NU5C_MARPO
ID NU5C_MARPO Reviewed; 692 AA.
AC P06264;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 94.
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; Synonyms=ndh5;
OS Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX DOI=10.1038/322572a0;
RA Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT "Chloroplast gene organization deduced from complete sequence of liverwort
RT Marchantia polymorpha chloroplast DNA.";
RL Nature 322:572-574(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3199437; DOI=10.1016/0022-2836(88)90004-6;
RA Kohchi T., Shirai H., Fukuzawa H., Sano T., Komano T., Umesono K.,
RA Inokuchi H., Ozeki H., Ohyama K.;
RT "Structure and organization of Marchantia polymorpha chloroplast genome.
RT IV. Inverted repeat and small single copy regions.";
RL J. Mol. Biol. 203:353-372(1988).
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; X04465; CAA28129.1; -; Genomic_DNA.
DR PIR; A00453; DELVN5.
DR RefSeq; NP_039343.1; NC_001319.1.
DR AlphaFoldDB; P06264; -.
DR SMR; P06264; -.
DR GeneID; 2702575; -.
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..692
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000118193"
FT TRANSMEM 9..29
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 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
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 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..691
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 692 AA; 79279 MW; 8A1959AD4251DE6B CRC64;
MELIFQNVWF VPLFPFLASI LLGIGLFFFP NSIKKFRRLS SFISIMFLNI AMLLSFHFFW
QQITGSPIHR YLWSWVLYKN FVLEIGYLLD PLTSIMLVLV TTVAVMVMIY SDSYMFYDEG
YIKFFCYLSL FTASMLGLVL SPNLIQVYIF WELVGMCSYL LIGFWFTRPS AANACQKAFV
TNRIGDFGLL LGILGFYWIT GSFDFQQLSK RFFELLSYNQ INLVFATLCA LFLFLGPVAK
SAQFPLHIWL PDAMEGPTPI SALIHAATMV AAGIFLVARM FPLFQMLPFV MSIISWTGAI
TALLGATIAL AQKDLKKGLA YSTMSQLGYM MLALGIGSYK AGLFHLITHA YSKALLFLGS
GSVIHSMEPI VGYHPNKSQN MIFMGGLRQY MPITAITFLF GTLSLCGIPP FACFWSKDEI
LVNSWLHFPI LGSIAFFTAG LTAFYMFRIY FLTFEGDFRG HFFDDVKKLS SISIWGSLEF
NKEQFKLDKK STLYPKEANN IMLFPLIILT IPTVFIGFIG ILFDENKMNV DSLSYWLTLS
INSFNYSNSE KFLEFLFNAI PSVSIAFFGI LIAFYLYGPN FSFLKKEKKK LQLKSEIDIV
LKSFSNFIYN WSYYRAYIDG FYSSFFIKGL RFLIKIVSFI DRWIIDGIIN GIGIFSFFGG
ESLKYIEGGR ISSYLFFIIF CMFLFFLYSY II
