIH FDGSGLDLDL LSRWLTLSKN SFIESSNQYV IFYEFLQNVI FSVSIATFGL CIAFIFYGSI NSFFPNLFLI NLFFKKGV //