ID A0A249JMU4_9ROSI Unreviewed; 744 AA. AC A0A249JMU4; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 16-JAN-2019, entry version 5. 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:ASY02466.1}; OS Geranium reflexum. OG Plastid; Chloroplast {ECO:0000313|EMBL:ASY02466.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Geraniales; Geraniaceae; Geranium. OX NCBI_TaxID=379954 {ECO:0000313|EMBL:ASY02466.1}; RN [1] {ECO:0000313|EMBL:ASY02466.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28854633; DOI=.1093/gbe/evx124; RA Park S., Ruhlman T.A., Weng M.L., Hajrah N.H., Sabir J.S.M., RA Jansen R.K.; RT "Contrasting Patterns of Nucleotide Substitution Rates Provide Insight RT into Dynamic Evolution of Plastid and Mitochondrial Genomes of RT Geranium."; RL Genome Biol. Evol. 9:1766-1780(2017). 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|SAAS:SAAS01119703}; 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 ECO:0000256|SAAS:SAAS01119707}; 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 --------------------------------------------------------------------------- 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; KY687055; ASY02466.1; -; 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:ASY02466.1}; 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:ASY02466.1}; 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 6 28 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 40 60 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 92 110 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 122 139 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 145 167 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 179 201 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 221 239 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 260 278 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 284 306 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 327 348 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 354 373 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 393 412 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 424 447 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 545 566 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 600 622 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 721 742 Helical. {ECO:0000256|RuleBase:RU364062}. FT DOMAIN 72 128 Proton_antipo_N. {ECO:0000259|Pfam: FT PF00662}. FT DOMAIN 141 442 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 448 688 Proton_antipo_C. {ECO:0000259|Pfam: FT PF01010}. FT NON_TER 744 744 {ECO:0000313|EMBL:ASY02466.1}. SQ SEQUENCE 744 AA; 84613 MW; 1F6DAA8E2F8B92B9 CRC64; MEYTNKYSWI MPLIPLPVPM LIGVGLLLFP TTTKHLRRIW AFPTVFLLGI VMLLSAYLSI QQLNRSYIYQ YVWSWTINND FSLEFGHLID PLTSTMSILI TTVGLTVLIY SENYMFHDQG YLRFFYYMAF FNASMLGLVT SSNLIQIYIF WEFVGMCSYL LIGFWFTRPV AAKACQKAFV TNRVGDFSLL LGILGLYWIT GSFEFRDLFQ IFNNLVHNNE IPFLFFTLCA FLLFGGALAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIAIPSI LNLISLIAII TVFLGATLAL AQKDIKRVLA YSTMSQLGYM MLALGVGSYR AALFHLITHA YSKALLFLGS GSIIHSMEAL VGYSPEKSQN MVLMGGLTKH MPITKTAFLL GTLSLCGIPP LACFWSKDEI LNESWLYSPI FAIIAFSTAG FTAFYMFRIY LLTFEGHLNV YFLNYSGKRS SSLYSISLWG NEGLKTIQNP FFFKTSLTMN NKQRVPFFCK KTYRLDSSVR SMIRLFTHFG TKNTLPYPHE SENTMLFPIV VLFLFTFFVG AIGIPFNQEG GGLDILSKFL TPYRNLLHQK SNNSVGWHEF ITNGTLSVTI SYLGIVIASF LYKPFYLSLT KLNFINLFVK GGPKKIWRDK IINRIYDWSY NRGYIDAFYT ISLIKGIREL VEFTHFFDAR VIDGITNGLG ILSFFVGEGI KYVGGGRVSS YLLFYLSCVL ICLLIYYFLY FFNF //