ID   A0A060CY16_9ASTR        Unreviewed;       510 AA.
AC   A0A060CY16;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-NOV-2024, entry version 38.
DE   RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2, chloroplastic {ECO:0000256|HAMAP-Rule:MF_00445};
DE            EC=7.1.1.- {ECO:0000256|HAMAP-Rule:MF_00445};
DE   AltName: Full=NAD(P)H dehydrogenase, subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
DE   AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 {ECO:0000256|HAMAP-Rule:MF_00445};
GN   Name=ndhB {ECO:0000256|HAMAP-Rule:MF_00445,
GN   ECO:0000313|EMBL:AIB03821.1};
OS   Centaurea diffusa.
OG   Plastid; Chloroplast {ECO:0000313|EMBL:AIB03821.1}.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Centaureinae; Centaurea.
OX   NCBI_TaxID=124929 {ECO:0000313|EMBL:AIB03821.1};
RN   [1] {ECO:0000313|EMBL:AIB03821.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Turner K.G., Grassa C.J.;
RT   "Centaurea diffusa plastid genome.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) that is believed to belong to the
CC       minimal assembly required for catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The immediate
CC       electron acceptor for the enzyme is believed to be ubiquinone.
CC       {ECO:0000256|ARBA:ARBA00003257}.
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:0000256|HAMAP-Rule:MF_00445}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + NADH + (n+1) H(+)(in) = a plastoquinol +
CC         NAD(+) + n H(+)(out); 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:0000256|HAMAP-Rule:MF_00445};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a plastoquinone + NADPH + (n+1) H(+)(in) = a plastoquinol +
CC         NADP(+) + n H(+)(out); 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:0000256|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:0000256|HAMAP-Rule:MF_00445}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Plastid,
CC       chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_00445};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00445}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00445}.
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DR   EMBL; KJ690264; AIB03800.1; -; Genomic_DNA.
DR   EMBL; KJ690264; AIB03821.1; -; Genomic_DNA.
DR   RefSeq; YP_009040845.1; NC_024286.1.
DR   RefSeq; YP_009040866.1; NC_024286.1.
DR   AlphaFoldDB; A0A060CY16; -.
DR   GeneID; 19592143; -.
DR   GeneID; 19592176; -.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
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   NCBIfam; TIGR01770; NDH_I_N; 1.
DR   PANTHER; PTHR22773:SF116; NAD(P)H-QUINONE OXIDOREDUCTASE SUBUNIT 2 A, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR22773; NADH DEHYDROGENASE; 1.
DR   Pfam; PF19530; Ndh2_N; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
PE   3: Inferred from homology;
KW   Chloroplast {ECO:0000256|ARBA:ARBA00022528, ECO:0000313|EMBL:AIB03821.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00445};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00445};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00445};
KW   Plastid {ECO:0000313|EMBL:AIB03821.1};
KW   Plastoquinone {ECO:0000256|ARBA:ARBA00022957, ECO:0000256|HAMAP-
KW   Rule:MF_00445};
KW   Quinone {ECO:0000256|ARBA:ARBA00022719, ECO:0000256|HAMAP-Rule:MF_00445};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078, ECO:0000256|HAMAP-Rule:MF_00445};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_00445};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00445};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00445};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00445}.
FT   TRANSMEM        24..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        126..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        223..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        323..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        348..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        393..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        427..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   TRANSMEM        480..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00445"
FT   DOMAIN          18..117
FT                   /note="NAD(P)H-quinone oxidoreductase subunit 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19530"
FT   DOMAIN          146..442
FT                   /note="NADH:quinone oxidoreductase/Mrp antiporter membrane
FT                   subunit"
FT                   /evidence="ECO:0000259|Pfam:PF00361"
SQ   SEQUENCE   510 AA;  56706 MW;  7D2F395FCE93A3D9 CRC64;
     MIWHVQNENF ILDSTRIFMK AFRLLLFDGS LIFPECILIF GLILLLMIDS TSDQKDIPWL
     YFISSTSLVM SITALLFRWR EEPMISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE
     CTEMAITEFL LFVLTATIGG MFLCGANDLI TIFVAPECFS LCSYLLSGYT KKDVRSNEAT
     MKYLLMGGAS SSILVHGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGI
     GFKLSPAPSH QWTPDVYEGS PTPVVAFLSV TSKVAASASA TRIFDIPFYF SSNEWHLLLE
     ILAILSMILG NLIAITQTSM KRMLAYSSIA QIGYVIIGII VGDSNDGYAS MITYMLFYIS
     MNLGTFACIV LFGLRTGTEN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL
     FWCGWQAGLY FLVLIGLLTS VVSIYYYLKI IKLLMTGRNQ EITPHVRNYR RSPLRSNNSI
     ELSMIVCVIA STIPGISMNP IIAIAQDTLF
//