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NU5C_VITVI
ID   NU5C_VITVI              Reviewed;         749 AA.
AC   Q0ZIX1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic;
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase subunit 5;
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 5;
GN   Name=ndhF;
OS   Vitis vinifera (Grape).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Maxxa;
RX   PubMed=16603088; DOI=10.1186/1471-2148-6-32;
RA   Jansen R.K., Kaittanis C., Lee S.-B., Saski C., Tomkins J., Alverson A.J.,
RA   Daniell H.;
RT   "Phylogenetic analyses of Vitis (Vitaceae) based on complete chloroplast
RT   genome sequences: effects of taxon sampling and phylogenetic methods on
RT   resolving relationships among rosids.";
RL   BMC Evol. Biol. 6:32-32(2006).
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 (By similarity).
CC       {ECO:0000250}.
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   -!- 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   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000305}.
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DR   EMBL; DQ424856; ABE47582.1; -; Genomic_DNA.
DR   RefSeq; YP_567125.1; NC_007957.1.
DR   AlphaFoldDB; Q0ZIX1; -.
DR   SMR; Q0ZIX1; -.
DR   STRING; 29760.VIT_00s0246g00150.t01; -.
DR   GeneID; 4025035; -.
DR   KEGG; vvi:4025035; -.
DR   eggNOG; KOG4668; Eukaryota.
DR   InParanoid; Q0ZIX1; -.
DR   OrthoDB; 526738at2759; -.
DR   Proteomes; UP000009183; Chloroplast.
DR   ExpressionAtlas; Q0ZIX1; baseline and differential.
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:0003954; F:NADH dehydrogenase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Reference proteome; Thylakoid; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..749
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT                   chloroplastic"
FT                   /id="PRO_0000360974"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        329..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        553..573
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        607..627
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   749 AA;  84820 MW;  158EA56B47E35D41 CRC64;
     MEHTYQYAWI IPFLPLPIPM LLGVGLLLFP TATKNLRRMW SFTSVLLLSI VMTFSVNLSI
     HQINSSSIYQ YVWSWTINND FSLEFGYLID PLTSIMSILI TTVGIMVLIY SDNYMSHDQG
     YLRFFAYMSF FNASMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPI AANACQKAFV
     TNRVGDFGLL LGILGLYWIT GSFEFRDLFE IFNNLIYNYN NGTNFLFVSL CALFLFVGAV
     AKSAQFPLHV WLPDAMEGPT PISALIHAAT MVAAGIFLVA RLFPLFIVIP YIMNLISLIG
     IITILLGATL ALAQKDIKKS LAYSTMSQLG YTMLALGMGS YRAALFHLIT HAYSKALLFL
     GSGSIIHSME AIVGYSPDKS QNMVLMGGLT KHVPITKNTF LLGTLSLCGI PPLACFWSKD
     EILNDSWLYS PIFAIIACLT AGLTAFYMFR IYLLTFEGYF NVHCKNYSGK KSSLFYSISL
     WGKEGQKTIK KKIRLLTLLT TNNNENEKAS FFSKKVYRLD SNVRKMTRPF ITINQFDNKN
     TFLYPQESDN TMLFPLFALA LFTLFVGAIG IPFNQERMDF DILSKWLNPA TNLLHKNLNN
     YGDWYEFVIN AIFSVSISYF GIFLASLLYN PVYSSLQNLD LINSVAKKVP KRIFWDKIIN
     KVYNWSYNRG YIDAFYETSL TKGIRGLAEL THFFDGRVID GITNGVGVTS FFVGESIKYV
     GGGRISSYLF LYLSSVSILL LISYFFLNQ
 
 
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