NU2C_PHYPA
ID NU2C_PHYPA Reviewed; 501 AA.
AC Q6YXR9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00445};
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NAD(P)H dehydrogenase, subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=ndhB {ECO:0000255|HAMAP-Rule:MF_00445};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004;
RX PubMed=12954768; DOI=10.1093/nar/gkg726;
RA Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT evidence for the loss and relocation of rpoA from the chloroplast to the
RT nucleus.";
RL Nucleic Acids Res. 31:5324-5331(2003).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00445};
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00445};
CC -!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which
CC are encoded in the nucleus. {ECO:0000255|HAMAP-Rule:MF_00445}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_00445}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; AP005672; BAC85015.1; -; Genomic_DNA.
DR RefSeq; NP_904166.1; NC_005087.1.
DR AlphaFoldDB; Q6YXR9; -.
DR SMR; Q6YXR9; -.
DR PRIDE; Q6YXR9; -.
DR GeneID; 2546809; -.
DR KEGG; ppp:2546809; -.
DR InParanoid; Q6YXR9; -.
DR OrthoDB; 1153818at2759; -.
DR Proteomes; UP000006727; Chloroplast.
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 GO; GO:0019684; P:photosynthesis, light reaction; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00445; NDH1_NuoN_1; 1.
DR InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
DR InterPro; IPR001750; ND/Mrp_mem.
DR InterPro; IPR045693; Ndh2_N.
DR Pfam; PF19530; Ndh2_N; 1.
DR Pfam; PF00361; Proton_antipo_M; 1.
DR TIGRFAMs; TIGR01770; NDH_I_N; 1.
PE 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Reference proteome; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..501
FT /note="NAD(P)H-quinone oxidoreductase subunit 2,
FT chloroplastic"
FT /id="PRO_0000225348"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 501 AA; 55915 MW; D3D157805C6B142A CRC64;
MELELDLSFF YKTTILPECV LIFCLISILI LDLILKIKDK NVFFFISLVS LLLSIFILIF
QLKEEPVISF LGNFQADNFN KIFRIFIALC SILCIPLSID FIKCTKLAIT EFLIFLLTAT
IGGMFLCGAN DLITIFVSLE CLSLCSYLLS GYTKKDVRSN EAVMKYLLIG GTSSSILAYG
FSWLYGLSGG EFQLQKIADG LVSTEMYNSF GSLLALVFII VGIGFKLSLV PFHQWTPDVY
EGSPTPVVAF LSVASKIAGL ALLVRLFNIV FPFLPNQWHS LLEISAICSM ILGNLVAITQ
TSMKRMLAYS SISQIGYLMI GLVTGNFDGY TSMIVYLLFY IFMNLGTFAC IILFGLRTGT
DNIRDYSGLI LKDPLLTFSL ALCLLSLGGI PPLSGFFGKL YLFWCAWKTG LYFLVFIGLF
TSVISIYYYL KIIKLLITTE NKEVTSYVQS YTVSSFSLLS KNSIEVSIII CVIASIFLGI
FMNPIINILQ INLHLNTFTN I
