NU5C_NEPOL
ID NU5C_NEPOL Reviewed; 648 AA.
AC Q9TKV7;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Nephroselmis olivacea (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX NCBI_TaxID=31312;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-484 / S-N-5-8;
RX PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA Turmel M., Otis C., Lemieux C.;
RT "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT olivacea: insights into the architecture of ancestral chloroplast
RT genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
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; AF137379; AAD54890.1; -; Genomic_DNA.
DR RefSeq; NP_050919.1; NC_000927.1.
DR AlphaFoldDB; Q9TKV7; -.
DR SMR; Q9TKV7; -.
DR GeneID; 801943; -.
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:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
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 Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..648
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360952"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 648 AA; 71389 MW; B2139A68B60C1A2B CRC64;
MEIFHQAIWL IPVLPLSASM LSGIGLLTFR ETTSDLRRLH GALAIGAMAL SFVVSLGVLW
NQLHGIAPVR WIIEWMLTDT FRLEIGYWVD PLTSTMLVVV TSVALLVMIY SDEYMHVDEG
YVRFFVYLSI FTTSMLGLVL SPNLVQVYGF WELVGMCSYL LVGFWFTRPT AAEASQKAFI
TNRVGDFGLL LGILALYWMT GSFEFASIAD RLGDLLIAIP SLRTIACIAC ILVFMGPIAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGVFLVARM FPVFDQLPLV MELIAWTGTL
TAFLGATMAL TQSDIKKGLA YSTMSQLGYM IMALGTGAYS EALFHLTTHA YSKALLFLAA
GSVIHGMEPV VGFSPMQNQN MHRMGGLRKY MPLTAMTFLL GTCSICGIPP LACFWSKDAI
LAEVFATHPT CWLIAWLTAG MTGFYMFRIY FLTFEGSFRS DLGRAKPKES HLGMVAPLII
LAIPTVAIGS LGTPFAPVWE TFVHAPGQLS SLDEEFDLAE FLEMAGSSVG IGLLGISLSS
LMYRNYAIDA TRISEYFSPL NRLFASKWYI DDLYAQVIVQ GTRTIAQTLL IFDQRIIDGA
VNLTAFGTLS AADTLKYWEN GRVQFYILSI IFGVLFGSWL LTTHLSSL
