NU5C_ZYGCR
ID NU5C_ZYGCR Reviewed; 702 AA.
AC Q32RH9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 57.
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 Zygnema circumcarinatum (Green alga).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Zygnemophyceae; Zygnematophycidae;
OC Zygnematales; Zygnemataceae; Zygnema.
OX NCBI_TaxID=35869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16236178; DOI=10.1186/1741-7007-3-22;
RA Turmel M., Otis C., Lemieux C.;
RT "The complete chloroplast DNA sequences of the charophycean green algae
RT Staurastrum and Zygnema reveal that the chloroplast genome underwent
RT extensive changes during the evolution of the Zygnematales.";
RL BMC Biol. 3:22-22(2005).
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; AY958086; AAX45817.1; -; Genomic_DNA.
DR RefSeq; YP_636547.1; NC_008117.1.
DR AlphaFoldDB; Q32RH9; -.
DR SMR; Q32RH9; -.
DR GeneID; 4108137; -.
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..702
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360975"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
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 224..244
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 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 702 AA; 76590 MW; D640A9E26376A737 CRC64;
MQSINQYVWI IPLLPCLTAV ILGLGLISTK NATKSQRLGS AILSIGALLV TMLLSITVLW
EQVISDSAYR QLVSWIKVDN LFLEIGCLVD PLSAIMLVLV TTVGVLVMIY THGYMSHDQG
YVRFFAYLSL FTASMLGLVL SPNLVQVYAF WELVGMCSYL LVGFWFTRPS AAYACQKAFI
TNRVGDFGLL LGILALYWLT GSLEFDIVAS RAHQLLVENS ANTVLLTVCC VLLFLGPIAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGVYLVARL LPLFQEVPLV MDIVAWTGGI
TAVLGATVAL AQKDLKKGLA YSTMSQLGYM ILALGVGSYQ AGLFHLITHA YSKALLFLGS
GSVIHGIEPV VGYNPNQSQN MTYMGGLRSY MPITGVTFLI GTLSLCGVPP FACFWSKDEI
LADAWHKLPV LGLLAWLTAG LTAFYMFRMY FITFEGTFRG SSLISNKSSK QTLSVNKMDS
VFALSNQTKD NTSLKASKHL DPHESSNAMT IPLIVLTIPT ILIGFIGAPL PNGLTGSSLL
SHWLYLDNTE IVELSTNGWT EFAITALPSV SIGILGAFIA WIVYGPHVDR LKNNPVSIDP
SAEGWTGILL NSIYNWSLRR AYIDEIYDQT FVWATRSSAN ALAWFDQWTI DGIVNVGGLF
TLLGGEGTRY TESGRTSAYI FVLGIGLVFV MIAAVLFNFF HL
