ID I6TCA0_9MAGN Unreviewed; 670 AA. AC I6TCA0; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 16-JAN-2019, entry version 27. 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:AFM94248.1}; OS Monanthotaxis glomerulata. OG Plastid; Chloroplast {ECO:0000313|EMBL:AFM94248.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Magnoliidae; Magnoliales; Annonaceae; OC Annonoideae; Uvarieae; Monanthotaxis. OX NCBI_TaxID=1202423 {ECO:0000313|EMBL:AFM94248.1}; RN [1] {ECO:0000313|EMBL:AFM94248.1} RP NUCLEOTIDE SEQUENCE. RA Wang J., Thomas D.C., Su Y.C.F., Meinke S., Chatrou L.W., RA Saunders R.M.K.; RT "A plastid DNA phylogeny of Dasymaschalon (Annonaceae) and allied RT genera: Evidence for generic non-monophyly and the parallel RT evolutionary loss of inner petals."; RL Taxon 61:545-558(2012). 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 -!- 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; JQ768620; AFM94248.1; -; 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:AFM94248.1}; 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:AFM94248.1}; 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 18 39 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 70 88 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 100 119 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 125 145 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 157 177 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 197 217 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 238 259 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 265 284 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 305 326 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 406 429 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 524 545 Helical. {ECO:0000256|RuleBase:RU364062}. FT TRANSMEM 579 601 Helical. {ECO:0000256|RuleBase:RU364062}. FT DOMAIN 51 107 Proton_antipo_N. {ECO:0000259|Pfam: FT PF00662}. FT DOMAIN 119 347 Proton_antipo_M. {ECO:0000259|Pfam: FT PF00361}. FT DOMAIN 426 667 Proton_antipo_C. {ECO:0000259|Pfam: FT PF01010}. FT NON_TER 1 1 {ECO:0000313|EMBL:AFM94248.1}. FT NON_TER 670 670 {ECO:0000313|EMBL:AFM94248.1}. SQ SEQUENCE 670 AA; 75675 MW; 6DCEA36676746FF9 CRC64; GLGLLIIPTA AKNARRMWTF PSVSLLSIVM VFSAHLSIYQ INGSYVYQYL CSWTINNDFS FEFGHLIDPL SSIMSILITT VGIAVLFYSD NYMSHDQGYL RFFTSMSFFT ISMLGLVTST NLVQIYIFWE LVGMCSYLLI GFWFTRPIAA NACQKAFVTN RVGDFGLLLG ILGFYWITGS FEFRELFEIL NNLISNNGVN CLFATLCAFL LFVGAIAKSA QFPLHVWLPD AMEGPTPISA LIHAATMVAA GIFLVARLFP LFRVIPHIMW LISLVGIITV LLGATLSLAQ RDIKRGLAYS TMSQLGYIML APGIGSFRAA LFHLITHAYS KALLFLGSGS VIHSMESIVG YSPDKSQNMV XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXXXFA IIAYSAAGLT AFYMFRIYLL TFEGHLRVQF QNYSGTKNSS LYSIPIWGNE GMGLSNKNLP FLVINDNNNK ERLSFFSNKV YQMDGNVRNP MRFFSTYSDN KDTSIYPHES DNTMLLPLLI LFLFTLFVGS IGIPFERLGT GFDILSKWLI PQITFLQKDL NFSVDWYEFL INSIFSVSIA CFGIFIASLF YGPVYSSFQN LDLINSFVKM SPKRIFSDRI KYGIYSWSYN RGYIDIFYAT FFIKGIRRLA LLTNFFDKRI //