NU2C_ADICA
ID NU2C_ADICA Reviewed; 498 AA.
AC Q85FP1;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 67.
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 Adiantum capillus-veneris (Maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT "Complete nucleotide sequence of the chloroplast genome from a
RT leptosporangiate fern, Adiantum capillus-veneris L.";
RL DNA Res. 10:59-65(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC TISSUE=Frond;
RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA Wolf P.G., Rowe C.A., Hasebe M.;
RT "High levels of RNA editing in a vascular plant chloroplast genome:
RT analysis of transcripts from the fern Adiantum capillus-veneris.";
RL Gene 339:89-97(2004).
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=1 {ECO:0000269|PubMed:15363849}, 31
CC {ECO:0000269|PubMed:15363849}, 94 {ECO:0000269|PubMed:15363849}, 166
CC {ECO:0000269|PubMed:15363849}, 170 {ECO:0000269|PubMed:15363849}, 178
CC {ECO:0000269|PubMed:15363849}, 185 {ECO:0000269|PubMed:15363849}, 189
CC {ECO:0000269|PubMed:15363849}, 260 {ECO:0000269|PubMed:15363849}, 262
CC {ECO:0000269|PubMed:15363849}, 309 {ECO:0000269|PubMed:15363849}, 310
CC {ECO:0000269|PubMed:15363849}, 351 {ECO:0000269|PubMed:15363849}, 381
CC {ECO:0000269|PubMed:15363849}, 384 {ECO:0000269|PubMed:15363849}, 385
CC {ECO:0000269|PubMed:15363849}, 386 {ECO:0000269|PubMed:15363849}, 394
CC {ECO:0000269|PubMed:15363849}, 415 {ECO:0000269|PubMed:15363849}, 417
CC {ECO:0000269|PubMed:15363849}, 436 {ECO:0000269|PubMed:15363849}, 475
CC {ECO:0000269|PubMed:15363849}; Note=The initiatior methionine is
CC created by RNA editing.;
CC -!- MISCELLANEOUS: A second copy of the second exon exists; it is not known
CC if it is transcribed or not.
CC -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; AY178864; AAP29370.2; -; Genomic_DNA.
DR RefSeq; NP_848038.2; NC_004766.1.
DR AlphaFoldDB; Q85FP1; -.
DR SMR; Q85FP1; -.
DR GeneID; 807345; -.
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..498
FT /note="NAD(P)H-quinone oxidoreductase subunit 2,
FT chloroplastic"
FT /id="PRO_0000117650"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 211..231
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 306..326
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 498 AA; 54810 MW; 0B387F9148FE498F CRC64;
MNDINLFLAK LTYTSAKLTI LPEIILILGL VAVVVIDLLS KGKNTFLLYK ISMVTLLASA
VILLWQWGFF TAYERSHARD FGNIFRFFLL ICSLLSISSS VDYILCSKMS LAEFLLFKLA
AGLGGMVLSC ANDLVTIYVS LEFLALSSCF LSGYTKRDMR SNEATMKFLL MSGASSSLLL
YGFSLLYGLS GGQLQLDKIV DGIIFNRYGS IIYLSAAFTT AGTAFKLSLF PFHQWTPDVY
EGSPTPVVAF FSVTSKVAAL ALFTRLFGLI FPYFSNEWHV AVGLLATFSM ILGNLIAVTQ
RSVKRMLAFS SISQIGYIMI GVLSADSGNG YASMITYTFI YILMNLGTFA CITLFGLRTG
TDNIRDYAGL YMKDPVLTFS LVLCLLSLGG MPPLSGFFGK LYLFWHGWKA GLYSLVLVAL
VTSVISIYYY LKIIKLMFTG KSGRSDTPLN SRQNSLVSLS ISISKNSLEI AMIICALAST
LSGIFIDPII EITRNTFF
