NU5C_CARCG
ID NU5C_CARCG Reviewed; 743 AA.
AC Q9TL56;
DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 72.
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 Carpenteria californica (Tree anemone).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Cornales; Hydrangeaceae; Carpenteria.
OX NCBI_TaxID=23101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10877943; DOI=10.1006/mpev.1999.0769;
RA Olmstead R.G., Kim K.-J., Jansen R.K., Wagstaff S.J.;
RT "The phylogeny of the asteridae sensu lato based on chloroplast ndhF gene
RT sequences.";
RL Mol. Phylogenet. Evol. 16:96-112(2000).
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; AF130217; AAF08173.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9TL56; -.
DR SMR; Q9TL56; -.
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..743
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000118178"
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 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 280..300
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 607..627
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 743 AA; 83781 MW; 3D25E310D8EE2DC6 CRC64;
MEHTYQYAWI IPFVPLPVPM LIGVGLLLFP TATKNLRRVW AFHSVLLLSI VMIFSIDLSI
QQINSSSIYQ YVWSWVINND FSLELGYLID PLTSIMLILI TTVGIMVLIY SDSYMSHDQG
YLRFFAYMSF FSTSMLGLVT SSNLIQIYIF WELVGMCSYL LIGFWFTRPL AANACQKAFV
TNRIGDLGLL LGILGFYWIT GSFEFRDLFQ IVTNLIYNNE VNLVFLTICA VLLFAGAVAK
SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGIFLVARL LPLFIVIPYI LNLISFIGII
TLLLGATLAL AQKDIKRSLA YSTMSQLGYM MLALGMGSYR SALFHLITHA YPKALLFLGS
GSVIHSMETV VGYSPDKSQN MVLMGGLTKH VPITKTAFFL GTLSLCGIPP LACFWSKDEI
LNDSWLYSPI FAIIACSTAG LTAFYMFRIY LLTFEGHLNV HFQNYSGKKN ISFYSISLWG
KGGLKTVNKN FCLLTLLTTN NESASFFSNK TYRIDENIRK MTRPFMTITH FGNKNTYSYP
YESDNTMLLP LLVLVLFTLF VGAIGIPFNQ EGMDLDILSK WLSPSINLLH QDLNNSMDWY
EFVKDAIFSV SIAYFGIVIA SFLYKPVYSS LQNLDLINSF VKTGPNRIFW DKIINVIYDW
SYNRGYIDAF YATSLTGGIR GLAELTNFFD RRVIDGITNG VGVMSFFVGE GIRYLGGGRI
SSYLFLYLSY VSIFLLIYYF LNL
