NU2C2_IPOPU
ID NU2C2_IPOPU Reviewed; 508 AA.
AC P0CC77; A7Y3J8;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 26.
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};
OS Ipomoea purpurea (Common morning glory) (Pharbitis purpurea).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Ipomoeeae; Ipomoea.
OX NCBI_TaxID=4121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17956636; DOI=10.1186/1471-2229-7-57;
RA McNeal J.R., Kuehl J.V., Boore J.L., dePamphilis C.W.;
RT "Complete plastid genome sequences suggest strong selection for retention
RT of photosynthetic genes in the parasitic plant genus Cuscuta.";
RL BMC Plant Biol. 7:57-57(2007).
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 -!- SIMILARITY: Belongs to the complex I subunit 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_00445}.
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DR EMBL; EU118126; ABV02413.1; -; Genomic_DNA.
DR RefSeq; YP_001468352.1; NC_009808.1.
DR RefSeq; YP_001468372.1; NC_009808.1.
DR AlphaFoldDB; P0CC77; -.
DR SMR; P0CC77; -.
DR GeneID; 5601271; -.
DR GeneID; 5601303; -.
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 3: Inferred from homology;
KW Chloroplast; Membrane; NAD; NADP; Plastid; Plastoquinone; Quinone;
KW Thylakoid; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="NAD(P)H-quinone oxidoreductase subunit 2 B,
FT chloroplastic"
FT /id="PRO_0000391276"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
FT TRANSMEM 59..79
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 227..247
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 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00445"
SQ SEQUENCE 508 AA; 56426 MW; 072E96F9FCB37068 CRC64;
MSWHVQNENF ILDSTRIFMK AFHLLLFDGS LIFPECILIF GLILLLMIDS TSDQKERPWL
YFISSTSLVM SITALLFRWR EEPMISFSGN FQTNNFNEIF QFLILLCSTL CIPLSVEYIE
CTEMAITEFL LFVLTATLGG MFLCGANDFI TIFVAPECFS LCSYLLSGYT KKDVRSNEAT
MKYLLMGGAS SSILVHGFSW LYGLSGGEIE LQEIVNGLIN TQMYNSPGIS IALIFITVGI
GFKLSPAPSH QWTPDVYEGS PTPVVAFLSV TSKVAASASA TRIFDIPFYF SSNEWHLLLE
ILAILSMILG NLIAITQTSM KRMLAYSSIG QIGYVIIGII VGDSNDGYAS MITYMLFYIS
MNLGAFACIV LFGLRTGTDN IRDYAGLYTK DPFLALSLAL CLLSLGGLPP LAGFFGKLYL
FWCGWQAGLY FLVFIGLLTS VVSIYYYLKI IKLLMTGRNQ AITPHVRNYR RSPSNNSIEL
SMIVCVIAST IPGISMNPII AIAQDTLF
