NU5C_NUPAD
ID NU5C_NUPAD Reviewed; 740 AA.
AC A1XG02;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 54.
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 Nuphar advena (Common spatterdock) (Nuphar lutea subsp. advena).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nuphar.
OX NCBI_TaxID=77108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17573971; DOI=10.1186/1471-2164-8-174;
RA Raubeson L.A., Peery R., Chumley T.W., Dziubek C., Fourcade H.M.,
RA Boore J.L., Jansen R.K.;
RT "Comparative chloroplast genomics: analyses including new sequences from
RT the angiosperms Nuphar advena and Ranunculus macranthus.";
RL BMC Genomics 8:174-174(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; DQ354691; ABC60506.2; -; Genomic_DNA.
DR RefSeq; YP_001001581.2; NC_008788.1.
DR AlphaFoldDB; A1XG02; -.
DR SMR; A1XG02; -.
DR GeneID; 4699584; -.
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..740
FT /note="NAD(P)H-quinone oxidoreductase subunit 5,
FT chloroplastic"
FT /id="PRO_0000360955"
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 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 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
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 719..739
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 740 AA; 83134 MW; 259D9A1B9E16917C CRC64;
MERTYQYAWI IPFVPLLVTM LIGLGLLLIP TATKNIRRIW AFPAVLLLSI VMVFSTKLAI
QQINGSSIYE YLWSWSITSD FSLEFGYLID PLTSIMSILI TTVGIMVLIY SDNYMSHDQG
YLRFFAYMSF FNTSMLGLVT SPNLIQIHIF WELVGMCSYL LIGFWFTRPI AANACQKAFV
TNRVGDFGLL LGILGFYLIT GSFEFQDLFE IFNDSIINNN EINSSFATLC AFLLFLGAVA
KSAQFPLHVW LPDAMEGPTP ISALIHAATM VAAGIFLVAR LLPLFIGIPY IMNIISLIGL
ITVLLGATLA LAQRDIKRSL AYSTMSQLGY IMLALGIGSY RAALFHLITH AYSKALLFLG
SGSIIHSMEP IVGYSPAKSQ NMVLMGGLTK YMPITKTTFF LGTLSLCGIP PLACFWSKDE
IINDSWLYSP IFATIACYTA GLTAFYMFRM YLLTFEGHLR SNFKNYSGHT NSSFYSISIW
GQEGSKPVSS NLLLATRNNN DKSSFSSCPF SNTYKIAGYV RNMRSSFSTH FLNKDPYTLL
YPHESDNTML FPLLILAIFT LFVGCIGIRF GQEVMEVDIL SKWLTPSMKL LHQNSTEDWY
KFVTNAFYSV SIAYFGIFIA SVLYGSVYSD RQNLYLINSF AKMGPKMRIR LEQIINVIYN
WSYNRGYIDV YYEKVFIRGI RGLAQLAHSF DRRVIDGVTN GVGVASFFLG EGIKYIGGGR
ISSYLFLYLA CVSIVLLLVK
