NU2C2_ARATH
ID NU2C2_ARATH Reviewed; 512 AA.
AC P0CC33; O47022; Q9T3G4;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=NAD(P)H-quinone oxidoreductase subunit 2 B, 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 B {ECO:0000255|HAMAP-Rule:MF_00445};
DE AltName: Full=NADH-plastoquinone oxidoreductase subunit 2 B {ECO:0000255|HAMAP-Rule:MF_00445};
GN Name=ndhB2 {ECO:0000255|HAMAP-Rule:MF_00445}; Synonyms=ndhB-B;
GN OrderedLocusNames=AtCg01250;
OS Arabidopsis thaliana (Mouse-ear cress).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC STRAIN=cv. Landsberg erecta;
RA del Campo E.M., Albertazzi F., Freyer R., Maier R.M., Sabater B.,
RA Martin M.;
RT "Sequence and transcript editing of ndhB gene of Arabidopsis thaliana L.
RT plastid.";
RL (er) Plant Gene Register PGR98-093(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10574454; DOI=10.1093/dnares/6.5.283;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.;
RT "Complete structure of the chloroplast genome of Arabidopsis thaliana.";
RL DNA Res. 6:283-290(1999).
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|Ref.1}, 156
CC {ECO:0000269|Ref.1}, 196 {ECO:0000269|Ref.1}, 249 {ECO:0000269|Ref.1},
CC 277 {ECO:0000269|Ref.1}, 279 {ECO:0000269|Ref.1}, 419
CC {ECO:0000269|Ref.1}, 494 {ECO:0000269|Ref.1};
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA84447.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP000423; BAA84447.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_051119.2; NC_000932.1.
DR AlphaFoldDB; P0CC33; -.
DR SMR; P0CC33; -.
DR PRIDE; P0CC33; -.
DR GeneID; 4042815; -.
DR KEGG; ath:ArthCp086; -.
DR Araport; ATCG01250; -.
DR HOGENOM; CLU_007100_1_2_1; -.
DR InParanoid; P0CC33; -.
DR OrthoDB; 1153818at2759; -.
DR BioCyc; ARA:ATCG01250-MON; -.
DR PRO; PR:P0CC33; -.
DR Proteomes; UP000006548; Chloroplast.
DR ExpressionAtlas; P0CC33; baseline and differential.
DR Genevisible; P0CC33; AT.
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 Reference proteome; RNA editing; Thylakoid; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..512
FT /note="NAD(P)H-quinone oxidoreductase subunit 2 B,
FT chloroplastic"
FT /id="PRO_0000391254"
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 183..203
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 512 AA; 57153 MW; 1A998961C3556F2A CRC64;
MIWHVQNENF ILDSTRIFMK AFHLLLFDGS FIFPECILIF GLILLLMIDL TSDQKDIPWL
YFISSTSFVM SITALLFRWR EEPMISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE
CTEMAITEFL LFILTATLGG MFLCGANDLI TIFVALECFS LCSYLLSGYT KKDIRSNEAT
MKYLLMGGAS SSILVYGFSW LYGSSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGI
GFKLSLAPFH QWTPDVYEGS PTPVVAFLSV TSKVAALALA TRIFDIPFYF SSNEWHLLLE
ILAILSMIFG NLIAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNGGYAS MITYMLFYIA
MNLGTFACII LFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL
FWCGWQAGLY FLVSIGLLTS VLSIYYYLKI IKLLMTGRNQ EITPHMRNYR ISPLRSNNSI
ELSMIVCVIA STILGISMNP IIAIAQDTLF SF
