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NU5C_AVEFA
ID   NU5C_AVEFA              Reviewed;         212 AA.
AC   P92230;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 72.
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;
DE   Flags: Fragment;
GN   Name=ndhF;
OS   Avena fatua (Wild oats).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Aveninae; Avena.
OX   NCBI_TaxID=4499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9299221; DOI=10.1006/mpev.1997.0416;
RA   Catalan P., Kellogg E.A., Olmstead R.G.;
RT   "Phylogeny of Poaceae subfamily Pooideae based on chloroplast ndhF gene
RT   sequences.";
RL   Mol. Phylogenet. Evol. 8:150-166(1997).
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; U71018; AAB39655.1; -; Genomic_DNA.
DR   PIR; T09590; T09590.
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.
DR   InterPro; IPR002128; NADH_UbQ_OxRdtase_chlpt_su5_C.
DR   Pfam; PF01010; Proton_antipo_C; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           <1..>212
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT                   chloroplastic"
FT                   /id="PRO_0000118174"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         212
SQ   SEQUENCE   212 AA;  24152 MW;  8F41A77004B6FAB9 CRC64;
     HFQNYSSTKE GPLYSISLWG KRIPKGVNRG FILSTTKNGV SFFLQNIPKI QGNTTNRIGS
     FSTSXGXKKT FAYPHETXNT MLFPLLILLL FTLFIGXXXI SFDNGGADNG IGGLTILSKW
     LTPSINFTQE SSNSSINSYE FFTNAIYSVS LAIFGLFIAY IFYGSSYSFF QNLDLQNSFY
     KESPFSYFFD KIKKNIYSWS YNRGYIDIFY TR
 
 
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