NU5C_CERDE
ID NU5C_CERDE Reviewed; 741 AA.
AC A8SEF0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 41.
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 Ceratophyllum demersum (Rigid hornwort) (Coontail).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ceratophyllales; Ceratophyllaceae;
OC Ceratophyllum.
OX NCBI_TaxID=4428;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18048334; DOI=10.1073/pnas.0708072104;
RA Moore M.J., Bell C.D., Soltis P.S., Soltis D.E.;
RT "Using plastid genome-scale data to resolve enigmatic relationships among
RT basal angiosperms.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19363-19368(2007).
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; EF614270; ABQ81498.1; -; Genomic_DNA.
DR RefSeq; YP_001542494.1; NC_009962.1.
DR AlphaFoldDB; A8SEF0; -.
DR SMR; A8SEF0; -.
DR GeneID; 5729485; -.
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..741
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360918"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
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 280..300
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..626
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 721..741
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 741 AA; 83540 MW; C660FEDE4D8717F3 CRC64;
MEHTYQYAWI IPLLPLTVTM LIGLGLLLFP IATKNLRRMW AVPSVLFLSI GMLLSVELAI
QQINQSSVYK YLWSWTINND FSLEFGYLID PLTSIMSILI TTVGILVLIY SDNYMSHDQG
YLRFFSYLSF FNASMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFARPI AANACQKAFV
TNRVGDFGLL LGILGLYWIT GSFEFRDLFE LCNNLIPNNG VNSLFATLCA FLLFLGAVAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIVIPYI MNLISLIGVI
TLLLGATLAL SQRDIKRSLA YSTMSQLGYI MLAPGIGSYR TALFHLITHA YSKALLFLGS
GSIIHSMEPI VGYSPEKSQN MALMGGLTKY VPITKTTFFW GTLSLCGIPP LACFWSKDEI
LHDSWLYSPI FAIIAYATAG LTAFYMFRMY LLTFDGYLRI HFKKYSGNKK GSFYSISIWG
QKELKPVNSN FLLSTVNNNE KVSFFSTKTS QIDGNVRPLM HSLSIHFSNL SKKDIFTYPH
ESDNTMLLPL LLLGLFTWFV GLIGIPFNQE EEGFDILSKW LIPPINLLHQ NSSSPVDWYE
FITNSILSVS ISVFGIFTAS LLYGSVYSSF KNMELINSVV KISPKRSLLD RIINVIYNWS
CNRGYIDVFY ARSLTMMIRG LAQLTHFFDR RVIDGITNGF GIVSFFVGEG IKYAGGGRIS
SYIFYYSSYV LIFVLIFYFF I
