NU5C_DAMDI
ID NU5C_DAMDI Reviewed; 744 AA.
AC Q32126;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 78.
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 Dampiera diversifolia (Blue dampiera).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Goodeniaceae; core Goodeniaceae;
OC LAD clade; Dampiera.
OX NCBI_TaxID=41565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7479788; DOI=10.1073/pnas.92.22.10379;
RA Kim K.-J., Jansen R.K.;
RT "ndhF sequence evolution and the major clades in the sunflower family.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10379-10383(1995).
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; L39386; AAC37742.1; -; Genomic_DNA.
DR PIR; T13043; T13043.
DR AlphaFoldDB; Q32126; -.
DR SMR; Q32126; -.
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..744
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000118181"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
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 290..312
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 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 744 AA; 84171 MW; 1A92DB816F322A5F CRC64;
MEQTYQYGWI IPFLPLPVPM LIGLGLLLFP TATKSLRRMW AFQSVLLLSI VMIFSMNLSI
QQINSSSVYQ YVWSWIINND FSLEFGYLID PLTSIMSILI TTVGIMVLSY SDNYMSHDHG
YLRFFAYMSF FSTSMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPL AANACQKAFV
TNRVGDFGLL LGILGIYWIT GSFEFRDLFQ IFNSLISNNE VNFLFVTFCA LLLFTGAIAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLIARL LPLFIVIPHI MNFISLIGII
TLFLGATLAL AQKDIKRGLA YSTMSQLGYM VLALGMGSYR SALFHLITHA YSKALLFLGS
GSVIHSMETL VGYSPQKSQN MGLMGGLTKH VPITKTAFLL GTLSLCGIPP LACFWSKDEI
LNDSWLYSPI FAIIAWSTAG LTAFYMCRIY LLSFEGHLNA HFQNYSGKKN TPLSSIYIWG
KEASEISKKN FCELILLKMK RTECPSFFSK KGCKLDEKVR NMIQPFLSIS YLGNNKTYFY
PYESDNTMLF PILILGLFTL FIGFLGIPSN HEGVDLDILS KWLTPSINLL HQNTNTSLDL
YEFSKDSIFS VSIASLGIFI AFFLYKPVYS SFQILDLINL FVKRGPKRIF SDKIKKGIYD
WSSNRAYIDP FYTTFLTVGM RKLAELTHFF DRRIIDGIPN GVGLMIFFVA EGIKSLGGGR
ISSYLFFYLS HLSFFLLIYY FLNF
