ID Q6VQB4_9ERIC Unreviewed; 415 AA. AC Q6VQB4; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 29-MAY-2024, entry version 66. DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000256|ARBA:ARBA00018648}; DE AltName: Full=NAD(P)H dehydrogenase subunit 5 {ECO:0000256|ARBA:ARBA00031649}; DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 {ECO:0000256|ARBA:ARBA00029876}; DE Flags: Fragment; GN Name=ndhF {ECO:0000313|EMBL:AAR86929.1}; OS Thibaudia pachyantha. OG Plastid; Chloroplast {ECO:0000313|EMBL:AAR86929.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Ericaceae; Vaccinioideae; Vaccinieae; Thibaudia. OX NCBI_TaxID=180746 {ECO:0000313|EMBL:AAR86929.1}; RN [1] {ECO:0000313|EMBL:AAR86929.1} RP NUCLEOTIDE SEQUENCE. RA Powell E.A., Kron K.A.; RT "Molecular systematics of the northern Andean blueberries (Vaccinieae, RT Vaccinioideae, Ericaceae)."; RL Submitted (JUN-2003) 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}. 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 -!- 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 -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which CC are encoded in the nucleus. {ECO:0000256|ARBA:ARBA00011199}. 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}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004454}. CC -!- SIMILARITY: Belongs to the complex I subunit 5 family. CC {ECO:0000256|ARBA:ARBA00008200}. 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; AY331971; AAR86929.1; -; Genomic_DNA. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:TreeGrafter. 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 GO; GO:0015990; P:electron transport coupled proton transport; IEA:TreeGrafter. 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 NCBIfam; TIGR01974; NDH_I_L; 1. DR PANTHER; PTHR42829; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR PANTHER; PTHR42829:SF2; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5; 1. DR Pfam; PF00361; Proton_antipo_M; 1. DR Pfam; PF00662; Proton_antipo_N; 1. DR PRINTS; PR01434; NADHDHGNASE5. DR PRINTS; PR01435; NPOXDRDTASE5. PE 3: Inferred from homology; KW Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:AAR86929.1}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW NAD {ECO:0000256|ARBA:ARBA00023027}; NADP {ECO:0000256|ARBA:ARBA00022857}; KW Plastid {ECO:0000313|EMBL:AAR86929.1}; KW Plastoquinone {ECO:0000256|ARBA:ARBA00022957}; KW Quinone {ECO:0000256|ARBA:ARBA00022719}; KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 20..42 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 69..91 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 103..122 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 129..149 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 203..221 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 241..263 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 275..293 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 309..329 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 336..355 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 375..397 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 57..107 FT /note="NADH-Ubiquinone oxidoreductase (complex I) chain 5 FT N-terminal" FT /evidence="ECO:0000259|Pfam:PF00662" FT DOMAIN 123..411 FT /note="NADH:quinone oxidoreductase/Mrp antiporter membrane FT subunit" FT /evidence="ECO:0000259|Pfam:PF00361" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAR86929.1" FT NON_TER 415 FT /evidence="ECO:0000313|EMBL:AAR86929.1" SQ SEQUENCE 415 AA; 46550 MW; 0BE1512C4218CA9E CRC64; PLXIGVGLLL FPRATKNIRR IWAFLSVLLL SIVMIMAIDL SIQQVNRSFI YQYIWSWVIN NDFSIELGYL IDPLTSIMLI LISSIGIMVL IYSDNYLSHD QGYLRFFTYM SFFSTSMLGL VISSNLIQIY FFWELIGMCS YLLIGFWFTR PVAXNACQKA FVTNRVGDFG FLLGXLSFYX IIGSFEFQDL FEISKNLIYN NEINLLFLIF CVPLLFIGAA AKSAQFPLHV WLPDAMEGPT PISALIHAAT MVAAGIFLVA RLLPLFITIP YIKNSISFIA IITLFLGATL ALAEKDIKRS LAYSTMSQLG YIMLAISMGS YRTGLFHLIT HAYSKALLFL ASGSVIHSME TIVGYSPDKS QNLVLMGGLR KHIPITKIAF LLGTLSLCGI PPLACFWSKD EIINDSWLYS PXXXT //