ID   NU5C_PSEMZ              Reviewed;          29 AA.
AC   P85928;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic {ECO:0000250|UniProtKB:P15958};
DE            EC=7.1.1.-;
DE   AltName: Full=NAD(P)H dehydrogenase subunit 5 {ECO:0000250|UniProtKB:P15958};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 5 {ECO:0000250|UniProtKB:P15958};
DE   Flags: Fragment;
OS   Pseudotsuga menziesii (Douglas-fir) (Abies menziesii).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae;
OC   Pseudotsuga.
OX   NCBI_TaxID=3357;
RN   [1] {ECO:0000305}
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18602030; DOI=10.1016/j.jprot.2008.06.004;
RA   Islam M.A., Sturrock R.N., Ekramoddoullah A.K.M.;
RT   "A proteomics approach to identify proteins differentially expressed in
RT   Douglas-fir seedlings infected by Phellinus sulphurascens.";
RL   J. Proteomics 71:425-438(2008).
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|UniProtKB:P15958}.
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:0000305};
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:0000305};
CC   -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC       are encoded in the nucleus. {ECO:0000250|UniProtKB:P15958}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250|UniProtKB:P15958}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P15958}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 5 family. {ECO:0000255}.
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DR   AlphaFoldDB; P85928; -.
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:0048038; F:quinone binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           <1..>29
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT                   chloroplastic"
FT                   /id="PRO_0000397954"
FT   TRANSMEM        <1..15
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P15958, ECO:0000255"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:18602030"
FT   NON_TER         29
FT                   /evidence="ECO:0000303|PubMed:18602030"
SQ   SEQUENCE   29 AA;  3051 MW;  14D7BCDB13E06F19 CRC64;
     SGSIIHSMEA NVGYSPDKSQ NMVLMGGLK