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NU2C1_TOBAC
ID   NU2C1_TOBAC             Reviewed;         510 AA.
AC   P0CC98; P06256; Q32720;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2 A, 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 A {ECO:0000255|HAMAP-Rule:MF_00445};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 A {ECO:0000255|HAMAP-Rule:MF_00445};
GN   Name=ndhB1 {ECO:0000255|HAMAP-Rule:MF_00445}; Synonyms=ndh2-A;
OS   Nicotiana tabacum (Common tobacco).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Bright Yellow 4;
RX   PubMed=16453699; DOI=10.1002/j.1460-2075.1986.tb04464.x;
RA   Shinozaki K., Ohme M., Tanaka M., Wakasugi T., Hayashida N.,
RA   Matsubayashi T., Zaita N., Chunwongse J., Obokata J.,
RA   Yamaguchi-Shinozaki K., Ohto C., Torazawa K., Meng B.-Y., Sugita M.,
RA   Deno H., Kamogashira T., Yamada K., Kusuda J., Takaiwa F., Kato A.,
RA   Tohdoh N., Shimada H., Sugiura M.;
RT   "The complete nucleotide sequence of the tobacco chloroplast genome: its
RT   gene organization and expression.";
RL   EMBO J. 5:2043-2049(1986).
RN   [2]
RP   SEQUENCE REVISION.
RA   Sugiura M.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RX   PubMed=8541494; DOI=10.1007/bf00041158;
RA   Freyer R., Lopez C., Maier R.M., Martin M., Sabater B., Koessel H.;
RT   "Editing of the chloroplast ndhB encoded transcript shows divergence
RT   between closely related members of the grass family (Poaceae).";
RL   Plant Mol. Biol. 29:679-684(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.
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   -!- RNA EDITING: Modified_positions=50 {ECO:0000269|PubMed:8541494}, 156
CC       {ECO:0000269|PubMed:8541494}, 196 {ECO:0000269|PubMed:8541494}, 204
CC       {ECO:0000269|PubMed:8541494}, 246 {ECO:0000269|PubMed:8541494}, 249
CC       {ECO:0000269|PubMed:8541494}, 277 {ECO:0000269|PubMed:8541494}, 279
CC       {ECO:0000269|PubMed:8541494}, 494 {ECO:0000269|PubMed:8541494};
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR   EMBL; Z00044; CAA77428.1; ALT_SEQ; Genomic_DNA.
DR   PIR; A00420; DENTN2.
DR   RefSeq; NP_054547.1; NC_001879.2.
DR   RefSeq; NP_054570.1; NC_001879.2.
DR   AlphaFoldDB; P0CC98; -.
DR   SMR; P0CC98; -.
DR   GeneID; 800509; -.
DR   GeneID; 800511; -.
DR   KEGG; nta:800509; -.
DR   KEGG; nta:800511; -.
DR   OrthoDB; 1153818at2759; -.
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   2: Evidence at transcript level;
KW   Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW   RNA editing; Thylakoid; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..510
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 2 A,
FT                   chloroplastic"
FT                   /id="PRO_0000117680"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        418..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ   SEQUENCE   510 AA;  56883 MW;  7B6F250FE30302B0 CRC64;
     MIWHVQNENF ILDSTRIFMK AFHLLLFDGS LIFPECILIF GLILLLMIDL TSDQKDIPWL
     YFISSTSLVM SITALLFRWR EEPMISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE
     CTEMAITEFL LFVLTATLGG MFLCGANDLI TIFVALECFS LCSYLLSGYT KKDVRSNEAT
     MKYLLMGGAS SSILVYGFSW LYGLSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGI
     GFKLSLAPFH QWTPDVYEGS PTPVVAFLSV TSKVAALALA TRIFDIPFYF SSNEWHLLLE
     ILAILSMILG NLIAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNDGYAS MITYMLFYIS
     MNLGTFACIV LFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL
     FWCGWQAGLY FLVLIGLLTS VVSIYYYLKI IKLLMTGRNQ EITPHVRNYR RSPLRSNNSI
     ELSMIVCVIA STILGISMNP IIAIAQDSLF
 
 
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