ID A0A8F5DP25_DROBR Unreviewed; 747 AA. AC A0A8F5DP25; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 25-MAY-2022, entry version 2. 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:QXJ79972.1}; OS Drosera burmannii (Burmese sundew). OG Plastid; Chloroplast {ECO:0000313|EMBL:QXJ79972.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Droseraceae; Drosera. OX NCBI_TaxID=4365 {ECO:0000313|EMBL:QXJ79972.1}; RN [1] {ECO:0000313|EMBL:QXJ79972.1} RP NUCLEOTIDE SEQUENCE. RA Zhang E.; RT "Characterization of the complete chloroplast genome of Drosera burmanni RT Vahl."; RL Submitted (DEC-2020) 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; MW316693; QXJ79972.1; -; Genomic_DNA. 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; PTHR42829; 1. DR Pfam; PF01010; Proton_antipo_C; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. 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:QXJ79972.1}; 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}; Transport {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..200 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 220..239 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 260..281 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 287..311 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 546..566 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 605..625 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT TRANSMEM 721..741 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU364062" FT DOMAIN 75..125 FT /note="Proton_antipo_N" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 141..442 FT /note="Proton_antipo_M" FT /evidence="ECO:0000259|Pfam:PF00361" FT DOMAIN 448..688 FT /note="Proton_antipo_C" FT /evidence="ECO:0000259|Pfam:PF01010" SQ SEQUENCE 747 AA; 85066 MW; 996A804FD780556F CRC64; MEYTYKYAWV IPLFPLPVTM SIGFGLLFIP TATKDIRRMW AFPSVLLLSI AMCFSANLSI QQINGSFTYQ CLWSWIINND FLLEFGYLID PLTSIMSILI TTVGILVFIY SDNYMSHDQG YLRFFAHMSF FNASMLGLVT SSNLIQIYIF WELVGMCSYF LIGFWFTRPV AASACQKAFV TNRIGDFGLL LGILGFYWIT GSFEFRDLFQ IVNTLIHKNG VNSFFVTLCA FLLFVGTIAK SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIVIPYI MNIICLVGII TLLLGATLAL AQRDIKRSLA YSTMSQLGYI MLALGIGSYR AALFHLITHA YSKALLFLGS GSIIHSMEPI VGYSPEKSQN MVLMGGLTKY VPITKTTFFL GTLSLCGIPP LACFWSKDEI IHDSWLYSPI FALIAWFTAG LTAFYMFRMY LLTFDGYLRI YFQDYSSFSS TKNSSFYSIS LWGKEPLKEV NSNLIFSKMN KNIFWFFSKD LSKIDKNVRN KIRDFSTYFI NRYTYMYPHE SSNTMLFPLL VLVLFTLFIG SIGIPFNGGI IDLDLLSKWL TPSTTFFSPN FNYSEDWYEF LSNTFFSVGI ALFGLFLASI FYGSIYSSFK NFGLMNFFLK RGPKIIILEK IKGVIYNWSY NRGYIDVFYT GIFTMSIRGL AELTQFFDKF LIDGIINGIG VASFFMSEGI KYMGGGRISS YLFLYFSYIS IFLLIFISFS LPNFQFS //