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NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic (EC 1.6.5.-) (NAD(P)H dehydrogenase, subunit 2 A) (NADH-plastoquinone oxidoreductase subunit 2 A)

 NU2C1_PHAVU             Reviewed;         492 AA.
P0CD28; A4GGF6;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 1.
15-FEB-2017, entry version 20.
RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2 A, chloroplastic {ECO:0000255|HAMAP-Rule:MF_00445};
EC=1.6.5.- {ECO:0000255|HAMAP-Rule:MF_00445};
AltName: Full=NAD(P)H dehydrogenase, subunit 2 A {ECO:0000255|HAMAP-Rule:MF_00445};
AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 A {ECO:0000255|HAMAP-Rule:MF_00445};
Name=ndhB1 {ECO:0000255|HAMAP-Rule:MF_00445};
Phaseolus vulgaris (Kidney bean) (French bean).
Plastid; Chloroplast.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Phaseolus.
NCBI_TaxID=3885;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Negro Jamapa;
PubMed=17623083; DOI=10.1186/1471-2164-8-228;
Guo X., Castillo-Ramirez S., Gonzalez V., Bustos P.,
Fernandez-Vazquez J.L., Santamaria R.I., Arellano J., Cevallos M.A.,
Davila G.;
"Rapid evolutionary change of common bean (Phaseolus vulgaris L)
plastome, and the genomic diversification of legume chloroplasts.";
BMC Genomics 8:228-228(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Moore M.J., Triplett E.W., Broughton W.J., Soltis P.S., Soltis D.E.;
"Complete nucleotide sequence of the plastid genome of the common
bean, Phaseolus vulgaris.";
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via
FMN and iron-sulfur (Fe-S) centers, to quinones in the
photosynthetic chain and possibly in a chloroplast respiratory
chain. The immediate electron acceptor for the enzyme in this
species is believed to be plastoquinone. Couples the redox
reaction to proton translocation, and thus conserves the redox
energy in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_00445}.
-!- CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) +
plastoquinol. {ECO:0000255|HAMAP-Rule:MF_00445}.
-!- SUBUNIT: NDH is composed of at least 16 different subunits, 5 of
which are encoded in the nucleus. {ECO:0000255|HAMAP-
Rule:MF_00445}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_00445}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_00445}.
-!- SIMILARITY: Belongs to the complex I subunit 2 family.
{ECO:0000255|HAMAP-Rule:MF_00445}.
-!- CAUTION: This protein is smaller than usual in this organism, and
may not be functional. {ECO:0000305}.
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EMBL; DQ886273; ABH88139.1; -; Genomic_DNA.
EMBL; EU196765; ABW22808.1; -; Genomic_DNA.
RefSeq; YP_001122857.1; NC_009259.1.
RefSeq; YP_001165477.1; NC_009259.1.
GeneID; 4961767; -.
GeneID; 5075325; -.
KEGG; pvu:PhvuCp103; -.
KEGG; pvu:PhvuCp75; -.
KO; K05573; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
HAMAP; MF_00445; NDH1_NuoN_1; 1.
InterPro; IPR010096; NADH-Q_OxRdtase_suN/2.
InterPro; IPR001750; ND/Mrp_mem.
Pfam; PF00361; Proton_antipo_M; 1.
TIGRFAMs; TIGR01770; NDH_I_N; 1.
3: Inferred from homology;
Chloroplast; Membrane; NAD; NADP; Oxidoreductase; Plastid;
Plastoquinone; Quinone; Thylakoid; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 492 NAD(P)H-quinone oxidoreductase subunit 2
A, chloroplastic.
/FTId=PRO_0000344279.
TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 39 59 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 81 101 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 106 126 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 131 151 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 165 185 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 209 229 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 277 297 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 305 325 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 336 356 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 377 397 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 400 420 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
TRANSMEM 464 484 Helical. {ECO:0000255|HAMAP-
Rule:MF_00445}.
SEQUENCE 492 AA; 54449 MW; 636D3E6C65DCE7BB CRC64;
MKAFHLLLFD GSLIFPECIL IFGLILLLMI DSTSDQKDIS WFYFISSTSL VMSITALLFR
WREEPMIAFS GNLQTNNFNE IFQFLILLCS TLCIPLSVEY IECTEMAITE FLLFILTTTL
GGMFLCGAND LITIFVALEC FSLCSYLLSG YTKKDVRSNE ATTKYLLMGG ASSSILVHGF
SWLYGSSGGE IELQEIVNGL INTQMYNSPG ILIALLFITV GIGFKLSPAP SHQWTPDVYE
GSPTPVVAFL SVTSKVAASA SATRIFDIPF YFSSNEWHLL LEILAILSMI LGNLIAITQT
SMKRMLAYSS IGQIGYVIIG IIVGDSNGGY ASMITYMLFY ISMNLGTFAC IVSFGLRTGT
DNIRDYAGLY TKDPYLALSL ALCLLSLGGL PPLAGFFGKL HLFWCGWQAG LYFLVSIGLL
TSVVSIYYYL KIIKLLMTGR NQEITPHVRN YRRSPFRSNN SIEFSMIVCV IASTIPGISM
NPIIEIAQDT LF


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